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(PDF) MscL Channel Inactivation: Role of Helices & Gate
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window.loswp.showSignupCaptcha = false window.loswp.willEdgeCache = false; window.loswp.work = {"work":{"id":123589065,"created_at":"2024-09-05T09:24:58.936-07:00","from_world_paper_id":258986754,"updated_at":"2025-02-02T10:11:53.208-08:00","_data":{"publisher":"Elsevier BV","ai_abstract":"The paper investigates the inactivation mechanisms of the bacterial mechanosensitive channel MscL, focusing on the role of flexible transmembrane helices and a unique 'dry' gate in the process. It highlights how MscL channels respond to mechanical stress, providing insights into their cooperative behavior and interaction with neighboring proteins. Through a combination of patch clamp, fluorescence, and advanced imaging techniques, the study reveals that MscL channels can form clusters in the membrane, influencing their activity. This research contributes to a deeper understanding of mechanosensitivity in bacterial cells, demonstrating potential implications for the study of mechanosensitive channels in other organisms.","ai_title_tag":"MscL Channel Inactivation: Role of Helices \u0026 Gate","publication_date":"2010,,","publication_name":"Biophysical Journal"},"document_type":"paper","pre_hit_view_count_baseline":null,"quality":"low","language":"en","title":"Inactivation of the Bacterial Mechanosensitive Channel MscL Involves Flexible Transmembrane Helices and a ‘Dry’ Gate","broadcastable":false,"draft":null,"has_indexable_attachment":true,"indexable":true}}["work"]; window.loswp.workCoauthors = [32819717]; window.loswp.locale = "en"; window.loswp.countryCode = "SG"; window.loswp.cwvAbTestBucket = ""; window.loswp.designVariant = "ds_vanilla"; window.loswp.fullPageMobileSutdModalVariant = "control"; window.loswp.useOptimizedScribd4genScript = false; window.loginModal = {}; window.loginModal.appleClientId = 'edu.academia.applesignon'; window.userInChina = "false";</script><script defer="" src="https://accounts.google.com/gsi/client"></script><div class="ds-loswp-container"><div class="ds-work-card--grid-container"><div class="ds-work-card--container js-loswp-work-card"><div class="ds-work-card--cover"><div class="ds-work-cover--wrapper"><div class="ds-work-cover--container"><button class="ds-work-cover--clickable js-swp-download-button" data-signup-modal="{"location":"swp-splash-paper-cover","attachmentId":117986231,"attachmentType":"pdf"}"><img alt="First page of “Inactivation of the Bacterial Mechanosensitive Channel MscL Involves Flexible Transmembrane Helices and a ‘Dry’ Gate”" class="ds-work-cover--cover-thumbnail" src="https://0.academia-photos.com/attachment_thumbnails/117986231/mini_magick20240905-1-xntxbr.png?1725553564" /><img alt="PDF Icon" class="ds-work-cover--file-icon" src="//a.academia-assets.com/images/single_work_splash/adobe_icon.svg" /><div class="ds-work-cover--hover-container"><span class="material-symbols-outlined" style="font-size: 20px" translate="no">download</span><p>Download Free PDF</p></div><div class="ds-work-cover--ribbon-container">Download Free PDF</div><div class="ds-work-cover--ribbon-triangle"></div></button></div></div></div><div class="ds-work-card--work-information"><h1 class="ds-work-card--work-title">Inactivation of the Bacterial Mechanosensitive Channel MscL Involves Flexible Transmembrane Helices and a ‘Dry’ Gate</h1><div class="ds-work-card--work-authors ds-work-card--detail"><a class="ds-work-card--author js-wsj-grid-card-author ds2-5-body-md ds2-5-body-link" data-author-id="32819717" href="https://umd.academia.edu/SergeiSukharev"><img alt="Profile image of Sergei Sukharev" class="ds-work-card--author-avatar" src="//a.academia-assets.com/images/s65_no_pic.png" />Sergei Sukharev</a></div><div class="ds-work-card--detail"><p class="ds-work-card--detail ds2-5-body-sm">2010, Biophysical Journal</p><div class="ds-work-card--work-metadata"><div class="ds-work-card--work-metadata__stat"><span class="material-symbols-outlined" style="font-size: 20px" translate="no">visibility</span><p class="ds2-5-body-sm" id="work-metadata-view-count">…</p></div><div class="ds-work-card--work-metadata__stat"><span class="material-symbols-outlined" style="font-size: 20px" translate="no">description</span><p class="ds2-5-body-sm">1 page</p></div><div class="ds-work-card--work-metadata__stat"><span class="material-symbols-outlined" style="font-size: 20px" translate="no">link</span><p class="ds2-5-body-sm">1 file</p></div></div><script>(async () => { const workId = 123589065; 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It highlights how MscL channels respond to mechanical stress, providing insights into their cooperative behavior and interaction with neighboring proteins. Through a combination of patch clamp, fluorescence, and advanced imaging techniques, the study reveals that MscL channels can form clusters in the membrane, influencing their activity. This research contributes to a deeper understanding of mechanosensitivity in bacterial cells, demonstrating potential implications for the study of mechanosensitive channels in other organisms.