<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE root>
<article xmlns:mml="http://www.w3.org/1998/Math/MathML" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xmlns:ali="http://www.niso.org/schemas/ali/1.0/" article-type="research-article" dtd-version="1.2" xml:lang="en"><front><journal-meta><journal-id journal-id-type="publisher-id">Membrane and Cell Biology</journal-id><journal-title-group><journal-title xml:lang="en">Membrane and Cell Biology</journal-title><trans-title-group xml:lang="ru"><trans-title>Биологические мембраны</trans-title></trans-title-group></journal-title-group><issn publication-format="print">0233-4755</issn><issn publication-format="electronic">3034-5219</issn><publisher><publisher-name xml:lang="en">The Russian Academy of Sciences</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="publisher-id">405976</article-id><article-id pub-id-type="doi">10.7868/S3034521926010031</article-id><article-categories><subj-group subj-group-type="toc-heading" xml:lang="en"><subject>Articles</subject></subj-group><subj-group subj-group-type="toc-heading" xml:lang="ru"><subject>СТАТЬИ</subject></subj-group><subj-group subj-group-type="article-type"><subject>Research Article</subject></subj-group></article-categories><title-group><article-title xml:lang="en">The Role of Lipid Rafts in the Regulation of Piezo1 Channels in C2C12 Myoblasts</article-title><trans-title-group xml:lang="ru"><trans-title>Роль липидных рафтов в регуляции каналов Piezo1 в миобластах C2C12</trans-title></trans-title-group></title-group><contrib-group><contrib contrib-type="author"><name-alternatives><name xml:lang="en"><surname>Bildyug</surname><given-names>N. B</given-names></name><name xml:lang="ru"><surname>Бильдюг</surname><given-names>Н. Б</given-names></name></name-alternatives><email>nbildyug@gmail.com</email><xref ref-type="aff" rid="aff1"/></contrib><contrib contrib-type="author"><name-alternatives><name xml:lang="en"><surname>Vasileva</surname><given-names>V. Y</given-names></name><name xml:lang="ru"><surname>Васильева</surname><given-names>В. Ю</given-names></name></name-alternatives><email>-</email><xref ref-type="aff" rid="aff1"/></contrib><contrib contrib-type="author"><name-alternatives><name xml:lang="en"><surname>Shenkman</surname><given-names>B. S</given-names></name><name xml:lang="ru"><surname>Шенкман</surname><given-names>Б. С</given-names></name></name-alternatives><email>-</email><xref ref-type="aff" rid="aff2"/></contrib><contrib contrib-type="author"><name-alternatives><name xml:lang="en"><surname>Mirzoev</surname><given-names>T. M</given-names></name><name xml:lang="ru"><surname>Мирзоев</surname><given-names>Т. М</given-names></name></name-alternatives><email>tmirzoev@yandex.ru</email><xref ref-type="aff" rid="aff2"/></contrib></contrib-group><aff-alternatives id="aff1"><aff><institution xml:lang="en">Institute of Cytology of the Russian Academy of Sciences</institution></aff><aff><institution xml:lang="ru">Институт цитологии РАН</institution></aff></aff-alternatives><aff-alternatives id="aff2"><aff><institution xml:lang="en">Institute of Biomedical Problems of the Russian Academy of Sciences</institution></aff><aff><institution xml:lang="ru">Институт медико-биологических проблем РАН</institution></aff></aff-alternatives><pub-date date-type="pub" iso-8601-date="2026-02-15" publication-format="electronic"><day>15</day><month>02</month><year>2026</year></pub-date><volume>43</volume><issue>1</issue><issue-title xml:lang="en">VOL 43, NO1 ()</issue-title><issue-title xml:lang="ru">ТОМ 43, №1 ()</issue-title><fpage>26</fpage><lpage>39</lpage><history><date date-type="received" iso-8601-date="2026-04-03"><day>03</day><month>04</month><year>2026</year></date></history><permissions><copyright-statement xml:lang="en">Copyright ©; 2026, Russian Academy of Sciences</copyright-statement><copyright-statement xml:lang="ru">Copyright ©; 2026, Российская академия наук</copyright-statement><copyright-year>2026</copyright-year><copyright-holder xml:lang="en">Russian Academy of Sciences</copyright-holder><copyright-holder xml:lang="ru">Российская академия наук</copyright-holder><ali:free_to_read xmlns:ali="http://www.niso.org/schemas/ali/1.0/" start_date="2027-02-15"/></permissions><self-uri xlink:href="https://journals.rcsi.science/0233-4755/article/view/405976">https://journals.rcsi.science/0233-4755/article/view/405976</self-uri><abstract xml:lang="en"><p>Piezo1 channels are mechanically activated (MA) cation channels that play an important role in skeletal muscle physiology. However, the specific mechanisms of Piezo1 regulation in skeletal muscle are not yet fully understood. At the same time, the activity of different ion channels is known to be dependent on lipid rafts, which are dynamic microdomains in the cell membrane enriched in sphingolipids and cholesterol. Therefore, the aim of this study was to evaluate the role of lipid rafts in the muscle-specific regulation of Piezo1 using a cholesterol-removing agent, methyl-beta-cyclodextrin (MβCD), and the sphingolipid sphingosine-1-phosphate (S1P) in a C2C12 myoblast model. Fluorescence labeling and intracellular calcium measurements demonstrated that the disruption of lipid rafts with MβCD resulted in disassembly of the initially present actin cytoskeleton in C2C12 cells and decreased Piezo1-mediated Ca<sup>2+</sup> influx into the cells. In contrast, stimulation of myoblasts with S1P resulted in increased formation of lipid rafts and actin stress fibers, as well as enhanced Ca<sup>2+</sup> influx through Piezo1 channels. These findings suggest the involvement of lipid rafts in the regulation of Piezo1 activity in C2C12 myoblasts, which may be mediated by lipid raft components themselves and/or by lipid raft-induced rearrangements of the actin cytoskeleton.</p></abstract><trans-abstract xml:lang="ru"><p>Каналы Piezo1 представляют собой механоактивируемые (МА) катионные каналы, которые играют важную роль в физиологии скелетных мышц. Однако конкретные механизмы регуляции Piezo1 в мышечной ткани остаются не изученными. В то же время известно, что активность различных ионных каналов зависит от липидных рафтов, которые представляют собой динамические микродомены плазматической мембраны клеток, обогащенные сфинголипидами и холестерином. Целью данного исследования являлась оценка роли липидных рафтов в регуляции Piezo1 в скелетных мышцах на модели мышиных миобластов C2C12 с использованием холестерин-секвестрирующего агента – метил-бета-циклодекстрина (МЦД) – и сфинголипида сфингозин-1-фосфата (S1P). Результаты флуоресцентного окрашивания и измерения внутриклеточного кальция показали, что разрушение липидных рафтов с помощью МЦД приводило к разборке активного цитоскелета в клетках C2C12 и снижению опосредованного Piezo1 притока Ca<sup>2+</sup>. S1P, напротив, стимулировал образование липидных рафтов и активных стресс-фибрилл в этих клетках и вызывал усиление притока Ca<sup>2+</sup> через каналы Piezo1. Полученные результаты свидетельствуют об участии липидных рафтов в регуляции активности Piezo1 в миобластах C2C12, которая может быть опосредована компонентами липидных рафтов и/или зависимой от липидных рафтов перестройкой активного цитоскелета.