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<span>Types</span> </div> </a> <button aria-controls="toc-Types-sublist" class="cdx-button cdx-button--weight-quiet cdx-button--icon-only vector-toc-toggle"> <span class="vector-icon mw-ui-icon-wikimedia-expand"></span> <span>Toggle Types subsection</span> </button> <ul id="toc-Types-sublist" class="vector-toc-list"> <li id="toc-Glucose_transporter_(GLUTs)" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Glucose_transporter_(GLUTs)"> <div class="vector-toc-text"> <span class="vector-toc-numb">2.1</span> <span>Glucose transporter (GLUTs)</span> </div> </a> <ul id="toc-Glucose_transporter_(GLUTs)-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Mitochondrial_Ca2+_uniporter_(MCU)" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Mitochondrial_Ca2+_uniporter_(MCU)"> <div class="vector-toc-text"> <span class="vector-toc-numb">2.2</span> <span>Mitochondrial <span>Ca<sup>2+</sup></span> uniporter (MCU)</span> </div> </a> <ul id="toc-Mitochondrial_Ca2+_uniporter_(MCU)-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Large_neutral_amino_acid_transporter_(LAT1)" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Large_neutral_amino_acid_transporter_(LAT1)"> <div class="vector-toc-text"> <span class="vector-toc-numb">2.3</span> <span>Large neutral amino acid transporter (LAT1)</span> </div> </a> <ul id="toc-Large_neutral_amino_acid_transporter_(LAT1)-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Equilibrative_nucleoside_transporters_(ENTs)" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Equilibrative_nucleoside_transporters_(ENTs)"> <div class="vector-toc-text"> <span class="vector-toc-numb">2.4</span> <span>Equilibrative nucleoside transporters (ENTs)</span> </div> </a> <ul id="toc-Equilibrative_nucleoside_transporters_(ENTs)-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-Mechanism" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#Mechanism"> <div class="vector-toc-text"> <span class="vector-toc-numb">3</span> <span>Mechanism</span> </div> </a> <ul id="toc-Mechanism-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Physiological_processes" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#Physiological_processes"> <div class="vector-toc-text"> <span class="vector-toc-numb">4</span> <span>Physiological processes</span> </div> </a> <ul id="toc-Physiological_processes-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Mutations" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#Mutations"> <div class="vector-toc-text"> <span class="vector-toc-numb">5</span> <span>Mutations</span> </div> </a> <ul id="toc-Mutations-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-See_also" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#See_also"> <div class="vector-toc-text"> <span class="vector-toc-numb">6</span> <span>See also</span> </div> </a> <ul id="toc-See_also-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-References" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#References"> <div class="vector-toc-text"> <span class="vector-toc-numb">7</span> <span>References</span> </div> </a> <ul id="toc-References-sublist" class="vector-toc-list"> </ul> </li> </ul> </div> </div> </nav> </div> </div> <div class="mw-content-container"> <main id="content" class="mw-body"> <header class="mw-body-header vector-page-titlebar"> <nav aria-label="Contents" class="vector-toc-landmark"> <div id="vector-page-titlebar-toc" class="vector-dropdown vector-page-titlebar-toc vector-button-flush-left" > <input type="checkbox" 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href="mw-data:TemplateStyles:r1251242444"><table class="box-Page_numbers_needed plainlinks metadata ambox ambox-style" role="presentation"><tbody><tr><td class="mbox-image"><div class="mbox-image-div"><span typeof="mw:File"><span><img alt="" src="//upload.wikimedia.org/wikipedia/commons/thumb/3/3b/Text_document_with_page_number_icon.svg/40px-Text_document_with_page_number_icon.svg.png" decoding="async" width="40" height="40" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/3/3b/Text_document_with_page_number_icon.svg/60px-Text_document_with_page_number_icon.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/3/3b/Text_document_with_page_number_icon.svg/80px-Text_document_with_page_number_icon.svg.png 2x" data-file-width="48" data-file-height="48" /></span></span></div></td><td class="mbox-text"><div class="mbox-text-span">This article cites its <a href="/wiki/Wikipedia:Citing_sources" title="Wikipedia:Citing sources">sources</a> but <b>does not provide <a href="/wiki/Wikipedia:CITEHOW" class="mw-redirect" title="Wikipedia:CITEHOW">page references</a></b>.<span class="hide-when-compact"> You can help by providing page numbers for existing citations.</span> <span class="date-container"><i>(<span class="date">May 2015</span>)</i></span><span class="hide-when-compact"><i> (<small><a href="/wiki/Help:Maintenance_template_removal" title="Help:Maintenance template removal">Learn how and when to remove this message</a></small>)</i></span></div></td></tr></tbody></table> </div> </div><span class="hide-when-compact"><i> (<small><a href="/wiki/Help:Maintenance_template_removal" title="Help:Maintenance template removal">Learn how and when to remove this message</a></small>)</i></span></div></td></tr></tbody></table> <figure class="mw-halign-right" typeof="mw:File/Thumb"><a href="/wiki/File:Porters.PNG" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/6/6c/Porters.PNG/250px-Porters.PNG" decoding="async" width="250" height="145" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/6/6c/Porters.PNG/375px-Porters.PNG 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/6/6c/Porters.PNG/500px-Porters.PNG 2x" data-file-width="550" data-file-height="318" /></a><figcaption>Comparison of transport proteins</figcaption></figure> <p><b>Uniporters,</b> also known as <b>solute carriers</b> or <b>facilitated transporters</b>, are a type of <a href="/wiki/Membrane_transport_protein" title="Membrane transport protein">membrane transport protein</a> that passively transports solutes (small molecules, ions, or other substances) across a cell membrane.<sup id="cite_ref-Zhang_XC_1-0" class="reference"><a href="#cite_note-Zhang_XC-1"><span class="cite-bracket">[</span>1<span class="cite-bracket">]</span></a></sup> It uses <a href="/wiki/Facilitated_diffusion" title="Facilitated diffusion">facilitated diffusion</a> for the movement of solutes down their concentration gradient from an area of high concentration to an area of low concentration.<sup id="cite_ref-Alberts_2-0" class="reference"><a href="#cite_note-Alberts-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup> Unlike <a href="/wiki/Active_transport" title="Active transport">active transport</a>, it does not require energy in the form of <a href="/wiki/Adenosine_triphosphate" title="Adenosine triphosphate">ATP</a> to function. Uniporters are specialized to carry one specific ion or molecule and can be categorized as either channels or carriers.<sup id="cite_ref-3" class="reference"><a href="#cite_note-3"><span class="cite-bracket">[</span>3<span class="cite-bracket">]</span></a></sup> Facilitated diffusion may occur through three mechanisms: uniport, symport, or antiport. The difference between each mechanism depends on the direction of transport, in which uniport is the only transport not coupled to the transport of another solute.