</p><div class="ds-work-card--button-container"><button class="ds2-5-button js-swp-download-button" data-signup-modal="{"location":"continue-reading-button--work-card","attachmentId":117986231,"attachmentType":"pdf","workUrl":"https://www.academia.edu/123589065/Inactivation_of_the_Bacterial_Mechanosensitive_Channel_MscL_Involves_Flexible_Transmembrane_Helices_and_a_Dry_Gate"}">See full PDF</button><button class="ds2-5-button ds2-5-button--secondary js-swp-download-button" data-signup-modal="{"location":"download-pdf-button--work-card","attachmentId":117986231,"attachmentType":"pdf","workUrl":"https://www.academia.edu/123589065/Inactivation_of_the_Bacterial_Mechanosensitive_Channel_MscL_Involves_Flexible_Transmembrane_Helices_and_a_Dry_Gate"}"><span class="material-symbols-outlined" style="font-size: 20px" translate="no">download</span>Download PDF</button></div><div class="ds-signup-banner-trigger-container"><div class="ds-signup-banner-trigger ds-signup-banner-trigger-control"></div></div><div class="ds-signup-banner ds-signup-banner-control"><div id="ds-signup-banner-close-button"><button class="ds2-5-button ds2-5-button--secondary ds2-5-button--inverse"><span class="material-symbols-outlined" style="font-size: 20px" translate="no">close</span></button></div><div class="ds-signup-banner-ctas"><img src="//a.academia-assets.com/images/academia-logo-capital-white.svg" /><h4 class="ds2-5-heading-serif-sm">Sign up for access to the world's latest research</h4><button class="ds2-5-button ds2-5-button--inverse ds2-5-button--full-width js-swp-download-button" data-signup-modal="{"location":"signup-banner"}">Sign up for free<span class="material-symbols-outlined" style="font-size: 20px" translate="no">arrow_forward</span></button></div><div class="ds-signup-banner-divider"></div><div class="ds-signup-banner-reasons"><div class="ds-signup-banner-reasons-item"><span class="material-symbols-outlined" style="font-size: 24px" translate="no">check</span><span>Get notified about relevant papers</span></div><div class="ds-signup-banner-reasons-item"><span class="material-symbols-outlined" style="font-size: 24px" translate="no">check</span><span>Save papers to use in your research</span></div><div class="ds-signup-banner-reasons-item"><span class="material-symbols-outlined" style="font-size: 24px" translate="no">check</span><span>Join the discussion with peers</span></div><div class="ds-signup-banner-reasons-item"><span class="material-symbols-outlined" style="font-size: 24px" translate="no">check</span><span>Track your impact</span></div></div></div><script>(() => { // Set up signup banner show/hide behavior: // 1. 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Abe</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Neuroscience Research Supplements, 1990</p><p class="ds-related-work--abstract ds2-5-body-sm">TRP channels of the transient receptor potential ion channel superfamily are involved in a wide variety of mechanosensory processes, including touch sensation, pain, blood pressure regulation, bone loading and detection of cerebrospinal fluid flow. However, in many instances it is unclear whether TRP channels are the primary transducers of mechanical force in these processes. In this study, we tested stretch activation of eleven TRP channels from six mammalian subfamilies. We found that these TRP channels were insensitive to short membrane stretches in cellular systems. Furthermore, we purified TRPC6 and demonstrated its insensitivity to stretch in liposomes, an artificial bilayer system free from cellular components. Additionally, we demonstrated that, when expressed in C. elegans neurons, mouse TRPC6 restores the mechanoresponse of a touch insensitive mutant but requires diacylglycerol for activation. These results strongly suggest that the mammalian members of the TRP ion channel family are insensitive to tension induced by cell membrane stretching and, thus, are more likely to be activated by cytoplasmic tethers or downstream components and to act as amplifiers of cellular mechanosensory signaling cascades.</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Stretch-activated ion channels and membrane mechanics","attachmentId":111509260,"attachmentType":"pdf","work_url":"https://www.academia.edu/114961108/Stretch_activated_ion_channels_and_membrane_mechanics","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/114961108/Stretch_activated_ion_channels_and_membrane_mechanics"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="1" data-entity-id="25948536" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/25948536/Mechanosensitive_ion_channels_and_their_mode_of_activation">Mechanosensitive ion channels and their mode of activation</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="49751316" href="https://independent.academia.edu/CatherineBerrier">Catherine Berrier</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Biochimie, 1998</p><p class="ds-related-work--abstract ds2-5-body-sm">~ Mechanosensitive channels are ion channels whose activity is dependent on a mechanical stress on the membrane, They are believed to play a central role in mechanolransduction, the process by which mechanical energy is convened into electrical or chemical signals in biological celh;. Recent progress, which has been made at the molecular level, is presented, and the two currem models of activation of these channels arc discussed (Q Soci6t6 fi'anqaise de biochinfie et biologic mol6culaire / Elsevier, Paris), ion channel / mechanosensitive channel I stretch-activated channel / patch-clamp *Present address: URA-CNRS 1218, Facult6 de Pharmacie, Universit6 Paris-Sud, 5, rue Jean-Baptiste-CI6ment, 92296 Ch;~tenay-Malabry cedex, France.