</p></trans-abstract><kwd-group xml:lang="en"><kwd>Piezo1</kwd><kwd>myoblasts</kwd><kwd>lipid rafts</kwd><kwd>actin cytoskeleton</kwd></kwd-group><kwd-group xml:lang="ru"><kwd>Piezo1</kwd><kwd>миобласты</kwd><kwd>липидные рафты</kwd><kwd>актиновый цитоскелет</kwd></kwd-group><funding-group><funding-statement xml:lang="ru">Данное исследование поддержано Российским научным фондом (РНФ, грант № 22-75-10046).</funding-statement></funding-group></article-meta></front><body></body><back><ref-list><ref id="B1"><label>1.</label><mixed-citation>Kefauver J.M., Ward A.B., Patapoutian A. 2020. Discoveries in structure and physiology of mechanically activated ion channels. Nature. 587 (7835), 567–576. https://www.doi.org/10.1038/s41586-020-2933-1</mixed-citation></ref><ref id="B2"><label>2.</label><mixed-citation>Poole K. 2022. The diverse physiological functions of mechanically activated ion channels in mammals. Annu. Rev. Physiol. 84, 307–329. https://www.doi.org/10.1146/annurev-physiol-060721-100935</mixed-citation></ref><ref id="B3"><label>3.</label><mixed-citation>Coste B., Mathur J., Schmidt M., Earley T.J., Ranade S., Petrus M.J., Dubin A.E., Patapoutian A. 2010. Piezo1 and Piezo2 are essential components of distinct mechanically activated cation channels. Science. 330 (6000), 55–60. https://www.doi.org/10.1126/science.1193270</mixed-citation></ref><ref id="B4"><label>4.</label><mixed-citation>Woo S.H., Lukacs V., de Nooij J.C., Zaytseva D., Criddle C.R., Francisco A., Jessell T.M., Wilkinson K.A., Patapoutian A. 2015. Piezo2 is the principal mechanotransduction channel for proprioception. Nat. Neurosci. 18 (12), 1756–1762. https://www.doi.org/10.1038/nn.4162</mixed-citation></ref><ref id="B5"><label>5.</label><mixed-citation>Tsuchiya M., Hara Y., Okuda M., Itoh K., Nishioka R., Shiomi A., Nagao K., Mori M., Mori Y., Ikenouchi J., Suzuki R., Tanaka M., Ohwada T., Aoki J., Kanagawa M., Toda T., Nagata Y., Matsuda R., Takayama Y., Tominaga M., Umeda M. 2018. Cell surface flip-flop of phosphatidylserine is critical for PIEZO1-mediated myotube formation. Nat. Commun. 9 (1), 2049.</mixed-citation></ref><ref id="B6"><label>6.</label><mixed-citation>Bosutti A., Giniatullin A., Odnoshivkina Y., Giudice L., Malm T., Sciancalepore M., Giniatullin R., D’Andrea P., Lorenzon P., Bernareggi A. 2021. “Time window” effect of Yoda1-evoked Piezo1 channel activity during mouse skeletal muscle differentiation. Acta. Physiol. (Oxf). 233 (4), e13702. https://www.doi.org/10.1111/apha.13702</mixed-citation></ref><ref id="B7"><label>7.</label><mixed-citation>Ortuste Quiroga H.P., Ganassi M., Yokoyama S., Nakamura K., Yamashita T., Raimbach D., Hagiwara A., Harrington O., Breach-Teji J., Asakura A., Suzuki Y., Tominaga M., Zammit P.S., Goto K. 2022. Fine-tuning of Piezo1 expression and activity ensures efficient myoblast fusion during skeletal myogenesis. Cells. 11 (3). https://www.doi.org/10.3390/cells11030393</mixed-citation></ref><ref id="B8"><label>8.</label><mixed-citation>Hirata Y., Nomura K., Kato D., Tachibana Y., Niikura T., Uchiyama K., Hosooka T., Fukui T., Oe K., Kuroda R., Hara Y., Adachi T., Shibasaki K., Wake H., Ogawa W. 2022. A Piezo1/KLF15/IL-6 axis mediates immobilization-induced muscle atrophy. J. Clin. Invest. 132 (10), 1–13. https://www.doi.org/10.1172/JCI154611</mixed-citation></ref><ref id="B9"><label>9.</label><mixed-citation>Mirzoev T.M. 2023. The emerging role of Piezo1 channels in skeletal muscle physiology. Biophys. Rev. 15 (5), 1171–1184. https://www.doi.org/10.1007/s12551-023-01154-6</mixed-citation></ref><ref id="B10"><label>10.