<sup id="cite_ref-4" class="reference"><a href="#cite_note-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup> </p><p>Uniporter carrier proteins work by binding to one <a href="/wiki/Molecule" title="Molecule">molecule</a> or <a href="/wiki/Substrate_(biochemistry)" class="mw-redirect" title="Substrate (biochemistry)">substrate</a> at a time. Uniporter channels open in response to a stimulus and allow the free flow of specific molecules.<sup id="cite_ref-Alberts_2-1" class="reference"><a href="#cite_note-Alberts-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup> </p><p>There are several ways in which the opening of uniporter channels may be regulated: </p> <ol><li><a href="/wiki/Voltage" title="Voltage">Voltage</a> – Regulated by the difference in voltage across the membrane</li> <li><a href="/wiki/Stress_(physics)" class="mw-redirect" title="Stress (physics)">Stress</a> – Regulated by physical <a href="/wiki/Pressure" title="Pressure">pressure</a> on the transporter (as in the <a href="/wiki/Cochlea" title="Cochlea">cochlea</a> of the <a href="/wiki/Ear" title="Ear">ear</a>)</li> <li><a href="/wiki/Ligand" title="Ligand">Ligand</a> – Regulated by the binding of a ligand to either the intracellular or extracellular side of the <a href="/wiki/Cell_(biology)" title="Cell (biology)">cell</a></li></ol> <p>Uniporters are found in <a href="/wiki/Mitochondrion" title="Mitochondrion">mitochondria</a>, <a href="/wiki/Cell_membrane" title="Cell membrane">plasma membranes</a> and <a href="/wiki/Neuron" title="Neuron">neurons</a>.The uniporter in the mitochondria is responsible for <a href="/wiki/Calcium" title="Calcium">calcium</a> uptake.<sup id="cite_ref-Zhang_XC_1-1" class="reference"><a href="#cite_note-Zhang_XC-1"><span class="cite-bracket">[</span>1<span class="cite-bracket">]</span></a></sup> The calcium channels are used for <a href="/wiki/Cell_signaling" title="Cell signaling">cell signaling</a> and triggering <a href="/wiki/Apoptosis" title="Apoptosis">apoptosis</a>. The calcium uniporter transports calcium across the inner mitochondrial membrane and is activated when calcium rises above a certain concentration.<sup id="cite_ref-5" class="reference"><a href="#cite_note-5"><span class="cite-bracket">[</span>5<span class="cite-bracket">]</span></a></sup> The <a href="/wiki/CD98" title="CD98">amino acid transporters</a> function in transporting neutral <a href="/wiki/Amino_acid" title="Amino acid">amino acids</a> for <a href="/wiki/Neurotransmitter" title="Neurotransmitter">neurotransmitter</a> production in brain cells.<sup id="cite_ref-Häfliger_P_6-0" class="reference"><a href="#cite_note-Häfliger_P-6"><span class="cite-bracket">[</span>6<span class="cite-bracket">]</span></a></sup> <a href="/wiki/Voltage-gated_potassium_channel" title="Voltage-gated potassium channel">Voltage-gated potassium channels</a> are also uniporters found in neurons and are essential for <a href="/wiki/Action_potential" title="Action potential">action potentials</a>.<sup id="cite_ref-7" class="reference"><a href="#cite_note-7"><span class="cite-bracket">[</span>7<span class="cite-bracket">]</span></a></sup> This channel is activated by a voltage gradient created by <a href="/wiki/Na%2B/K%2B-ATPase" class="mw-redirect" title="Na+/K+-ATPase">sodium-potassium pumps</a>. When the membrane reaches a certain voltage, the channels open, which <a href="/wiki/Depolarization" title="Depolarization">depolarizes</a> the membrane, leading to an <a href="/wiki/Action_potential" title="Action potential">action potential</a> being sent down the membrane.<sup id="cite_ref-8" class="reference"><a href="#cite_note-8"><span class="cite-bracket">[</span>8<span class="cite-bracket">]</span></a></sup> <a href="/wiki/Glucose_transporter" title="Glucose transporter">Glucose transporters</a> are found in the plasma membrane and play a role in transporting <a href="/wiki/Glucose" title="Glucose">glucose</a>. They help to bring glucose from the blood or extracellular space into cells usually to be utilized for metabolic processes in generating energy.<sup id="cite_ref-Olson_AL_9-0" class="reference"><a href="#cite_note-Olson_AL-9"><span class="cite-bracket">[</span>9<span class="cite-bracket">]</span></a></sup> </p><p>Uniporters are essential for certain physiological processes in cells, such as nutrient uptake, waste removal, and maintenance of ionic balance. </p> <meta property="mw:PageProp/toc" /> <div class="mw-heading mw-heading2"><h2 id="Discovery">Discovery</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Uniporter&action=edit&section=1" title="Edit section: Discovery"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:Scheme_facilitated_diffusion_in_cell_membrane-en.svg" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/9/91/Scheme_facilitated_diffusion_in_cell_membrane-en.svg/220px-Scheme_facilitated_diffusion_in_cell_membrane-en.svg.png" decoding="async" width="220" height="96" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/9/91/Scheme_facilitated_diffusion_in_cell_membrane-en.svg/330px-Scheme_facilitated_diffusion_in_cell_membrane-en.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/9/91/Scheme_facilitated_diffusion_in_cell_membrane-en.svg/440px-Scheme_facilitated_diffusion_in_cell_membrane-en.svg.png 2x" data-file-width="581" data-file-height="254" /></a><figcaption>Facilitated diffusion using transport proteins</figcaption></figure> <p>Early research in the 19th and 20th centuries on <a href="/wiki/Osmosis" title="Osmosis">osmosis</a> and <a href="/wiki/Diffusion" title="Diffusion">diffusion</a> provided the foundation for understanding the <a href="/wiki/Passive_transport" title="Passive transport">passive movement</a> of molecules across cell membranes.<sup id="cite_ref-10" class="reference"><a href="#cite_note-10"><span class="cite-bracket">[</span>10<span class="cite-bracket">]</span></a></sup> </p><p>In 1855, the physiologist <a href="/wiki/Adolf_Eugen_Fick" title="Adolf Eugen Fick">Adolf Fick</a> was the first to define osmosis and simple diffusion as the tendency for <a href="/wiki/Solution_(chemistry)" title="Solution (chemistry)">solutes</a> to move from a region of higher concentration to a lower concentration, also very well-known as <a href="/wiki/Fick%27s_laws_of_diffusion" title="Fick's laws of diffusion">Fick's Laws of Diffusion</a>.<sup id="cite_ref-Stillwell_W_11-0" class="reference"><a href="#cite_note-Stillwell_W-11"><span class="cite-bracket">[</span>11<span class="cite-bracket">]</span></a></sup> Through the work of <a href="/wiki/Charles_Overton" title="Charles Overton">Charles Overton</a> in the 1890s, the concept that the <a href="/wiki/Biological_membrane" title="Biological membrane">biological membrane</a> is <a href="/wiki/Semipermeable_membrane" title="Semipermeable membrane">semipermeable</a> became important to understanding the regulation of substances in and out of the cells.<sup id="cite_ref-Stillwell_W_11-1" class="reference"><a href="#cite_note-Stillwell_W-11"><span class="cite-bracket">[</span>11<span class="cite-bracket">]</span></a></sup> The discovery of <a href="/wiki/Facilitated_diffusion" title="Facilitated diffusion">facilitated diffusion</a> by Wittenberg and Scholander suggested that <a href="/wiki/Protein" title="Protein">proteins</a> in the cell membrane aid in the transport of molecules.<sup id="cite_ref-12" class="reference"><a href="#cite_note-12"><span class="cite-bracket">[</span>12<span class="cite-bracket">]</span></a></sup> In the 1960s - 1970s, studies on the transport of <a href="/wiki/Glucose" title="Glucose">glucose</a> and other nutrients highlighted the <a href="/wiki/Specificity_(biochemistry)" class="mw-redirect" title="Specificity (biochemistry)">specificity</a> and <a href="/wiki/Selectivity_(biochemistry)" class="mw-redirect" title="Selectivity (biochemistry)">selectivity</a> of <a href="/wiki/Membrane_transport_protein" title="Membrane transport protein">membrane transport proteins</a>.