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[[Protein Data Bank|PDB]] {{PDBe|3uvj}} }} '''Guanylate cyclase''' (EC 4.6.1.2, also known as '''guanyl cyclase''', '''guanylyl cyclase''', or '''GC'''; systematic name '''GTP diphosphate-lyase (cyclizing; 3′,5′-cyclic-GMP-forming)''') is a [[lyase]] [[enzyme]] that converts [[guanosine triphosphate]] (GTP) to [[cyclic guanosine monophosphate]] (cGMP) and [[pyrophosphate]]:<ref name="Martin Berka Tsai Murad 2005 pp. 478–492"/> : GTP = 3′,5′-cyclic GMP + diphosphate It is often part of the [[G protein]] [[Biochemical cascade|signaling cascade]] that is activated by low [[Calcium encoding|intracellular calcium levels]] and inhibited by high intracellular calcium levels. In response to calcium levels, guanylate cyclase synthesizes cGMP from GTP. cGMP keeps cGMP-gated [[Ion channel|channel]]s open, allowing for the entry of calcium into the cell.<ref>{{cite journal |author1=Sakurai K. |author2=Chen J. |author3=Kefalov V. | year = 2011 | title = Role of guanylate cylcase modulation in mouse cone phototransduction | journal = The Journal of Neuroscience | volume = 31| issue = 22| pages = 7991–8000 | doi=10.1523/jneurosci.6650-10.2011 | pmid=21632921 | pmc=3124626}}</ref> Like [[Cyclic adenosine monophosphate|cAMP]], cGMP is an important [[Second messenger system|second messenger]] that internalizes the message carried by intercellular messengers such as [[peptide hormone]]s and [[nitric oxide]] and can also function as an [[Autocrine signaling|autocrine signal]].<ref name="Martin Berka Tsai Murad 2005 pp. 478–492">{{cite book | last1=Martin | first1=Emil | last2=Berka | first2=Vladimir | last3=Tsai | first3=Ah-Lim | last4=Murad | first4=Ferid | title=Methods in Enzymology | chapter=Soluble Guanylyl Cyclase: The Nitric Oxide Receptor | publisher=Elsevier | year=2005 | volume=396 | isbn=978-0-12-182801-1 | issn=0076-6879 | doi=10.1016/s0076-6879(05)96040-0 | pages=478–492 | pmid=16291255 | quote=Soluble guanylyl cyclase is recognized as the most sensitive physiologic receptor for nitric oxide. Binding of nitric oxide to the heme moiety of the cyclase induces its capacity to synthesize the second messenger cGMP.}}</ref> Depending on cell type, it can drive adaptive/developmental changes requiring [[Protein biosynthesis|protein synthesis]]. In [[smooth muscle]], cGMP is the signal for relaxation, and is coupled to many [[Homeostasis|homeostatic mechanism]]s including regulation of [[vasodilation]], vocal tone, [[Beta cell|insulin secretion]], and [[peristalsis]]. Once formed, cGMP can be degraded by [[phosphodiesterase]]s, which themselves are under different forms of regulation, depending on the tissue. ==Reaction== Guanylate cyclase catalyzes the reaction of [[guanosine triphosphate]] (GTP) to [[cyclic GMP|3',5'-cyclic guanosine monophosphate]] (cGMP) and [[pyrophosphate]]: <gallery> Image:Guanosintriphosphat_protoniert.svg|[[Guanosine triphosphate|GTP]] Image:CGMP.svg|[[Cyclic guanosine monophosphate|cGMP]] </gallery> ==Effects== Guanylate cyclase is found in the [[retina]] (RETGC) and modulates [[visual phototransduction]] in [[Rod cell|rod]]s and [[Cone cell|cone]]s. It is part of the [[Calcium metabolism|calcium negative feedback system]] that is activated in response to the hyperpolarization of the [[Photoreceptor cell|photoreceptor]]s by light. This causes less intracellular calcium, which stimulates [[guanylate cyclase activator|guanylate cyclase-activating proteins]] (GCAPs). Studies have shown that cGMP synthesis in cones is about 5-10 times higher than it is in rods, which may play an important role in modulating cone adaption to light.<ref>{{cite journal | vauthors = Takemoto N, Tachibanaski S, Kawamura S | year = 2009 | title = High cGMP synthetic activity in carp cones | journal = Proc Natl Acad Sci USA | volume = 106 | issue = 28| pages = 11788–11793 | doi=10.1073/pnas.0812781106| pmc = 2710672 | pmid=19556550| bibcode = 2009PNAS..10611788T | doi-access = free }}</ref> In addition, studies have shown that [[zebrafish]] express a higher number of GCAPs than mammals, and that zebrafish GCAPs can bind at least three calcium ions.