pHocal adhesion kinase regulation is on a FERM foundation

Increases in intracellular pH (pHi) occur upon integrin receptor binding to matrix proteins and in tumor cells. In this issue, Choi et al. (2013. J. Cell Biol. http://dx.doi.org/10.1083/jcb.201308034) show that pHi increase activates FAK by causing deprotonation of histidine 58 in its FERM (band 4.1...

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Detalles Bibliográficos
Autores principales: Lawson, Christine, Schlaepfer, David D.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2013
Materias:
Reviews
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3776349/
https://www.ncbi.nlm.nih.gov/pubmed/24043698
http://dx.doi.org/10.1083/jcb.201308034
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author Lawson, Christine
Schlaepfer, David D.
author_facet Lawson, Christine
Schlaepfer, David D.
author_sort Lawson, Christine
collection PubMed
description Increases in intracellular pH (pHi) occur upon integrin receptor binding to matrix proteins and in tumor cells. In this issue, Choi et al. (2013. J. Cell Biol. http://dx.doi.org/10.1083/jcb.201308034) show that pHi increase activates FAK by causing deprotonation of histidine 58 in its FERM (band 4.1, ezrin, radixin, moesin) homology domain, which exposes a region important for FAK autophosphorylation. This model of FAK activation could contribute to motility of tumor cells by promoting focal adhesion turnover.
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spelling pubmed-37763492014-03-16 pHocal adhesion kinase regulation is on a FERM foundation Lawson, Christine Schlaepfer, David D. J Cell Biol Reviews Increases in intracellular pH (pHi) occur upon integrin receptor binding to matrix proteins and in tumor cells. In this issue, Choi et al. (2013. J. Cell Biol. http://dx.doi.org/10.1083/jcb.201308034) show that pHi increase activates FAK by causing deprotonation of histidine 58 in its FERM (band 4.1, ezrin, radixin, moesin) homology domain, which exposes a region important for FAK autophosphorylation. This model of FAK activation could contribute to motility of tumor cells by promoting focal adhesion turnover. The Rockefeller University Press 2013-09-16 /pmc/articles/PMC3776349/ /pubmed/24043698 http://dx.doi.org/10.1083/jcb.201308034 Text en © 2013 Lawson and Schlaepfer This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).
spellingShingle Reviews
Lawson, Christine
Schlaepfer, David D.
pHocal adhesion kinase regulation is on a FERM foundation
title pHocal adhesion kinase regulation is on a FERM foundation
title_full pHocal adhesion kinase regulation is on a FERM foundation
title_fullStr pHocal adhesion kinase regulation is on a FERM foundation
title_full_unstemmed pHocal adhesion kinase regulation is on a FERM foundation
title_short pHocal adhesion kinase regulation is on a FERM foundation
title_sort phocal adhesion kinase regulation is on a ferm foundation
topic Reviews
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3776349/
https://www.ncbi.nlm.nih.gov/pubmed/24043698
http://dx.doi.org/10.1083/jcb.201308034
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