<sup id="cite_ref-13" class="reference"><a href="#cite_note-13"><span class="cite-bracket">[</span>13<span class="cite-bracket">]</span></a></sup> </p><p>Technological advancements in biochemistry helped isolate and characterize these proteins from cell membranes. Genetic studies on <a href="/wiki/Bacteria" title="Bacteria">bacteria</a> and <a href="/wiki/Yeast" title="Yeast">yeast</a> identified genes responsible for encoding transporters. This led to the discovery of <a href="/wiki/SLC2A10" title="SLC2A10">glucose transporters</a> (GLUT proteins), with <a href="/wiki/GLUT1" title="GLUT1">GLUT1</a> being the first to be characterized.<sup id="cite_ref-Thorens_B_14-0" class="reference"><a href="#cite_note-Thorens_B-14"><span class="cite-bracket">[</span>14<span class="cite-bracket">]</span></a></sup> Identification of gene families encoding various transporters, such as <a href="/wiki/Solute_carrier_family" title="Solute carrier family">solute carrier (SLC) families</a>, also advanced knowledge on uniporters and its functions.<sup id="cite_ref-Thorens_B_14-1" class="reference"><a href="#cite_note-Thorens_B-14"><span class="cite-bracket">[</span>14<span class="cite-bracket">]</span></a></sup> </p><p>Newer research is focusing on techniques using <a href="/wiki/Recombinant_DNA" title="Recombinant DNA">recombinant DNA technology</a>, <a href="/wiki/Electrophysiology" title="Electrophysiology">electrophysiology</a> and advanced imaging to understand uniporter functions. These experiments are designed to <a href="/wiki/Cloning_vector" title="Cloning vector">clone</a> and express transporter genes in host cells to further analyze the three-dimensional structure of uniporters, as well as directly observe the movement of ions through proteins in real-time.<sup id="cite_ref-Thorens_B_14-2" class="reference"><a href="#cite_note-Thorens_B-14"><span class="cite-bracket">[</span>14<span class="cite-bracket">]</span></a></sup> The discovery of <a href="/wiki/Mutation" title="Mutation">mutations</a> in uniporters has been linked to diseases such as <a href="/wiki/GLUT1_deficiency_syndrome" class="mw-redirect" title="GLUT1 deficiency syndrome">GLUT1 deficiency syndrome</a>, <a href="/wiki/Cystic_fibrosis" title="Cystic fibrosis">cystic fibrosis</a>, <a href="/wiki/Hartnup_disease" title="Hartnup disease">Hartnup disease</a>, <a href="/wiki/Primary_hyperoxaluria" title="Primary hyperoxaluria">primary hyperoxaluria</a> and <a href="/wiki/Hypokalemic_periodic_paralysis" title="Hypokalemic periodic paralysis">hypokalemic periodic paralysis</a>.<sup id="cite_ref-15" class="reference"><a href="#cite_note-15"><span class="cite-bracket">[</span>15<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="Types">Types</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Uniporter&action=edit&section=2" title="Edit section: Types"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <div class="mw-heading mw-heading3"><h3 id="Glucose_transporter_(GLUTs)"><span id="Glucose_transporter_.28GLUTs.29"></span>Glucose transporter (GLUTs)</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Uniporter&action=edit&section=3" title="Edit section: Glucose transporter (GLUTs)"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The glucose transporter (GLUTs) is a type of uniporter responsible for the <a href="/wiki/Facilitated_diffusion" title="Facilitated diffusion">facilitated diffusion</a> of glucose molecules across cell membranes.<sup id="cite_ref-Olson_AL_9-1" class="reference"><a href="#cite_note-Olson_AL-9"><span class="cite-bracket">[</span>9<span class="cite-bracket">]</span></a></sup><a href="/wiki/Glucose" title="Glucose">Glucose</a> is a vital energy source for most living cells, however, due to its large size, it cannot freely move through the cell membrane.<sup id="cite_ref-Navale_AM_16-0" class="reference"><a href="#cite_note-Navale_AM-16"><span class="cite-bracket">[</span>16<span class="cite-bracket">]</span></a></sup> The glucose transporter is specialized in transporting glucose specifically across the membrane. The GLUT proteins have several types of <a href="/wiki/Protein_isoform" title="Protein isoform">isoforms</a>, each distributed in different <a href="/wiki/Tissue_(biology)" title="Tissue (biology)">tissues</a> and exhibiting different <a href="/wiki/Chemical_kinetics" title="Chemical kinetics">kinetic properties.</a><sup id="cite_ref-Navale_AM_16-1" class="reference"><a href="#cite_note-Navale_AM-16"><span class="cite-bracket">[</span>16<span class="cite-bracket">]</span></a></sup> </p> <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:Glucose-6-phosphatase_system.svg" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/4/4a/Glucose-6-phosphatase_system.svg/220px-Glucose-6-phosphatase_system.svg.png" decoding="async" width="220" height="141" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/4/4a/Glucose-6-phosphatase_system.svg/330px-Glucose-6-phosphatase_system.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/4/4a/Glucose-6-phosphatase_system.svg/440px-Glucose-6-phosphatase_system.svg.png 2x" data-file-width="620" data-file-height="398" /></a><figcaption>Glucose transporter</figcaption></figure> <p>GLUTs are <a href="/wiki/Integral_membrane_protein" title="Integral membrane protein">integral membrane proteins</a> composed of <a href="/wiki/Alpha_helix" title="Alpha helix">12 α-helix membrane spanning regions</a>.<sup id="cite_ref-Navale_AM_16-2" class="reference"><a href="#cite_note-Navale_AM-16"><span class="cite-bracket">[</span>16<span class="cite-bracket">]</span></a></sup> The GLUT proteins are encoded by the <a href="/wiki/SLA2" title="SLA2">SLC2 genes</a> and categorized into three classes based on <a href="/wiki/Protein_primary_structure" title="Protein primary structure">amino acid sequence</a> similarity.<sup id="cite_ref-17" class="reference"><a href="#cite_note-17"><span class="cite-bracket">[</span>17<span class="cite-bracket">]</span></a></sup> Humans have been found to express fourteen GLUT proteins. Class I GLUTs include <a href="/wiki/GLUT1" title="GLUT1">GLUT1</a>, one of the most studied isoforms, and <a href="/wiki/GLUT2" title="GLUT2">GLUT2</a>.<sup id="cite_ref-Navale_AM_16-3" class="reference"><a href="#cite_note-Navale_AM-16"><span class="cite-bracket">[</span>16<span class="cite-bracket">]</span></a></sup> GLUT1 is found in various tissues like the <a href="/wiki/Red_blood_cell" title="Red blood cell">red blood cells</a>, <a href="/wiki/Brain" title="Brain">brain</a>, and <a href="/wiki/Blood%E2%80%93brain_barrier" title="Blood–brain barrier">blood-brain barrier</a> and is responsible for basal <a href="/wiki/Glucose_uptake" title="Glucose uptake">glucose uptake</a>.<sup id="cite_ref-Navale_AM_16-4" class="reference"><a href="#cite_note-Navale_AM-16"><span class="cite-bracket">[</span>16<span class="cite-bracket">]</span></a></sup> GLUT2 is predominantly found in the <a href="/wiki/Liver" title="Liver">liver</a>, <a href="/wiki/Pancreas" title="Pancreas">pancreas</a>, and <a href="/wiki/Small_intestine" title="Small intestine">small intestines</a>.<sup id="cite_ref-Navale_AM_16-5" class="reference"><a href="#cite_note-Navale_AM-16"><span class="cite-bracket">[</span>16<span class="cite-bracket">]</span></a></sup> It plays an important role in insulin secretion from <a href="/wiki/Beta_cell" title="Beta cell">pancreatic beta cells</a>. Class II includes the <a href="/wiki/GLUT3" title="GLUT3">GLUT3</a> and <a href="/wiki/GLUT4" title="GLUT4">GLUT4</a>.