</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Mechanosensitive ion channels and their mode of activation","attachmentId":46303435,"attachmentType":"pdf","work_url":"https://www.academia.edu/25948536/Mechanosensitive_ion_channels_and_their_mode_of_activation","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/25948536/Mechanosensitive_ion_channels_and_their_mode_of_activation"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="2" data-entity-id="13673625" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/13673625/Adaptive_behavior_of_bacterial_mechanosensitive_channels_is_coupled_to_membrane_mechanics">Adaptive behavior of bacterial mechanosensitive channels is coupled to membrane mechanics</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="32880372" href="https://umcp.academia.edu/AndriyAnishkin">Andriy Anishkin</a><span>, </span><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="32819717" href="https://umd.academia.edu/SergeiSukharev">Sergei Sukharev</a></div><p class="ds-related-work--metadata ds2-5-body-xs">The Journal of General Physiology, 2010</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Adaptive behavior of bacterial mechanosensitive channels is coupled to membrane mechanics","attachmentId":45076388,"attachmentType":"pdf","work_url":"https://www.academia.edu/13673625/Adaptive_behavior_of_bacterial_mechanosensitive_channels_is_coupled_to_membrane_mechanics","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/13673625/Adaptive_behavior_of_bacterial_mechanosensitive_channels_is_coupled_to_membrane_mechanics"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="3" data-entity-id="25948543" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/25948543/The_Purified_Mechanosensitive_Channel_TREK_1_Is_Directly_Sensitive_to_Membrane_Tension">The Purified Mechanosensitive Channel TREK-1 Is Directly Sensitive to Membrane Tension</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="49751316" href="https://independent.academia.edu/CatherineBerrier">Catherine Berrier</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Journal of Biological Chemistry, 2013</p><p class="ds-related-work--abstract ds2-5-body-sm">Background: For eukaryotic cells, a direct gating of mechanosensitive channels by membrane tension has not been demonstrated. Results: The mouse TREK-1 was purified and reconstituted in liposomes amenable to patch clamp recording. Conclusion: The channel displayed expected electrophysiological properties, and positive pressure could reversibly close it. Significance: TREK-1, a eukaryotic mechanosensitive channel, is directly sensitive to a modification of membrane tension.</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"The Purified Mechanosensitive Channel TREK-1 Is Directly Sensitive to Membrane Tension","attachmentId":46303440,"attachmentType":"pdf","work_url":"https://www.academia.edu/25948543/The_Purified_Mechanosensitive_Channel_TREK_1_Is_Directly_Sensitive_to_Membrane_Tension","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/25948543/The_Purified_Mechanosensitive_Channel_TREK_1_Is_Directly_Sensitive_to_Membrane_Tension"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="4" data-entity-id="7164160" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/7164160/Two_Families_of_Mechanosensitive_Channel_Proteins">Two Families of Mechanosensitive Channel Proteins</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="12385240" href="https://ashford.academia.edu/fayeblue">faye blue</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Microbiology and Molecular Biology Reviews, 2003</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Two Families of Mechanosensitive Channel Proteins","attachmentId":33795504,"attachmentType":"pdf","work_url":"https://www.academia.edu/7164160/Two_Families_of_Mechanosensitive_Channel_Proteins","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/7164160/Two_Families_of_Mechanosensitive_Channel_Proteins"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="5" data-entity-id="24893356" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/24893356/Contributions_of_the_Different_Extramembranous_Domains_of_the_Mechanosensitive_Ion_Channel_MscL_to_Its_Response_to_Membrane_Tension">Contributions of the Different Extramembranous Domains of the Mechanosensitive Ion Channel MscL to Its