<ref>{{cite journal | vauthors = Scholten A, Koch K | year = 2011 | title = Differential calcium signaling by cone specific guanylate cyclase-activing proteins from the zebrafish retina | doi = 10.1371/journal.pone.0023117| pmid = 21829700 | pmc = 3149064 | journal = PLOS ONE | volume = 6 | issue = 8| pages = e23117 | bibcode = 2011PLoSO...623117S | doi-access = free }}</ref> [[Guanylate cyclase 2C]] (GC-C) is an enzyme expressed mainly in intestinal neurons. Activation of GC-C amplifies the excitatory cell response that is modulated by [[glutamate]] and [[acetylcholine receptor]]s. GC-C, while known mainly for its secretory regulation in the [[intestinal epithelium]], is also expressed in the brain. To be specific, it is found in the [[Soma (biology)|somata]] and [[dendrite]]s of [[Dopaminergic cell groups|dopaminergic neuron]]s in the [[ventral tegmental area]] (VTA) and the [[substantia nigra]]. Some studies implicate this pathway as having a role in [[Attention deficit hyperactivity disorder|attention deficiency and hyperactive behavior]].<ref>{{cite journal | vauthors = Gong R, Ding C, Hu J, Lu Y, Liu F, Mann E, Xu F, Cohen M, Luo M | year = 2011 | title = Role for the membrane receptor guanylate cyclase-c in attention deficiency and hyperactive behavior }}</ref> Soluble guanylate cyclase contains a molecule of [[heme]], and is activated primarily by the binding of nitric oxide (NO) to that heme.<ref>{{cite book | vauthors = Derbyshire ER, Marletta MA | title = CGMP: Generators, Effectors and Therapeutic Implications | year = 2009 | chapter = Biochemistry of soluble guanylate cyclase | series = Handbook of Experimental Pharmacology | volume = 191 | issue =  | pages = 17–31|doi=10.1007/978-3-540-68964-5_2 | pmid = 19089323| isbn = 978-3-540-68960-7 | s2cid = 25597341 }}</ref> sGC is primary receptor for NO a gaseous, membrane-soluble [[neurotransmitter]]. sGC expression has been shown to be highest in the [[striatum]] compared to other brain regions and has been explored as a possible candidate for restoring striatal dysfunction in [[Parkinson's disease]]. sGC acts as an intracellular intermediary for regulating dopamine and glutamate. Upregulation, which creates neuronal sensitivity, of the cGMP in a dopamine-depleted striatum has been associated with the symptoms of Parkinson's. Increased intracellular cGMP has been shown to contribute to excessive neuron excitability and locomotor activity. Activation of this pathway can also stimulate [[glutamate–glutamine cycle|presynaptic glutamate release]] and cause an upregulation of [[AMPA]] receptors postsynaptically.<ref>{{cite journal | vauthors = Tseng K, Caballero A, Dec A, Cass D, Simak N, Sunu E, Park M, Blume S, Sammut S, Park D, West | year = 2011 | title = Inhibition of striatal soluble guanylate cyclase-cGMP signaling reverses basal ganglia dysfunction and akinesia in experimental Parkinsonism | journal = PLOS ONE | volume = 6| issue = 11| pages = e27187| doi = 10.1371/journal.pone.0027187 | pmid=22073284 | pmc=3206945| bibcode = 2011PLoSO...627187T | doi-access = free }}</ref> ==Types== There are membrane-bound (type 1, [[guanylate cyclase-coupled receptor]]) and soluble (type 2, [[soluble guanylate cyclase]]) forms of guanylate cyclases. Membrane bound guanylate cyclases include an external ligand-binding domain (e.g., for peptide hormones such as [[brain natriuretic peptide|BNP]] and [[atrial natriuretic peptide|ANP]]), a transmembrane domain, and an internal catalytic domain homologous to [[adenylyl cyclase]]s.