<sup id="cite_ref-Navale_AM_16-6" class="reference"><a href="#cite_note-Navale_AM-16"><span class="cite-bracket">[</span>16<span class="cite-bracket">]</span></a></sup> GLUT3, primarily found in the brain, <a href="/wiki/Neuron" title="Neuron">neurons</a> and <a href="/wiki/Placenta" title="Placenta">placenta</a>, has a high <a href="/wiki/Affinity_electrophoresis" title="Affinity electrophoresis">affinity</a> for glucose in facilitating glucose uptake into neurons.<sup id="cite_ref-Navale_AM_16-7" class="reference"><a href="#cite_note-Navale_AM-16"><span class="cite-bracket">[</span>16<span class="cite-bracket">]</span></a></sup> <a href="/wiki/GLUT4" title="GLUT4">GLUT4</a> plays a role in insulin-regulated glucose uptake and is mainly found in insulin-sensitive tissues such as muscle and <a href="/wiki/Adipose_tissue" title="Adipose tissue">adipose tissue</a>.<sup id="cite_ref-Navale_AM_16-8" class="reference"><a href="#cite_note-Navale_AM-16"><span class="cite-bracket">[</span>16<span class="cite-bracket">]</span></a></sup> Class III includes <a href="/wiki/GLUT5" title="GLUT5">GLUT5</a>, found in the <a href="/wiki/Small_intestine" title="Small intestine">small intestine</a>, <a href="/wiki/Kidney" title="Kidney">kidney</a>, <a href="/wiki/Testicle" title="Testicle">testes</a>, and <a href="/wiki/Skeletal_muscle" title="Skeletal muscle">skeletal muscle</a>.<sup id="cite_ref-Navale_AM_16-9" class="reference"><a href="#cite_note-Navale_AM-16"><span class="cite-bracket">[</span>16<span class="cite-bracket">]</span></a></sup> Unlike the other GLUTs, GLUT5 specifically transports <a href="/wiki/Fructose" title="Fructose">fructose</a> rather than glucose.<sup id="cite_ref-Navale_AM_16-10" class="reference"><a href="#cite_note-Navale_AM-16"><span class="cite-bracket">[</span>16<span class="cite-bracket">]</span></a></sup> </p><p>Glucose transporters allow glucose molecules to move down their concentration gradient from areas of high glucose concentration to areas of low concentration. This process often involves bringing glucose from the <a href="/wiki/Extracellular_space" title="Extracellular space">extracellular space</a> or <a href="/wiki/Blood" title="Blood">blood</a> into the cell. The concentration gradient set up by glucose concentrations fuels the process without the need for ATP.<sup id="cite_ref-18" class="reference"><a href="#cite_note-18"><span class="cite-bracket">[</span>18<span class="cite-bracket">]</span></a></sup> </p><p>When glucose binds to the glucose transporter, the protein channels change shape and undergo a conformational change to transport the glucose across the membrane. Once the glucose unbinds, the protein returns to its original shape. The glucose transporter is essential for carrying out physiological processes that require high energy demands in the brain, muscles, and kidneys by providing an adequate amount of energy substrate for <a href="/wiki/Metabolism" title="Metabolism">metabolism</a>. <a href="/wiki/Diabetes" title="Diabetes">Diabetes</a>, an example of a condition that involves glucose metabolism, highlights the importance of the regulation of glucose uptake in disease management.<sup id="cite_ref-19" class="reference"><a href="#cite_note-19"><span class="cite-bracket">[</span>19<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Mitochondrial_Ca2+_uniporter_(MCU)"><span id="Mitochondrial_Ca2.2B_uniporter_.28MCU.29"></span>Mitochondrial <style data-mw-deduplicate="TemplateStyles:r1123817410">.mw-parser-output .template-chem2-su{display:inline-block;font-size:80%;line-height:1;vertical-align:-0.35em}.mw-parser-output .template-chem2-su>span{display:block;text-align:left}.mw-parser-output sub.template-chem2-sub{font-size:80%;vertical-align:-0.35em}.mw-parser-output sup.template-chem2-sup{font-size:80%;vertical-align:0.65em}</style><span class="chemf nowrap">Ca<sup>2+</sup></span> uniporter (MCU)</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Uniporter&action=edit&section=4" title="Edit section: Mitochondrial Ca2+ uniporter (MCU)"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The <b>mitochondrial calcium uniporter</b> (MCU) is a protein complex located in the inner mitochondrial matrix that functions to take up calcium ions (Ca2+) into the <a href="/wiki/Mitochondrial_matrix" title="Mitochondrial matrix">matrix</a> from the <a href="/wiki/Cytoplasm" title="Cytoplasm">cytoplasm</a>.<sup id="cite_ref-De_Stefani_D_20-0" class="reference"><a href="#cite_note-De_Stefani_D-20"><span class="cite-bracket">[</span>20<span class="cite-bracket">]</span></a></sup> The transport of calcium ions is specifically used in cellular function for regulating energy production in the mitochondria, cytosolic <a href="/wiki/Calcium_signaling" title="Calcium signaling">calcium signaling</a>, and <a href="/wiki/Cell_death" title="Cell death">cell death</a>. The uniporter becomes activated when cytoplasmic levels of calcium rise above 1 uM.<sup id="cite_ref-De_Stefani_D_20-1" class="reference"><a href="#cite_note-De_Stefani_D-20"><span class="cite-bracket">[</span>20<span class="cite-bracket">]</span></a></sup> </p><p>The <a href="/wiki/Mitochondrial_calcium_uniporter" title="Mitochondrial calcium uniporter">MCU complex</a> comprises 4 parts: the port-forming subunits, regulatory subunits <a href="/wiki/MICU1_(gene)" class="mw-redirect" title="MICU1 (gene)">MICU1</a> and MICU2, and an auxiliary subunit, EMRE.<sup id="cite_ref-D'Angelo_D_21-0" class="reference"><a href="#cite_note-D'Angelo_D-21"><span class="cite-bracket">[</span>21<span class="cite-bracket">]</span></a></sup> These subunits work together to regulate the uptake of calcium in the mitochondria. Specifically, the EMRE subunit functions for the transport of calcium, and the MICU subunit functions in tightly regulating the activity of MCU to prevent the overload of calcium concentrations in the cytoplasm.<sup id="cite_ref-D'Angelo_D_21-1" class="reference"><a href="#cite_note-D'Angelo_D-21"><span class="cite-bracket">[</span>21<span class="cite-bracket">]</span></a></sup> Calcium is fundamental for signaling pathways in cells, as well as for cell death pathways.<sup id="cite_ref-D'Angelo_D_21-2" class="reference"><a href="#cite_note-D'Angelo_D-21"><span class="cite-bracket">[</span>21<span class="cite-bracket">]</span></a></sup> The function of the mitochondrial uniporter is critical for maintaining cellular <a href="/wiki/Homeostasis" title="Homeostasis">homeostasis</a>. </p><p>The MICU1 and MICU2 subunits are a <a href="/wiki/Protein_dimer" title="Protein dimer">heterodimer</a> connected by a <a href="/wiki/Disulfide" title="Disulfide">disulfide bridge</a>.<sup id="cite_ref-De_Stefani_D_20-2" class="reference"><a href="#cite_note-De_Stefani_D-20"><span class="cite-bracket">[</span>20<span class="cite-bracket">]</span></a></sup> When there are high levels of cytoplasmic calcium, the MICU1-MICU2 heterodimer undergoes a <a href="/wiki/Conformational_change" title="Conformational change">conformational change</a>.<sup id="cite_ref-De_Stefani_D_20-3" class="reference"><a href="#cite_note-De_Stefani_D-20"><span class="cite-bracket">[</span>20<span class="cite-bracket">]</span></a></sup> The heterodimer subunits have cooperative activation, which means <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1123817410"><span class="chemf nowrap">Ca<sup>2+</sup></span> binding to one MICU subunit in the heterodimer induces a conformational change on the other MICU subunits. The uptake of calcium is balanced by the <a href="/wiki/Sodium-calcium_exchanger" title="Sodium-calcium exchanger">sodium-calcium exchanger</a>.