TRPM4 is a novel component of the adhesome required for focal adhesion disassembly, migration and contractility

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dc.contributor.authorCáceres, Mónica
dc.contributor.authorOrtiz, Liliana
dc.contributor.authorRecabarren, Tatiana
dc.contributor.authorRomero, Anibal
dc.contributor.authorColombo, Alicia
dc.contributor.authorLeiva-Salcedo, Elías
dc.contributor.authorVarela, Diego
dc.contributor.authorRivas, José
dc.contributor.authorSilva, Ian
dc.contributor.authorMorales, Diego
dc.contributor.authorCampusano, Camilo
dc.contributor.authorAlmarza, Oscar
dc.contributor.authorSimon, Felipe
dc.contributor.authorToledo, Hector
dc.contributor.authorPark, Kang-Sik
dc.contributor.authorTrimmer, James S.
dc.contributor.authorCerda, Oscar
dc.date.accessioned2023-05-11T18:18:32Z
dc.date.available2023-05-11T18:18:32Z
dc.date.issued2015-06
dc.descriptionIndexación: Scopuses
dc.description.abstractCellular migration and contractility are fundamental processes that are regulated by a variety of concerted mechanisms such as cytoskeleton rearrangements, focal adhesion turnover, and Ca2+ oscillations. TRPM4 is a Ca2+-activated non-selective cationic channel (Ca2+-NSCC) that conducts monovalent but not divalent cations. Here, we used a mass spectrometry-based proteomics approach to identify putative TRPM4-associated proteins. Interestingly, the largest group of these proteins has actin cytoskeleton-related functions, and among these nine are specifically annotated as focal adhesion-related proteins. Consistent with these results, we found that TRPM4 localizes to focal adhesions in cells from different cellular lineages. We show that suppression of TRPM4 in MEFs impacts turnover of focal adhesions, serum-induced Ca2+ influx, focal adhesion kinase (FAK) and Rac activities, and results in reduced cellular spreading, migration and contractile behavior. Finally, we demonstrate that the inhibition of TRPM4 activity alters cellular contractility in vivo, affecting cutaneous wound healing. Together, these findings provide the first evidence, to our knowledge, for a TRP channel specifically localized to focal adhesions, where it performs a central role in modulating cellular migration and contractility. © 2015, Public Library of Science. All rights reserved. This is an open access article, free of all copyright, and may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose. The work is made available under the Creative Commons CC0 public domain dedication.es
dc.description.urihttps://journals.plos.org/plosone/article?id=10.1371/journal.pone.0130540
dc.identifier.citationPLoS ONE Volume 10, Issue 625 June 2015 Article number e0130540es
dc.identifier.doi10.1371/journal.pone.0130540
dc.identifier.issn1932-6203
dc.identifier.urihttps://repositorio.unab.cl/xmlui/handle/ria/49545
dc.language.isoenes
dc.publisherPublic Library of Sciencees
dc.rights.licenseAtribución 4.0 Internacional (CC BY 4.0)
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/deed.es
dc.subjectCation Channeles
dc.subjectGlibenclamidees
dc.subject9-Phenanthroles
dc.titleTRPM4 is a novel component of the adhesome required for focal adhesion disassembly, migration and contractilityes
dc.typeArtículoes
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