Response to Membrane Tension</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="33395898" href="https://independent.academia.edu/BMartinac">Boris Martinac</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Journal of Biological Chemistry, 2000</p><p class="ds-related-work--abstract ds2-5-body-sm">MscL is a mechanosensitive channel that is gated by tension in the membrane bilayer alone. It is a homooligomer of a protein comprising two transmembrane segments connected by an external loop, with the NH 2 and COOH termini located in the cytoplasm. The contributions of the extramembranous domains of the channel to its activity were investigated by specific proteolysis during patch-clamp experiments. Limited proteolysis of the COOH terminus or the NH 2 terminus increased the mechanosensitivity of the channel without changing its conductance. Strikingly, after cleavage of the external loop of each monomer, the channel was still functional, and its mechanosensitivity was increased dramatically, indicating that the loop acts as a spring that resists the opening of the channel and promotes its closure when it is open. These results indicate that the integrity of most of the extramembranous domains is not essential for mechanosensitivity. They suggest that these domains counteract the movement of the transmembrane helices to which they are connected, thus setting the level of sensitivity of the channel to tension.</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Contributions of the Different Extramembranous Domains of the Mechanosensitive Ion Channel MscL to Its Response to Membrane Tension","attachmentId":45213642,"attachmentType":"pdf","work_url":"https://www.academia.edu/24893356/Contributions_of_the_Different_Extramembranous_Domains_of_the_Mechanosensitive_Ion_Channel_MscL_to_Its_Response_to_Membrane_Tension","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/24893356/Contributions_of_the_Different_Extramembranous_Domains_of_the_Mechanosensitive_Ion_Channel_MscL_to_Its_Response_to_Membrane_Tension"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="6" data-entity-id="123588582" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/123588582/Mechanosensitive_Channels_History_Diversity_and_Emerging_Mechanisms">Mechanosensitive Channels: History, Diversity, and Emerging Mechanisms</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="32819717" href="https://umd.academia.edu/SergeiSukharev">Sergei Sukharev</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Biologičeskie membrany, 2023</p><p class="ds-related-work--abstract ds2-5-body-sm">Mechanical forces are inseparable from most cellular functions. Cell division, contraction, and adhesion generate intrinsic forces in the cells, whereas perturbations in the environment such as osmotic shifts, mechanical pressure, shear, or sound represent the external forces that the cells gauge and respond to. Mechanosensitive (MS) ion channels, which are the fastest mechanotransducers, represent a polyphyletic group with vastly diverse structural designs. In this review we briefly outline the history of the field by presenting major findings in a nearly chronological order, describe structural features of different groups, and attempt to illustrate some common physical principles of their gating mechanisms.</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Mechanosensitive Channels: History, Diversity, and Emerging Mechanisms","attachmentId":118009002,"attachmentType":"pdf","work_url":"https://www.academia.edu/123588582/Mechanosensitive_Channels_History_Diversity_and_Emerging_Mechanisms","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/123588582/Mechanosensitive_Channels_History_Diversity_and_Emerging_Mechanisms"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="7" data-entity-id="99097858" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/99097858/The_ion_channels_to_cytoskeleton_connection_as_potential_mechanism_of_mechanosensitivity">The ion channels to cytoskeleton connection as potential mechanism of mechanosensitivity</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="38581739" href="https://unsw.academia.edu/BorisMartinac">Boris Martinac</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Biochimica et Biophysica Acta (BBA) - Biomembranes, 2014</p><p class="ds-related-work--abstract ds2-5-body-sm">As biological force-sensing systems mechanosensitive (MS) ion channels present the best example of coupling molecular dynamics of membrane proteins to the mechanics of the surrounding cell membrane. In animal cells MS channels have over the past two decades been very much in focus of mechanotransduction research. In recent years this helped to raise awareness of basic and medical researchers about the role that abnormal MS channels may play in the pathophysiology of diseases, such as cardiac hypertrophy, atrial fibrillation, muscular dystrophy or polycystic kidney disease. To date a large number of MS channels from organisms of diverse phylogenetic origins have been identified at the molecular level; however, the structure of only