<sup id="cite_ref-D'Angelo_D_21-3" class="reference"><a href="#cite_note-D'Angelo_D-21"><span class="cite-bracket">[</span>21<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Large_neutral_amino_acid_transporter_(LAT1)"><span id="Large_neutral_amino_acid_transporter_.28LAT1.29"></span>Large neutral amino acid transporter (LAT1)</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Uniporter&action=edit&section=5" title="Edit section: Large neutral amino acid transporter (LAT1)"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:Protein_SLC3A2_PDB_2dh2.png" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/6/6d/Protein_SLC3A2_PDB_2dh2.png/220px-Protein_SLC3A2_PDB_2dh2.png" decoding="async" width="220" height="174" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/6/6d/Protein_SLC3A2_PDB_2dh2.png/330px-Protein_SLC3A2_PDB_2dh2.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/6/6d/Protein_SLC3A2_PDB_2dh2.png/440px-Protein_SLC3A2_PDB_2dh2.png 2x" data-file-width="951" data-file-height="751" /></a><figcaption>SLC3 protein coding gene for LAT1</figcaption></figure> <p>The <b>L-type amino acid transporter (LAT1)</b> is a uniporter that mediates the transport of <a href="/wiki/Neutral_amino_acid_transporter_A" title="Neutral amino acid transporter A">neutral amino acids</a> like <a href="/wiki/Tryptophan" title="Tryptophan">L-tryptophan</a>, <a href="/wiki/Leucine" title="Leucine">leucine</a>, <a href="/wiki/Histidine" title="Histidine">histidine</a>, <a href="/wiki/Proline" title="Proline">proline</a>, <a href="/wiki/Alanine" title="Alanine">alanine</a>, etc.<sup id="cite_ref-Häfliger_P_6-1" class="reference"><a href="#cite_note-Häfliger_P-6"><span class="cite-bracket">[</span>6<span class="cite-bracket">]</span></a></sup> <a href="/wiki/CD98" title="CD98">LAT1</a> favors the transport of amino acids with large branched or <a href="/wiki/Amino_acid" title="Amino acid">aromatic side chains</a>. The amino acid transporter functions to move essential amino acids into the <a href="/wiki/Intestinal_epithelium" title="Intestinal epithelium">intestinal epithelium</a>, <a href="/wiki/Placenta" title="Placenta">placenta</a>, and <a href="/wiki/Blood%E2%80%93brain_barrier" title="Blood–brain barrier">blood-brain barrier</a> for cellular processes such as metabolism and cell signaling.<sup id="cite_ref-Bhutia_YD_22-0" class="reference"><a href="#cite_note-Bhutia_YD-22"><span class="cite-bracket">[</span>22<span class="cite-bracket">]</span></a></sup> The transporter is of particular significance in the <a href="/wiki/Central_nervous_system" title="Central nervous system">central nervous system</a> as it provides the necessary amino acids for protein synthesis and <a href="/wiki/Neurotransmitter" title="Neurotransmitter">neurotransmitter production</a> in brain cells.<sup id="cite_ref-Bhutia_YD_22-1" class="reference"><a href="#cite_note-Bhutia_YD-22"><span class="cite-bracket">[</span>22<span class="cite-bracket">]</span></a></sup> <a href="/wiki/Aromatic_amino_acid" title="Aromatic amino acid">Aromatic amino acids</a> like <a href="/wiki/Phenylalanine" title="Phenylalanine">phenylalanine</a> and <a href="/wiki/Tryptophan" title="Tryptophan">tryptophan</a> are precursors for neurotransmitters like <a href="/wiki/Dopamine" title="Dopamine">dopamine</a>, <a href="/wiki/Serotonin" title="Serotonin">serotonin</a>, and <a href="/wiki/Norepinephrine" title="Norepinephrine">norepinephrine</a>.<sup id="cite_ref-Bhutia_YD_22-2" class="reference"><a href="#cite_note-Bhutia_YD-22"><span class="cite-bracket">[</span>22<span class="cite-bracket">]</span></a></sup> </p><p>LAT1 is a membrane protein of the <a href="/wiki/SLC7A14" title="SLC7A14">SLC7</a> family of transporters and works in conjunction with the <a href="/wiki/Solute_carrier_family" title="Solute carrier family">SLC3 family</a> member <a href="/wiki/4F2_cell-surface_antigen_heavy_chain" title="4F2 cell-surface antigen heavy chain">4F2hc</a> to form a <a href="/wiki/Protein_dimer" title="Protein dimer">heterodimeric</a> complex known as the 4F2hc complex.<sup id="cite_ref-Häfliger_P_6-2" class="reference"><a href="#cite_note-Häfliger_P-6"><span class="cite-bracket">[</span>6<span class="cite-bracket">]</span></a></sup> The heterodimer consists of a light chain and a heavy chain <a href="/wiki/Covalent_bond" title="Covalent bond">covalently bonded</a> by a <a href="/wiki/Disulfide_bond" class="mw-redirect" title="Disulfide bond">disulfide bond</a>. The light chain is the one that carries out transport, while the heavy chain is needed to stabilize the dimer.<sup id="cite_ref-Häfliger_P_6-3" class="reference"><a href="#cite_note-Häfliger_P-6"><span class="cite-bracket">[</span>6<span class="cite-bracket">]</span></a></sup> </p><p>There is some controversy over whether LAT1 is an uniporter or an <a href="/wiki/Antiporter" title="Antiporter">antiporter</a>. The transporter has uniporter characteristics of transporting amino acids into cells in a unidirectional manner down the concentration gradient. However, recently it has been found that the transporter has antiporter characteristics of exchanging neutral amino acids for abundant intracellular amino acids.<sup id="cite_ref-23" class="reference"><a href="#cite_note-23"><span class="cite-bracket">[</span>23<span class="cite-bracket">]</span></a></sup> Over-expression of LAT1 has been found in human <a href="/wiki/Cancer" title="Cancer">cancer</a> and is associated with playing a role in cancer metabolism.<sup id="cite_ref-24" class="reference"><a href="#cite_note-24"><span class="cite-bracket">[</span>24<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Equilibrative_nucleoside_transporters_(ENTs)"><span id="Equilibrative_nucleoside_transporters_.28ENTs.29"></span>Equilibrative nucleoside transporters (ENTs)</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Uniporter&action=edit&section=6" title="Edit section: Equilibrative nucleoside transporters (ENTs)"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The <b>nucleoside transporters</b>, or <b>equilibrative nucleoside transporters</b>, are uniporters that transport <a href="/wiki/Nucleoside" title="Nucleoside">nucleosides</a>, <a href="/wiki/Nucleobase" class="mw-redirect" title="Nucleobase">nucleobases</a>, and <a href="/wiki/Pharmacology" title="Pharmacology">therapeutic drugs</a> across the cell membrane.<sup id="cite_ref-Boswell_25-0" class="reference"><a href="#cite_note-Boswell-25"><span class="cite-bracket">[</span>25<span class="cite-bracket">]</span></a></sup> Nucleosides serve as building blocks for <a href="/wiki/Nucleic_acid" title="Nucleic acid">nucleic acid synthesis</a> and are key components for energy metabolism in creating <a href="/wiki/Adenosine_triphosphate" title="Adenosine triphosphate">ATP</a>/ <a href="/wiki/Guanosine_triphosphate" title="Guanosine triphosphate">GTP</a>.<sup id="cite_ref-Hollenstein_M_26-0" class="reference"><a href="#cite_note-Hollenstein_M-26"><span class="cite-bracket">[</span>26<span class="cite-bracket">]</span></a></sup> They also act as ligands for <a href="/wiki/Receptors,_amino_acid" class="mw-redirect" title="Receptors, amino acid">purinergic receptors</a> such as <a href="/wiki/Adenosine" title="Adenosine">adenosine</a> and <a href="/wiki/Inosine" title="Inosine">inosine</a>. ENTs allow the transport of nucleosides down their concentration gradient. They also have the ability to deliver nucleoside analogs to intracellular targets for the treatment of <a href="/wiki/Neoplasm" title="Neoplasm">tumors</a> and viral infections.