</label><mixed-citation>Sergeeva K.V., Tyganov S.A., Zaripova K.A., Shenkman B.S. 2025. Effect of mechanically activated calcium channels on passive stiffness and contraction amplitude of slow muscle. J. Evol. Biochem. Physiol. 61 (1), 115–121. https://www.doi.org/10.1134/S0022093025010089</mixed-citation></ref><ref id="B11"><label>11.</label><mixed-citation>Syeda R., Florendo M.N., Cox C.D., Kefauver J.M., Santos J.S., Martinac B., Patapoutian A. 2016. Piezo1 channels are inherently mechanosensitive. Cell Rep. 17 (7), 1739–1746. https://www.doi.org/10.1016/j.celrep.2016.10.033</mixed-citation></ref><ref id="B12"><label>12.</label><mixed-citation>Vasileva V., Chubinskiy-Nadezhdin V. 2023. Regulation of PIEZO1 channels by lipids and the structural components of extracellular matrix/cell cytoskeleton. J. Cell Physiol. 238 (5), 918–930. https://www.doi.org/10.1002/jcp.31001</mixed-citation></ref><ref id="B13"><label>13.</label><mixed-citation>George K.S., Wu S. 2012. Lipid raft: A floating island of death or survival. Toxicol. Appl. Pharmacol. 259 (3), 311–319. https://www.doi.org/10.1016/j.taap.2012.01.007</mixed-citation></ref><ref id="B14"><label>14.</label><mixed-citation>Simons K., Ikonen E. 1997. Functional rafts in cell membranes. Nature. 387 (6633), 569–572. https://www.doi.org/10.1038/42408</mixed-citation></ref><ref id="B15"><label>15.</label><mixed-citation>Anselmo S., Bonaccorso E., Gangemi C., Sancataldo G., Conti Nibali V., D’Angelo G. 2025. Lipid Rafts in signalling, diseases, and infections: What can be learned from fluorescence techniques? Membranes (Basel). 15 (1), 6. https://www.doi.org/10.3390/membranes15010006</mixed-citation></ref><ref id="B16"><label>16.</label><mixed-citation>D’Aprile C., Prioni S., Mauri L., Prinetti A., Grassi S. 2021. Lipid rafts as platforms for sphingosine 1-phosphate metabolism and signalling. Cell Signal. 80, 109929. https://www.doi.org/10.1016/j.cellsig.2021.109929</mixed-citation></ref><ref id="B17"><label>17.</label><mixed-citation>Sassoli C., Pierucci F., Zecchi-Orlandini S., Meacci E. 2019. Sphingosine 1-phosphate (S1P)/S1P receptor signaling and mechanotransduction: implications for intrinsic tissue repair/regeneration. Int. J. Mol. Sci. 20 (22), 5545. https://www.doi.org/10.3390/ijms20225545</mixed-citation></ref><ref id="B18"><label>18.</label><mixed-citation>Zhao J., Singleton P.A., Brown M.E., Dudek S.M., Garcia J.G. 2009. Phosphotyrosine protein dynamics in cell membrane rafts of sphingosine-1-phosphatestimulated human endothelium: role in barrier enhancement. Cell Signal. 21 (12), 1945–1960. https://www.doi.org/10.1016/j.cellsig.2009.09.002</mixed-citation></ref><ref id="B19"><label>19.</label><mixed-citation>Zajchowski L.D., Robbins S.M. 2002. Lipid rafts and little caves. Compartmentalized signalling in membrane microdomains. Eur. J. Biochem. 269 (3), 737–752. https://www.doi.org/10.1046/j.0014-2956.2001.02715.x</mixed-citation></ref><ref id="B20"><label>20.</label><mixed-citation>Burow P., Klapperstuck M., Markwardt F. 2015. Activation of ATP secretion via volume-regulated anion channels by sphingosine-1-phosphate in RAW macrophages. Pflugers Arch. 467 (6), 1215–1226. https://www.doi.org/10.1007/s00424-014-1561-8</mixed-citation></ref><ref id="B21"><label>21.</label><mixed-citation>Beverley K.M., Levitan I. 2024. Cholesterol regulation of mechanosensitive ion channels. Front. Cell Dev. Biol. 12, 1352259. https://www.doi.org/10.3389/fcell.2024.1352259</mixed-citation></ref><ref id="B22"><label>22.