<ref>{{cite journal | vauthors = Kuhn M | year = 2003 | title = Structure, Regulation, and Function of Mammalian Membrane Guanylate Cyclase Receptors, With a Focus on Guanylate Cyclase-A | journal = Circulation Research | volume = 93 | issue = 8| pages = 700–709 | doi=10.1161/01.res.0000094745.28948.4d| pmid = 14563709 | doi-access = free }}</ref> Recently, a directly light-gated guanylate cyclase has been discovered in an aquatic fungus.<ref name="Gao2015">{{cite journal | vauthors = Gao SQ, Nagpal J, Schneider MW, Kozjak-Pavlovic V, Nagel G, Gottschalk A | title = Optogenetic manipulation of cGMP in cells and animals by the tightly light-regulated guanylate-cyclase opsin CyclOp | journal = Nature Communications | volume = 6 | issue = 8046 | pages = 8046 | date = July 2015 | doi = 10.1038/ncomms9046 | pmid=26345128 | pmc=4569695| bibcode = 2015NatCo...6.8046G }}</ref><ref name="Scheib2015">{{cite journal |vauthors=Scheib U, Stehfest K, Gee CE, Körschen HG, Fudim R, Oertner TG, Hegemann P | title = The rhodopsin-guanylate cyclase of the aquatic fungus Blastocladiella emersonii enables fast optical control of cGMP signaling | journal = Science Signaling | volume = 8 | issue = 389 | pages = r8 |date = 2015 | doi=10.1126/scisignal.aab0611 | pmid=26268609| s2cid = 13140205 | url = https://zenodo.org/record/895813 }}</ref> In the mammalian retina, two forms of guanylate cyclase have been identified, each encoded by separate genes; [[RETGC-1]] and [[RETGC-2]]. RETGC-1 has been found to be expressed in higher levels in cones compared to rod cells. Studies have also shown that mutations in the RETGC-1 gene can lead to cone-rod dystrophy by disrupting the phototransduction processes. ==Mutations== [[Cone dystrophy]] (COD) is a retinal degradation of photoreceptor function wherein cone function is lost at the onset of the dystrophy but rod function is preserved until almost the end. COD has been linked to several genetic mutations including mutations in the [[GUCA1A|guanylate cyclase activator 1A]] (GUCA1A) and guanylate cyclase 2D (GUY2D) among other enzymes. To be specific, GUY2D codes for RETGC-1, which is involved in cone adaptation and photoreceptor sensitivity by synthesizing cGMP. Low concentrations of calcium cause the dimerization of RETGC-1 proteins through stimulation from guanylate cyclase-activating proteins (GCAP). This process happens at amino acids 817-857, and mutations in this region increase RETGC-1 affinity for GCAP. This works to alter the calcium sensitivity of the neuron by allowing mutant RETGC-1 to be activated by GCAP at higher calcium levels than the wild-type. Because RETGC-1 produces cGMP, which keeps cyclic nucleotide-gated channels open allowing the influx of calcium, this mutation causes extremely high intracellular calcium levels. Calcium, which plays many roles in the cell and is tightly regulated, disrupts the membrane when it appears in excess. Also, calcium is linked to [[apoptosis]] by causing the release of [[cytochrome c]]. Therefore, mutations in the RETGC-1 can cause COD by increasing intracellular calcium levels and stimulating cone photoreceptor death.<ref>{{cite journal | vauthors = Hoyos-Garcia M, Auz-Alexandre C, Almoguera B, Cantalapiedra D, Riveiro-Alvarez R, Lopez-Martinez A ''et al'' | year = 2011 | title = Mutation analysis at codon 838 of the guanylate cycllase 2D gene in Spanish families with autosomal dominant cone, cone-rod and macular dystrophies | journal = Molecular Vision | volume = 17 | pages = 1103–1109 | pmid = 21552474 | pmc = 3087450 }}</ref> ==See also== * [[Adenylyl cyclase]] * [[cyclic GMP|Cyclic guanosine monophosphate]] * [[Guanylyl cyclase activator]] (protein) ==References== {{reflist}} ==External links== * {{MeshName|Guanylate+Cyclase}} {{Intracellular signaling peptides and proteins}} {{Enzyme-linked receptors}} {{Phosphorus-oxygen lyases}} {{Enzymes}} {{Nitric oxide signaling}} {{Portal bar|Biology|border=no}} {{Authority control}} [[Category:EC 4.6.1]] 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