<sup id="cite_ref-Hollenstein_M_26-1" class="reference"><a href="#cite_note-Hollenstein_M-26"><span class="cite-bracket">[</span>26<span class="cite-bracket">]</span></a></sup> </p><p>ENTs are part of the <a href="/wiki/Major_facilitator_superfamily" title="Major facilitator superfamily">Major Facilitator Superfamily (MFS)</a> and are suggested to transport nucleosides using a clamp-and-switch model.<sup id="cite_ref-Hollenstein_M_26-2" class="reference"><a href="#cite_note-Hollenstein_M-26"><span class="cite-bracket">[</span>26<span class="cite-bracket">]</span></a></sup> In this model, the substrate first binds to the transporter, which leads to a conformational change that forms an occluded state (clamp). Then, the transporter switches to face the other side of the membrane and releases the bound substrate (switching).<sup id="cite_ref-Hollenstein_M_26-3" class="reference"><a href="#cite_note-Hollenstein_M-26"><span class="cite-bracket">[</span>26<span class="cite-bracket">]</span></a></sup> </p><p>ENTs have been found in <a href="/wiki/Protozoa" title="Protozoa">protozoa</a> and mammals. In humans, they have been discovered as ENT3 (hENT1-3) and <a href="/wiki/ENT4" class="mw-redirect" title="ENT4">ENT4</a> (hENT4) transporters.<sup id="cite_ref-Boswell_25-1" class="reference"><a href="#cite_note-Boswell-25"><span class="cite-bracket">[</span>25<span class="cite-bracket">]</span></a></sup> ENTs are expressed across all tissue types, but certain ENT proteins have been found to be more abundant in specific tissues. hENT1 is found mostly in the <a href="/wiki/Adrenal_gland" title="Adrenal gland">adrenal glands</a>, <a href="/wiki/Ovary" title="Ovary">ovary</a>, <a href="/wiki/Stomach" title="Stomach">stomach</a> and <a href="/wiki/Small_intestine" title="Small intestine">small intestines</a>.<sup id="cite_ref-Boswell_25-2" class="reference"><a href="#cite_note-Boswell-25"><span class="cite-bracket">[</span>25<span class="cite-bracket">]</span></a></sup> hENT2 is expressed mostly in neurological tissues and small parts of the <a href="/wiki/Skin" title="Skin">skin</a>, placenta, <a href="/wiki/Bladder" title="Bladder">urinary bladder</a>, <a href="/wiki/Cardiac_muscle" title="Cardiac muscle">heart muscle</a> and <a href="/wiki/Gallbladder" title="Gallbladder">gallbladder</a>.<sup id="cite_ref-Boswell_25-3" class="reference"><a href="#cite_note-Boswell-25"><span class="cite-bracket">[</span>25<span class="cite-bracket">]</span></a></sup> hENT3 is expressed highly in the <a href="/wiki/Cerebral_cortex" title="Cerebral cortex">cerebral cortex</a>, <a href="/wiki/Lateral_ventricles" title="Lateral ventricles">lateral ventricle</a>, <a href="/wiki/Ovary" title="Ovary">ovary</a> and <a href="/wiki/Adrenal_gland" title="Adrenal gland">adrenal gland</a>.<sup id="cite_ref-Boswell_25-4" class="reference"><a href="#cite_note-Boswell-25"><span class="cite-bracket">[</span>25<span class="cite-bracket">]</span></a></sup> hENT4 is more commonly known as the <a href="/wiki/Plasma_membrane_monoamine_transporter" title="Plasma membrane monoamine transporter">plasma membrane monoamine transporter (PMAT)</a>, as it facilitates the movement of organic <a href="/wiki/Ion" title="Ion">cations</a> and biogenic <a href="/wiki/Amine" title="Amine">amines</a> across the membrane.<sup id="cite_ref-Boswell_25-5" class="reference"><a href="#cite_note-Boswell-25"><span class="cite-bracket">[</span>25<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="Mechanism">Mechanism</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Uniporter&action=edit&section=7" title="Edit section: Mechanism"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:Uniporter_attivo.gif" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/9/98/Uniporter_attivo.gif/220px-Uniporter_attivo.gif" decoding="async" width="220" height="221" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/9/98/Uniporter_attivo.gif/330px-Uniporter_attivo.gif 1.5x, //upload.wikimedia.org/wikipedia/commons/9/98/Uniporter_attivo.gif 2x" data-file-width="399" data-file-height="400" /></a><figcaption>Mechanism of uniport transport across cell membrane</figcaption></figure><p>Uniporters work to transport molecules or ions by <a href="/wiki/Passive_transport" title="Passive transport">passive transport</a> across a cell membrane down its <a href="/wiki/Fick%27s_laws_of_diffusion" title="Fick's laws of diffusion">concentration gradient.</a> </p><p>Upon binding and recognition of a specific substrate molecule on one side of the uniporter membrane, a <a href="/wiki/Conformational_change" title="Conformational change">conformational change</a> is triggered in the transporter protein.<sup id="cite_ref-Fan_27-0" class="reference"><a href="#cite_note-Fan-27"><span class="cite-bracket">[</span>27<span class="cite-bracket">]</span></a></sup> This causes the transporter protein to change its three-dimensional shape, which ensures the substrate molecule is captured within the transporter proteins structure. The conformational change leads to the translocation of the substrate across the membrane onto the other side.<sup id="cite_ref-Fan_27-1" class="reference"><a href="#cite_note-Fan-27"><span class="cite-bracket">[</span>27<span class="cite-bracket">]</span></a></sup> On the other side of the membrane, the uniporter undergoes another conformational change in the release of the substrate molecule. The uniporter returns to its original conformation to bind another molecule for transport.<sup id="cite_ref-Fan_27-2" class="reference"><a href="#cite_note-Fan-27"><span class="cite-bracket">[</span>27<span class="cite-bracket">]</span></a></sup> </p><p>Unlike <a href="/wiki/Symporter" title="Symporter">symporters</a> and <a href="/wiki/Antiporter" title="Antiporter">antiporters</a>, uniporters transport one molecule/ion in a single direction based on the concentration gradient.<sup id="cite_ref-Majumder_P_28-0" class="reference"><a href="#cite_note-Majumder_P-28"><span class="cite-bracket">[</span>28<span class="cite-bracket">]</span></a></sup> The entire process depends on the substrate's concentration difference across the membrane to be the driving force for the transport by uniporters.<sup id="cite_ref-Majumder_P_28-1" class="reference"><a href="#cite_note-Majumder_P-28"><span class="cite-bracket">[</span>28<span class="cite-bracket">]</span></a></sup> Cellular energy in the form of <a href="/wiki/ATP-binding_motif" title="ATP-binding motif">ATP</a> is not required for this process.<sup id="cite_ref-Majumder_P_28-2" class="reference"><a href="#cite_note-Majumder_P-28"><span class="cite-bracket">[</span>28<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="Physiological_processes">Physiological processes</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Uniporter&action=edit&section=8" title="Edit section: Physiological processes"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Uniporters play an essential role in carrying out various cellular functions. Each uniporter is specialized to facilitate the transport of a specific molecule or ion across the cell membrane. Examples of a few of the physiological roles uniporters aid in include:<sup id="cite_ref-David_R_29-0" class="reference"><a href="#cite_note-David_R-29"><span class="cite-bracket">[</span>29<span class="cite-bracket">]</span></a></sup> </p> <ol><li>Nutrient Uptake: Uniporters facilitate the transport of essential <a href="/wiki/Nutrient" title="Nutrient">nutrients</a> into the cell. Glucose transporters (GLUTs) are uniporters that uptake glucose for <a href="/wiki/ATP_synthase" title="ATP synthase">energy production</a>.