</label><mixed-citation>Romanenko V.G., Fang Y., Byfield F., Travis A.J., Vandenberg C.A., Rothblat G.H., Levitan I. 2004. Cholesterol sensitivity and lipid raft targeting of Kir2.1 channels. Biophys. J. 87 (6), 3850–3861. https://www.doi.org/10.1529/biophysj.104.043273</mixed-citation></ref><ref id="B23"><label>23.</label><mixed-citation>Amsalem M., Poilbout C., Ferracci G., Delmas P., Padilla F. 2018. Membrane cholesterol depletion as a trigger of Nav1.9 channel-mediated inflammatory pain. EMBO J. 37 (8), e97349. https://www.doi.org/10.15252/embj.201797349</mixed-citation></ref><ref id="B24"><label>24.</label><mixed-citation>Chong J., De Vecchis D., Hyman A.J., Povstyan O.V., Ludlow M.J., Shi J., Beech D.J., Kalli A.C. 2021. Modeling of full-length Piezo1 suggests importance of the proximal N-terminus for dome structure. Biophys. J. 120 (8), 1343–1356. https://www.doi.org/10.1016/j.bpj.2021.02.003</mixed-citation></ref><ref id="B25"><label>25.</label><mixed-citation>Greenlee J.D., Liu K., Lopez-Cavestany M., King M.R. 2022. Piezo1 mechano-activation is augmented by resveratrol and differs between colorectal cancer cells of primary and metastatic origin. Molecules. 27 (17), 5430. https://www.doi.org/10.3390/molecules27175430</mixed-citation></ref><ref id="B26"><label>26.</label><mixed-citation>Cibelli A., Ballesteros-Gomez D., McCutcheon S., Yang G.L., Bispo A., Krawchuk M., Piedra G., Spray D.C. 2024. Astrocytes sense glymphatic-level shear stress through the interaction of sphingosine-1-phosphate with Piezo1. iScience. 27 (6), 110069. https://www.doi.org/10.1016/j.isci.2024.110069</mixed-citation></ref><ref id="B27"><label>27.</label><mixed-citation>Kang H., Hong Z., Zhong M., Klomp J., Bayless K.J., Mehta D., Karginov A.V., Hu G., Malik A.B. 2019. Piezo1 mediates angiogenesis through activation of MT1-MMP signaling. Am. J. Physiol. Cell Physiol. 316 (1), C92–C103. https://www.doi.org/10.1152/ajpcell.00346.2018</mixed-citation></ref><ref id="B28"><label>28.</label><mixed-citation>Chubinskiy-Nadezhdin V.I., Vasileva V.Y., Vassilieva I.O., Sudarikova A.V., Morachevskaya E.A., Negulyaev Y.A. 2019. Agonist-induced Piezo1 activation suppresses migration of transformed fibroblasts. Biochem. Biophys. Res. Commun. 514 (1), 173–179. https://www.doi.org/10.1016/j.bbrc.2019.04.139</mixed-citation></ref><ref id="B29"><label>29.</label><mixed-citation>Vasileva V.Y., Lysikova D.V., Sudarikova A.V., Khairullina Z.M., Kirillova P.I., Morachevskaya E.A., Chubinskiy-Nadezhdin V.I. 2024. Functional characterization of native Piezo1 as calcium and magnesium influx pathway in human myeloid leukemia cells. J. Cell Physiol. 239 (11), e31371. https://www.doi.org/10.1002/jcp.31371</mixed-citation></ref><ref id="B30"><label>30.</label><mixed-citation>Chubinskiy-Nadezhdin V., Semenova S., Vasileva V., Shatrova A., Pugovkina N., Negulyaev Y. 2022. Store-Operated Ca(2+) entry contributes to Piezo1- induced Ca(2+) increase in human endometrial stem cells. Int. J. Mol. Sci. 23 (7), 3763. https://www.doi.org/10.3390/ijms23073763</mixed-citation></ref><ref id="B31"><label>31.</label><mixed-citation>Vasileva V.Y., Chubinskiy-Nadezhdin V.I. 2022. Local mechano-dependent calcium influx controls the activity of calcium-dependent potassium channels of big and small conductance in human lymphoma cells. Cell Tiss. Biol. 16 (2), 150–156. https://www.doi.org/10.1134/S1990519X22020110</mixed-citation></ref><ref id="B32"><label>32.</label><mixed-citation>Syeda R., Xu J., Dubin A.E., Coste B., Mathur J., Huynh T., Matzen J., Lao J., Tully D.C., Engels I.H., Petrassi H.M., Schumacher A.M., Montal M., Bandell M., Patapoutian A. 2015. Chemical activation of the mechanotransduction channel Piezo1. Elife. 