few of them has been determined. Although their function has extensively been studied in a great variety of cells and tissues by different experimental approaches it is, with exception of bacterial MS channels, very little known about how these channels sense mechanical force and which cellular components may contribute to their function. By focusing on MS channels found in animal cells this article discusses the ways in which the connections between cytoskeleton and ion channels may contribute to mechanosensory transduction in these cells. This article is part of a Special Issue entitled: Reciprocal influences between cell cytoskeleton and membrane channels, receptors and transporters. This article is part of a Special Issue entitled: Reciprocal influences between cell cytoskeleton and membrane channels, receptors and transporters.</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"The ion channels to cytoskeleton connection as potential mechanism of mechanosensitivity","attachmentId":100275025,"attachmentType":"pdf","work_url":"https://www.academia.edu/99097858/The_ion_channels_to_cytoskeleton_connection_as_potential_mechanism_of_mechanosensitivity","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/99097858/The_ion_channels_to_cytoskeleton_connection_as_potential_mechanism_of_mechanosensitivity"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="8" data-entity-id="53051098" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/53051098/Stretch_Activated_Ion_Channels_What_Are_They">Stretch-Activated Ion Channels: What Are They?</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="34703212" href="https://independent.academia.edu/FrederickSachs">Frederick Sachs</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Physiology, 2010</p><p class="ds-related-work--abstract ds2-5-body-sm">Mechanosensitive ion channels (MSCs) exist in all cells, but mechanosensitivity is a phenotype not a genotype. Specialized mechanoreceptors such as the hair cells of the cochlea require elaborate mechanical impedance matching to couple the channels to the external stress. In contrast, MSCs in nonspecialized cells appear activated by stress in the bilayer local to the channel—within about three lipids. Local mechanical stress can be produced by far-field tension, amphipaths, phase separations, the cytoskeleton, the extracellular matrix, and the adhesion energy between the membrane and a patch pipette. Understanding MSC function requires under standing the stimulus.</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Stretch-Activated Ion Channels: What Are They?","attachmentId":70017200,"attachmentType":"pdf","work_url":"https://www.academia.edu/53051098/Stretch_Activated_Ion_Channels_What_Are_They","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/53051098/Stretch_Activated_Ion_Channels_What_Are_They"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="9" data-entity-id="118343006" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/118343006/Clustering_and_Functional_Interaction_of_MscL_Channels">Clustering and Functional Interaction of MscL Channels</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="32693741" href="https://independent.academia.edu/AnneUlrich">Anne Ulrich</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Biophysical Journal, 2010</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Clustering and Functional Interaction of MscL Channels","attachmentId":113992598,"attachmentType":"pdf","work_url":"https://www.academia.edu/118343006/Clustering_and_Functional_Interaction_of_MscL_Channels","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/118343006/Clustering_and_Functional_Interaction_of_MscL_Channels"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div></div></div><div class="ds-sticky-ctas--wrapper js-loswp-sticky-ctas hidden"><div class="ds-sticky-ctas--grid-container"><div class="ds-sticky-ctas--container"><button class="ds2-5-button js-swp-download-button" data-signup-modal="{"location":"continue-reading-button--sticky-ctas","attachmentId":117986231,"attachmentType":"pdf","workUrl":null}">See full PDF</button><button class="ds2-5-button ds2-5-button--secondary js-swp-download-button" data-signup-modal="{"location":"download-pdf-button--sticky-ctas","attachmentId":117986231,"attachmentType":"pdf","workUrl":null}"><span class="material-symbols-outlined" style="font-size: 20px" translate="no">download</span>Download PDF</button></div></div></div><div class="ds-below-fold--grid-container"><div class="ds-work--container js-loswp-embedded-document"><div class="attachment_preview" data-attachment="Attachment_117986231" style="display: none"><div class="js-scribd-document-container"><div class="scribd--document-loading js-scribd-document-loader" style="display: block;"><img alt="Loading..." src="//a.academia-assets.com/images/loaders/paper-load.gif" /><p>Loading Preview</p></div></div><div style="text-align: center;"><div class="scribd--no-preview-alert js-preview-unavailable"><p>Sorry, preview is currently unavailable. 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