<sup id="cite_ref-David_R_29-1" class="reference"><a href="#cite_note-David_R-29"><span class="cite-bracket">[</span>29<span class="cite-bracket">]</span></a></sup></li> <li>Ion homeostasis: Uniporters facilitate in maintaining the balance of ions (i.e., <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1123817410"><span class="chemf nowrap"><a href="/wiki/Na%2B_channel" class="mw-redirect" title="Na+ channel">Na<sup class="template-chem2-sup">+</sup></a></span> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1123817410"><span class="chemf nowrap"><a href="/wiki/Potassium_channel" title="Potassium channel">K<sup class="template-chem2-sup">+</sup></a></span>, <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1123817410"><span class="chemf nowrap"><a href="/wiki/Calcium_channel" title="Calcium channel">Ca<sup>2+</sup></a></span>, <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1123817410"><span class="chemf nowrap"><a href="/wiki/Chloride_channel" title="Chloride channel">Cl<sup class="template-chem2-sup">−</sup></a></span>) within cells <sup id="cite_ref-30" class="reference"><a href="#cite_note-30"><span class="cite-bracket">[</span>30<span class="cite-bracket">]</span></a></sup></li> <li><a href="/wiki/Metabolism" title="Metabolism">Metabolism</a>: Uniporters are involved in the transport of essential ions, <a href="/wiki/Amino_acid" title="Amino acid">amino acids</a> and molecules required for the <a href="/wiki/Metabolic_pathway" title="Metabolic pathway">metabolic pathway</a>, <a href="/wiki/Protein_biosynthesis" title="Protein biosynthesis">protein synthesis</a> and energy production<sup id="cite_ref-De_Stefani_D_20-4" class="reference"><a href="#cite_note-De_Stefani_D-20"><span class="cite-bracket">[</span>20<span class="cite-bracket">]</span></a></sup></li> <li><a href="/wiki/Cell_signaling" title="Cell signaling">Cell signaling</a>: Calcium uniporters help regulate intercellular calcium levels essential for <a href="/wiki/Signal_transduction" title="Signal transduction">signal transduction</a><sup id="cite_ref-Zhang_XC_1-2" class="reference"><a href="#cite_note-Zhang_XC-1"><span class="cite-bracket">[</span>1<span class="cite-bracket">]</span></a></sup></li> <li>Waste removal: Uniporters aid in removing <a href="/wiki/Metabolic_waste" title="Metabolic waste">metabolic waste</a> products and toxins from cells</li> <li><a href="/wiki/Acid%E2%80%93base_homeostasis" title="Acid–base homeostasis">pH regulation</a>: Transport of ions by uniporters also helps to maintain the overall <a href="/wiki/Acid-base_balance" class="mw-redirect" title="Acid-base balance">acid-base balance</a> within cells <sup id="cite_ref-31" class="reference"><a href="#cite_note-31"><span class="cite-bracket">[</span>31<span class="cite-bracket">]</span></a></sup></li></ol> <div class="mw-heading mw-heading2"><h2 id="Mutations">Mutations</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Uniporter&action=edit&section=9" title="Edit section: Mutations"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Mutations in genes encoding uniporters lead to dysfunctional transporter proteins being formed. This loss of function in uniporters causes disruption in cellular function which leads to various <a href="/wiki/Disease" title="Disease">diseases</a> and disorders. </p> <table class="wikitable"> <caption> </caption> <tbody><tr> <th>Gene with mutation </th> <th>Disease </th> <th>Result of disease </th></tr> <tr> <td>Mutations in the <a href="/wiki/GLUT1" title="GLUT1">SLC2A1 gene</a> which encode glucose transporters (GLUTs) <sup id="cite_ref-MedlinePlus_32-0" class="reference"><a href="#cite_note-MedlinePlus-32"><span class="cite-bracket">[</span>32<span class="cite-bracket">]</span></a></sup> </td> <td><a href="/wiki/GLUT1_deficiency" title="GLUT1 deficiency">GLUT1 Deficiency Syndrome</a><sup id="cite_ref-MedlinePlus_32-1" class="reference"><a href="#cite_note-MedlinePlus-32"><span class="cite-bracket">[</span>32<span class="cite-bracket">]</span></a></sup> </td> <td>Impaired glucose transport across the blood-brain barriers, and neurological symptoms such as seizures, development delay, and movement disorders <sup id="cite_ref-MedlinePlus-2_33-0" class="reference"><a href="#cite_note-MedlinePlus-2-33"><span class="cite-bracket">[</span>33<span class="cite-bracket">]</span></a></sup> </td></tr> <tr> <td>Mutations in the <a href="/wiki/Cystic_fibrosis_transmembrane_conductance_regulator" title="Cystic fibrosis transmembrane conductance regulator">CFTR gene</a> encoding <a href="/wiki/Ion_channel" title="Ion channel">ion channels</a><sup id="cite_ref-MedlinePlus_32-2" class="reference"><a href="#cite_note-MedlinePlus-32"><span class="cite-bracket">[</span>32<span class="cite-bracket">]</span></a></sup> </td> <td><a href="/wiki/Cystic_fibrosis" title="Cystic fibrosis">Cystic Fibrosis</a><sup id="cite_ref-MedlinePlus_32-3" class="reference"><a href="#cite_note-MedlinePlus-32"><span class="cite-bracket">[</span>32<span class="cite-bracket">]</span></a></sup> </td> <td>Problems with breathing and digestion due to thick mucus forming; affects multiple organs, primarily the lungs and digestive system <sup id="cite_ref-MedlinePlus-2_33-1" class="reference"><a href="#cite_note-MedlinePlus-2-33"><span class="cite-bracket">[</span>33<span class="cite-bracket">]</span></a></sup> </td></tr> <tr> <td>Mutation in <a href="/wiki/KCNA3" title="KCNA3">KCNA1 gene</a> encoding <a href="/wiki/Potassium_channel" title="Potassium channel">potassium channels</a><sup id="cite_ref-MedlinePlus_32-4" class="reference"><a href="#cite_note-MedlinePlus-32"><span class="cite-bracket">[</span>32<span class="cite-bracket">]</span></a></sup> </td> <td><a href="/wiki/Hypokalemic_periodic_paralysis" title="Hypokalemic periodic paralysis">Hypokalemic Periodic Paralysis</a><sup id="cite_ref-MedlinePlus_32-5" class="reference"><a href="#cite_note-MedlinePlus-32"><span class="cite-bracket">[</span>32<span class="cite-bracket">]</span></a></sup> </td> <td>Periodic muscle weakness; associated with low potassium levels due to altered transport activity <sup id="cite_ref-MedlinePlus-2_33-2" class="reference"><a href="#cite_note-MedlinePlus-2-33"><span class="cite-bracket">[</span>33<span class="cite-bracket">]</span></a></sup> </td></tr> <tr> <td>Mutations in the <a href="/wiki/SLC6A19_(gene)" class="mw-redirect" title="SLC6A19 (gene)">SLC6A19 gene</a> encoding amino acid transporter <sup id="cite_ref-MedlinePlus_32-6" class="reference"><a href="#cite_note-MedlinePlus-32"><span class="cite-bracket">[</span>32<span class="cite-bracket">]</span></a></sup> </td> <td><a href="/wiki/Hartnup_disease" title="Hartnup disease">Hartnup Disease</a><sup id="cite_ref-MedlinePlus_32-7" class="reference"><a href="#cite_note-MedlinePlus-32"><span class="cite-bracket">[</span>32<span class="cite-bracket">]</span></a></sup> </td> <td>Impaired absorption of certain amino acid in the intestines and kidneys <sup id="cite_ref-MedlinePlus-2_33-3" class="reference"><a href="#cite_note-MedlinePlus-2-33"><span class="cite-bracket">[</span>33<span class="cite-bracket">]</span></a></sup> </td></tr> <tr> <td>Mutations in the <a href="/wiki/AGXT" title="AGXT">AGXT gene</a> encoding peroxisomal membrane transporter <sup id="cite_ref-MedlinePlus_32-8" class="reference"><a href="#cite_note-MedlinePlus-32"><span class="cite-bracket">[</span>32<span class="cite-bracket">]</span></a></sup> </td> <td><a href="/wiki/Primary_hyperoxaluria" title="Primary hyperoxaluria">Primary Hyperoxaluria</a><sup id="cite_ref-MedlinePlus_32-9" class="reference"><a href="#cite_note-MedlinePlus-32"><span class="cite-bracket">[</span>32<span class="cite-bracket">]</span></a></sup> </td> <td>Metabolic disease; Leads to accumulation of oxalate in causing kidney stone and damage <sup