4, e07369. https://www.doi.org/10.7554/eLife.07369</mixed-citation></ref><ref id="B33"><label>33.</label><mixed-citation>Qi Y., Andolfi L., Frattini F., Mayer F., Lazzarino M., Hu J. 2015. Membrane stiffening by STOML3 facilitates mechanosensation in sensory neurons. Nat. Commun. 6, 8512. https://www.doi.org/10.1038/ncomms9512</mixed-citation></ref><ref id="B34"><label>34.</label><mixed-citation>Poole K., Herget R., Lapatsina L., Ngo H.D., Lewin G.R. 2014. Tuning Piezo ion channels to detect molecular-scale movements relevant for fine touch. Nat. Commun. 5, 3520. https://www.doi.org/10.1038/ncomms4520</mixed-citation></ref><ref id="B35"><label>35.</label><mixed-citation>Ridone P., Pandzic E., Vassalli M., Cox C.D., Macmillan A., Gottlieb P.A., Martinac B. 2020. Disruption of membrane cholesterol organization impairs the activity of PIEZO1 channel clusters. J. Gen Physiol. 152 (8), e201912515. https://www.doi.org/10.1085/jgp.201912515</mixed-citation></ref><ref id="B36"><label>36.</label><mixed-citation>Chubinskiy-Nadezhdin V.I., Efremova T.N., Khaitlina S.Y., Morachevskaya E.A. 2013. Functional impact of cholesterol sequestration on actin cytoskeleton in normal and transformed fibroblasts. Cell Biol. Int. 37 (6), 617–623. https://www.doi.org/10.1002/cbin.10079</mixed-citation></ref><ref id="B37"><label>37.</label><mixed-citation>Levina N.N., Lew R.R., Heath I.B. 1994. Cytoskeletal regulation of ion channel distribution in the tip-growing organism Saprolegnia ferax. J. Cell Sci. 107 (Pt 1), 127–134. https://www.doi.org/10.1242/jcs.107.1.127</mixed-citation></ref><ref id="B38"><label>38.</label><mixed-citation>Smith P.R., Saccomani G., Joe E.H., Angelides K.J., Benos D.J. 1991. Amiloride-sensitive sodium channel is linked to the cytoskeleton in renal epithelial cells. Proc. Natl. Acad. Sci. USA. 88 (16), 6971–6975. https://www.doi.org/10.1073/pnas.88.16.6971</mixed-citation></ref><ref id="B39"><label>39.</label><mixed-citation>Shumilina E.V., Negulyaev Y.A., Morachevskaya E.A., Hinssen H., Khaitlina S.Y. 2003. Regulation of sodium channel activity by capping of actin filaments. Mol. Biol. Cell. 14 (4), 1709–1716. https://www.doi.org/10.1091/mbc.e02-09-0622</mixed-citation></ref><ref id="B40"><label>40.</label><mixed-citation>Cantiello H.F. 1995. Role of the actin cytoskeleton on epithelial Na+ channel regulation. Kidney Int. 48 (4), 970–984. https://www.doi.org/10.1038/ki.1995.379</mixed-citation></ref><ref id="B41"><label>41.</label><mixed-citation>Schwiebert E.M., Mills J.W., Stanton B.A. 1994. Actin-based cytoskeleton regulates a chloride channel and cell volume in a renal cortical collecting duct cell line. J. Biol. Chem. 269 (10), 7081–7089.</mixed-citation></ref><ref id="B42"><label>42.</label><mixed-citation>Negulyaev Y.A., Vedernikova E.A., Maximov A.V. 1996. Disruption of actin filaments increases the activity of sodium-conducting channels in human myeloid leukemia cells. Mol. Biol. Cell. 7 (12), 1857–1864. https://www.doi.org/10.1091/mbc.7.12.1857</mixed-citation></ref><ref id="B43"><label>43.</label><mixed-citation>Negulyaev Y.A., Khaitlina S.Y., Hinssen H., Shumilina E.V., Vedernikova E.A. 2000. Sodium channel activity in leukemia cells is directly controlled by actin polymerization. J. Biol. Chem. 275 (52), 40933–40937. https://www.doi.org/10.1074/jbc.M008219200</mixed-citation></ref><ref id="B44"><label>44.