Epidermal growth factor receptor and integrins control force-dependent vinculin recruitment to E-cadherin junctions

Journal of Cell Science
Poonam SehgalDeborah Leckband

Abstract

This study reports novel findings that link E-cadherin (also known as CDH1)-mediated force-transduction signaling to vinculin targeting to intercellular junctions via epidermal growth factor receptor (EGFR) and integrins. These results build on previous findings that demonstrated that mechanically perturbed E-cadherin receptors activate phosphoinositide 3-kinase and downstream integrins in an EGFR-dependent manner. Results of this study show that this EGFR-mediated kinase cascade controls the force-dependent recruitment of vinculin to stressed E-cadherin complexes - a key early signature of cadherin-based mechanotransduction. Vinculin targeting requires its phosphorylation at tyrosine 822 by Abl family kinases (hereafter Abl), but the origin of force-dependent Abl activation had not been identified. We now present evidence that integrin activation, which is downstream of EGFR signaling, controls Abl activation, thus linking E-cadherin to Abl through a mechanosensitive signaling network. These findings place EGFR and integrins at the center of a positive-feedback loop, through which force-activated E-cadherin signals regulate vinculin recruitment to cadherin complexes in response to increased intercellular tension.This article h...Continue Reading

References

Oct 1, 1995·Current Opinion in Cell Biology·M Takeichi
Jul 1, 1995·Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire·N Wang, D E Ingber
Dec 24, 1996·Proceedings of the National Academy of Sciences of the United States of America·J M LewisJ Y Wang
May 23, 1998·The Journal of Cell Biology·A HuttenlocherA F Horwitz
Dec 6, 2001·Nature Reviews. Molecular Cell Biology·M Fukata, K Kaibuchi
Dec 26, 2001·Proceedings of the National Academy of Sciences of the United States of America·A Y TingR Y Tsien
Oct 11, 2002·Advances in Cancer Research·Ann Marie Pendergast
Mar 26, 2003·Nature Cell Biology·Rina PlattnerAnn Marie Pendergast
Oct 23, 2003·Annual Review of Cell and Developmental Biology·Alexander D BershadskyBenjamin Geiger
Feb 13, 2004·The Journal of Biological Chemistry·Akira KatsumiMartin Alexander Schwartz
Apr 23, 2005·Nature·Yingxiao WangShu Chien
Jul 19, 2005·Nature Reviews. Molecular Cell Biology·Barry M Gumbiner
Sep 20, 2005·Cancer Cell·Matthew J PaszekValerie M Weaver
Jan 10, 2006·Developmental Cell·A Wayne OrrMartin A Schwartz
Apr 12, 2006·Nature Reviews. Molecular Cell Biology·Viola Vogel, Michael Sheetz
Aug 23, 2006·Cell·Adam J EnglerDennis E Discher
Aug 25, 2006·Molecular Biology of the Cell·A Wayne OrrMartin A Schwartz
Jun 6, 2007·The Journal of Cell Biology·Marcello CurtoAndrea I McClatchey
Jun 8, 2007·Molecular Biology of the Cell·Robert W McLachlanAlpha S Yap
Nov 6, 2007·Molecular Biology of the Cell·Masakiyo SakaguchiNam-ho Huh
Jan 8, 2008·Biophysical Journal·Delphine Icard-ArcizetSylvie Hénon
Jan 30, 2008·Current Protocols in Cell Biology·M Takeichi, S Nakagawa
Jun 28, 2008·Current Opinion in Cell Biology·Martin A Schwartz, Douglas W DeSimone
Jan 21, 2009·Cancer Metastasis Reviews·Sanjay Kumar, Valerie M Weaver
Jan 24, 2009·Nature Reviews. Cancer·Darci T ButcherValerie M Weaver
Apr 25, 2009·Arteriosclerosis, Thrombosis, and Vascular Biology·Zhongming Chen, Ellie Tzima
Jun 25, 2009·Proceedings of the National Academy of Sciences of the United States of America·Jin-Hong KimAnand R Asthagiri
Oct 10, 2009·Journal of Biomechanics·Joseph P Califano, Cynthia A Reinhart-King
Nov 26, 2009·Cell·Kandice R LeventalValerie M Weaver
Jan 13, 2010·Cold Spring Harbor Perspectives in Biology·Lawrence Shapiro, William I Weis
Feb 18, 2010·Biophysical Journal·Benoit LadouxRené-Marc Mège
May 11, 2010·Nature Cell Biology·Thomas Lecuit
May 11, 2010·Nature Cell Biology·Shigenobu YonemuraMai Shibata
May 14, 2010·Proceedings of the National Academy of Sciences of the United States of America·Zhijun LiuChristopher S Chen
Sep 24, 2010·American Journal of Physiology. Cell Physiology·Ramaswamy KrishnanGeerten P van Nieuw Amerongen
Nov 19, 2010·Cold Spring Harbor Perspectives in Biology·Martin Alexander Schwartz
Dec 7, 2010·Current Opinion in Cell Biology·Karen E Kasza, Jennifer A Zallen

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Oct 10, 2018·The EMBO Journal·René HägerlingFriedemann Kiefer
Jul 23, 2019·F1000Research·Willem-Jan PannekoekMartijn Gloerich
Nov 28, 2020·Science·Huapeng H Yu, Jennifer A Zallen
Jan 17, 2021·Developmental Cell·Pierre-François LenneVirgile Viasnoff

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