id="cite_ref-MedlinePlus-2_33-4" class="reference"><a href="#cite_note-MedlinePlus-2-33"><span class="cite-bracket">[</span>33<span class="cite-bracket">]</span></a></sup> </td></tr></tbody></table> <div class="mw-heading mw-heading2"><h2 id="See_also">See also</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Uniporter&action=edit&section=10" title="Edit section: See also"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <ul><li><a href="/wiki/Antiporter" title="Antiporter">Antiporter</a></li> <li><a href="/wiki/Symporter" title="Symporter">Symporter</a></li></ul> <div class="mw-heading mw-heading2"><h2 id="References">References</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Uniporter&action=edit&section=11" title="Edit section: References"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <style data-mw-deduplicate="TemplateStyles:r1239543626">.mw-parser-output .reflist{margin-bottom:0.5em;list-style-type:decimal}@media screen{.mw-parser-output .reflist{font-size:90%}}.mw-parser-output .reflist .references{font-size:100%;margin-bottom:0;list-style-type:inherit}.mw-parser-output .reflist-columns-2{column-width:30em}.mw-parser-output .reflist-columns-3{column-width:25em}.mw-parser-output .reflist-columns{margin-top:0.3em}.mw-parser-output .reflist-columns ol{margin-top:0}.mw-parser-output .reflist-columns li{page-break-inside:avoid;break-inside:avoid-column}.mw-parser-output .reflist-upper-alpha{list-style-type:upper-alpha}.mw-parser-output .reflist-upper-roman{list-style-type:upper-roman}.mw-parser-output .reflist-lower-alpha{list-style-type:lower-alpha}.mw-parser-output .reflist-lower-greek{list-style-type:lower-greek}.mw-parser-output .reflist-lower-roman{list-style-type:lower-roman}</style><div class="reflist"> <div class="mw-references-wrap mw-references-columns"><ol class="references"> <li id="cite_note-Zhang_XC-1"><span class="mw-cite-backlink">^ <a href="#cite_ref-Zhang_XC_1-0"><sup><i><b>a</b></i></sup></a> <a href="#cite_ref-Zhang_XC_1-1"><sup><i><b>b</b></i></sup></a> <a href="#cite_ref-Zhang_XC_1-2"><sup><i><b>c</b></i></sup></a></span> <span class="reference-text"><style data-mw-deduplicate="TemplateStyles:r1238218222">.mw-parser-output cite.citation{font-style:inherit;word-wrap:break-word}.mw-parser-output .citation q{quotes:"\"""\"""'""'"}.mw-parser-output .citation:target{background-color:rgba(0,127,255,0.133)}.mw-parser-output .id-lock-free.id-lock-free a{background:url("//upload.wikimedia.org/wikipedia/commons/6/65/Lock-green.svg")right 0.1em center/9px no-repeat}.mw-parser-output .id-lock-limited.id-lock-limited a,.mw-parser-output .id-lock-registration.id-lock-registration a{background:url("//upload.wikimedia.org/wikipedia/commons/d/d6/Lock-gray-alt-2.svg")right 0.1em center/9px no-repeat}.mw-parser-output .id-lock-subscription.id-lock-subscription a{background:url("//upload.wikimedia.org/wikipedia/commons/a/aa/Lock-red-alt-2.svg")right 0.1em center/9px no-repeat}.mw-parser-output .cs1-ws-icon a{background:url("//upload.wikimedia.org/wikipedia/commons/4/4c/Wikisource-logo.svg")right 0.1em center/12px no-repeat}body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-free a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-limited a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-registration a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-subscription a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .cs1-ws-icon a{background-size:contain;padding:0 1em 0 0}.mw-parser-output .cs1-code{color:inherit;background:inherit;border:none;padding:inherit}.mw-parser-output .cs1-hidden-error{display:none;color:var(--color-error,#d33)}.mw-parser-output .cs1-visible-error{color:var(--color-error,#d33)}.mw-parser-output .cs1-maint{display:none;color:#085;margin-left:0.3em}.mw-parser-output .cs1-kern-left{padding-left:0.2em}.mw-parser-output .cs1-kern-right{padding-right:0.2em}.mw-parser-output .citation .mw-selflink{font-weight:inherit}@media screen{.mw-parser-output .cs1-format{font-size:95%}html.skin-theme-clientpref-night .mw-parser-output .cs1-maint{color:#18911f}}@media screen and (prefers-color-scheme:dark){html.skin-theme-clientpref-os .mw-parser-output .cs1-maint{color:#18911f}}</style><cite id="CITEREFZhangHan2016" class="citation journal cs1">Zhang XC, Han L (2016). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5138270">"Uniporter substrate binding and transport: reformulating mechanistic questions"</a>. <i>Biophys Rep</i>. <b>2</b> (2–4): 45–54. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1007%2Fs41048-016-0030-7">10.1007/s41048-016-0030-7</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5138270">5138270</a></span>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/28018963">28018963</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Biophys+Rep&rft.atitle=Uniporter+substrate+binding+and+transport%3A+reformulating+mechanistic+questions&rft.volume=2&rft.issue=2%E2%80%934&rft.pages=45-54&rft.date=2016&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC5138270%23id-name%3DPMC&rft_id=info%3Apmid%2F28018963&rft_id=info%3Adoi%2F10.1007%2Fs41048-016-0030-7&rft.aulast=Zhang&rft.aufirst=XC&rft.au=Han%2C+L&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC5138270&rfr_id=info%3Asid%2Fen.wikipedia.org%3AUniporter" class="Z3988"></span></span> </li> <li id="cite_note-Alberts-2"><span class="mw-cite-backlink">^ <a href="#cite_ref-Alberts_2-0"><sup><i><b>a</b></i></sup></a> <a href="#cite_ref-Alberts_2-1"><sup><i><b>b</b></i></sup></a></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFAlberts1998" class="citation book cs1">Alberts, Bruce (1998). <i>Essential cell biology : an introduction to the molecular biology of the cell</i>. 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"Uniporters, symporters and antiporters". <i>J Exp Biol</i>. <b>196</b>: 5–6. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1242%2Fjeb.196.1.5">10.1242/jeb.196.1.5</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/7823043">7823043</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=J+Exp+Biol&rft.atitle=Uniporters%2C+symporters+and+antiporters&rft.volume=196&rft.pages=5-6&rft.date=1994-11&rft_id=info%3Adoi%2F10.1242%2Fjeb.196.1.5&rft_id=info%3Apmid%2F7823043&rft.aulast=Wolfersberger&rft.aufirst=MG&rfr_id=info%3Asid%2Fen.wikipedia.org%3AUniporter" class="Z3988"></span></span> </li> <li id="cite_note-4"><span class="mw-cite-backlink"><b><a href="#cite_ref-4">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFPrattVoetVoet2002" class="citation book cs1">Pratt CA, Voet D, Voet JG (2002). <i>Fundamentals of biochemistry</i>. 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MedlinePlus.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=unknown&rft.jtitle=Genetic+Conditions&rft.atitle=GLUT1+deficiency+syndrome&rft_id=https%3A%2F%2Fmedlineplus.gov%2Fgenetics%2Fcondition%2Fglut1-deficiency-syndrome%2F&rfr_id=info%3Asid%2Fen.wikipedia.org%3AUniporter" class="Z3988"></span></span> </li> </ol></div></div> <div class="navbox-styles"><style data-mw-deduplicate="TemplateStyles:r1129693374">.mw-parser-output .hlist dl,.mw-parser-output .hlist ol,.mw-parser-output .hlist ul{margin:0;padding:0}.mw-parser-output .hlist dd,.mw-parser-output .hlist dt,.mw-parser-output .hlist li{margin:0;display:inline}.mw-parser-output .hlist.inline,.mw-parser-output .hlist.inline dl,.mw-parser-output .hlist.inline ol,.mw-parser-output .hlist.inline ul,.mw-parser-output .hlist dl dl,.mw-parser-output .hlist dl ol,.mw-parser-output .hlist dl ul,.mw-parser-output .hlist ol dl,.mw-parser-output .hlist ol ol,.mw-parser-output .hlist ol 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