</label><mixed-citation>Wang W.H., Cassola A., Giebisch G. 1994. Involvement of actin cytoskeleton in modulation of apical K channel activity in rat collecting duct. Am. J. Physiol. 267 (4 Pt 2), F592–F598. https://www.doi.org/10.1152/ajprenal.1994.267.4.F592</mixed-citation></ref><ref id="B45"><label>45.</label><mixed-citation>Staruschenko A., Negulyaev Y.A., Morachevskaya E.A. 2005. Actin cytoskeleton disassembly affects conductive properties of stretch-activated cation channels in leukaemia cells. Biochim. Biophys. Acta. 1669 (1), 53–60. https://www.doi.org/10.1016/j.bbamem.2005.02.013</mixed-citation></ref><ref id="B46"><label>46.</label><mixed-citation>Kamkin A., Kiseleva I., Isenberg G. 2003. Ion selectivity of stretch-activated cation currents in mouse ventricular myocytes. Pflugers Arch. 446 (2), 220–231. https://www.doi.org/10.1007/s00424-003-1018-y</mixed-citation></ref><ref id="B47"><label>47.</label><mixed-citation>Ito S., Suki B., Kume H., Numaguchi Y., Ishii M., Iwaki M., Kondo M., Naruse K., Hasegawa Y., Sokabe M. 2010. Actin cytoskeleton regulates stretch-activated Ca2+ influx in human pulmonary microvascular endothelial cells. Am. J. Respir. Cell Mol. Biol. 43 (1), 26–34. https://www.doi.org/10.1165/rcmb.2009-0073OC</mixed-citation></ref><ref id="B48"><label>48.</label><mixed-citation>Srinivasan Y., Elmer L., Davis J., Bennett V., Angelides K. 1988. Ankyrin and spectrin associate with voltage-dependent sodium channels in brain. Nature. 333 (6169), 177–180. https://www.doi.org/10.1038/333177a0</mixed-citation></ref><ref id="B49"><label>49.</label><mixed-citation>Wang J., Jiang J., Yang X., Zhou G., Wang L., Xiao B. 2022. Tethering Piezo channels to the actin cytoskeleton for mechanogating via the cadherinbeta-catenin mechanotransduction complex. Cell Rep. 38 (6), 110342. https://www.doi.org/10.1016/j.celrep.2022.110342</mixed-citation></ref><ref id="B50"><label>50.</label><mixed-citation>Gottlieb P.A., Bae C., Sachs F. 2012. Gating the mechanical channel Piezo1: A comparison between whole-cell and patch recording. Channels (Austin). 6 (4), 282–289. https://www.doi.org/10.4161/chan.21064</mixed-citation></ref><ref id="B51"><label>51.</label><mixed-citation>Cox C.D., Bae C., Ziegler L., Hartley S., Nikolova-Krstevski V., Rohde P.R., Ng C.A., Sachs F., Gottlieb P.A., Martinac B. 2016. Removal of the mechanoprotective influence of the cytoskeleton reveals PIEZO1 is gated by bilayer tension. Nat. Commun. 7, 10366. https://www.doi.org/10.1038/ncomms10366</mixed-citation></ref><ref id="B52"><label>52.</label><mixed-citation>Retailleau K., Duprat F., Arhatte M., Ranade S.S., Peyronnet R., Martins J.R., Jodar M., Moro C., Offermanns S., Feng Y., Demolombe S., Patel A., Honore E. 2015. Piezo1 in smooth muscle cells is involved in hypertension-dependent arterial remodeling. Cell Rep. 13 (6), 1161–1171. https://www.doi.org/10.1016/j.celrep.2015.09.072</mixed-citation></ref><ref id="B53"><label>53.</label><mixed-citation>Sbrana F., Sassoli C., Meacci E., Nosi D., Squecco R., Paternostro F., Tiribilli B., Zecchi-Orlandini S., Francini F., Formigli L. 2008. Role for stress fiber contraction in surface tension development and stretch-activated channel regulation in C2C12 myoblasts. Am. J. Physiol Cell Physiol. 295 (1), C160–C172. https://www.doi.org/10.1152/ajpcell.00014.2008</mixed-citation></ref><ref id="B54"><label>54.</label><mixed-citation>Formigli L., Meacci E., Sassoli C., Chellini F., Giannini R., Quercioli F., Tiribilli B., Squecco R., Bruni P., Francini F., Zecchi-Orlandini S. 2005. Sphingosine 1-phosphate induces cytoskeletal reorganization in C2C12 myoblasts: physiological relevance for stress fibres in the modulation of ion current through stretch-activated channels. J. Cell Sci. 118 (Pt 6), 1161–1171. https://www.doi.org/10.1242/jcs.01695</mixed-citation></ref><ref id="B55"><label>55.</label><mixed-citation>Narumiya S., Ishizaki T., Watanabe N. 1997. Rho effectors and reorganization of actin cytoskeleton. FEBS Lett. 410 (1), 68–72. https://www.doi.org/10.1016/s0014-5793(97)00317-7</mixed-citation></ref><ref id="B56"><label>56.</label><mixed-citation>Mack C.P., Somlyo A.V., Hautmann M., Somlyo A.P., Owens G.K. 2001. Smooth muscle differentiation marker gene expression is regulated by RhoA-mediated actin polymerization. J. Biol. Chem. 276 (1), 341–347. https://www.doi.org/10.1074/jbc.M005505200</mixed-citation></ref><ref id="B57"><label>57.</label><mixed-citation>Gonda K., Okamoto H., Takuwa N., Yatomi Y., Okazaki H., Sakurai T., Kimura S., Sillard R., Harii K., Takuwa Y. 1999. The novel sphingosine 1-phosphate receptor AGR16 is coupled via pertussis toxin-sensitive and -insensitive G-proteins to multiple signalling pathways. Biochem. J. 337 (Pt 1) (Pt 1), 67–75.</mixed-citation></ref><ref id="B58"><label>58.</label><mixed-citation>Okamoto H., Takuwa N., Yatomi Y., Gonda K., Shigematsu H., Takuwa Y. 1999. EDG3 is a functional receptor specific for sphingosine 1-phosphate and sphingosylphosphorylcholine with signaling characteristics distinct from EDG1 and AGR16. Biochem. Biophys. Res. Commun. 260 (1), 203–208. https://www.doi.org/10.1006/bbrc.1999.0886</mixed-citation></ref><ref id="B59"><label>59.</label><mixed-citation>Blaho V.A., Hla T. 2014. An update on the biology of Sphingosine 1-Phosphate receptors. J. Lipid Res. 55, 1596–1608. https://www.doi.org/10.1194/jlr.R046300</mixed-citation></ref><ref id="B60"><label>60.</label><mixed-citation>Donati C., Bruni P. 2006. Sphingosine 1-phosphate regulates cytoskeleton dynamics: implications in its biological response. Biochim. Biophys. Acta. 1758 (12), 2037–2048. https://www.doi.org/10.1016/j.bbamem.2006.06.015</mixed-citation></ref><ref id="B61"><label>61.</label><mixed-citation>Meacci E., Vasta V., Donati C., Farnararo M., Bruni P. 1999. Receptor-mediated activation of phospholipase D by sphingosine 1-phosphate in skeletal muscle C2C12 cells. A role for protein kinase C. FEBS Lett. 457 (2), 184–188. https://www.doi.org/10.1016/s0014-5793(99)01033-9</mixed-citation></ref><ref id="B62"><label>62.</label><mixed-citation>Becciolini L., Meacci E., Donati C., Cencetti F., Rapizzi E., Bruni P. 2006. Sphingosine 1-phosphate inhibits cell migration in C2C12 myoblasts. Biochim. Biophys. Acta. 1761 (1), 43–51. https://www.doi.org/10.1016/j.bbalip.2006.01.006</mixed-citation></ref><ref id="B63"><label>63.</label><mixed-citation>Sassoli C., Pierucci F., Zecchi-Orlandini S., Meacci E. 2019. Sphingosine 1-Phosphate (S1P)/S1P Receptor signaling and mechanotransduction: Implications for intrinsic tissue repair/regeneration. Int. J. Mol. Sci. 20 (22), 5545. https://www.doi.org/10.3390/ijms20225545</mixed-citation></ref><ref id="B64"><label>64.</label><mixed-citation>Cencetti F., Bernacchioni C., Tonelli F., Roberts E., Donati C., Bruni P. 2013. TGFβ1 evokes myoblast apoptotic response via a novel signaling pathway involving S1P4 transactivation upstream of Rho-kinase-2 activation. FASEB J. 27, 4532–4546. https://www.doi.org/10.1096/fj.13-228528</mixed-citation></ref><ref id="B65"><label>65.</label><mixed-citation>Chao P.C., Sachs F. 2021. Membrane tension. Curr. Top Membr. 88, 189–203. https://www.doi.org/10.1016/bs.ctm.2021.09.002</mixed-citation></ref></ref-list></back></article>
