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dc.contributor.authorBöttcher, Ralph T
dc.contributor.authorVeelders, Maik
dc.contributor.authorRombaut, Pascaline
dc.contributor.authorFaix, Jan
dc.contributor.authorTheodosiou, Marina
dc.contributor.authorStradal, Theresia E B
dc.contributor.authorRottner, Klemens
dc.contributor.authorZent, Roy
dc.contributor.authorHerzog, Franz
dc.contributor.authorFässler, Reinhard
dc.date.accessioned2017-11-07T12:37:33Z
dc.date.available2017-11-07T12:37:33Z
dc.date.issued2017-09-14
dc.identifier.citationKindlin-2 recruits paxillin and Arp2/3 to promote membrane protrusions during initial cell spreading. 2017 J. Cell Biol.en
dc.identifier.issn1540-8140
dc.identifier.pmid28912124
dc.identifier.doi10.1083/jcb.201701176
dc.identifier.urihttp://hdl.handle.net/10033/621164
dc.description.abstractCell spreading requires the coupling of actin-driven membrane protrusion and integrin-mediated adhesion to the extracellular matrix. The integrin-activating adaptor protein kindlin-2 plays a central role for cell adhesion and membrane protrusion by directly binding and recruiting paxillin to nascent adhesions. Here, we report that kindlin-2 has a dual role during initial cell spreading: it binds paxillin via the pleckstrin homology and F0 domains to activate Rac1, and it directly associates with the Arp2/3 complex to induce Rac1-mediated membrane protrusions. Consistently, abrogation of kindlin-2 binding to Arp2/3 impairs lamellipodia formation and cell spreading. Our findings identify kindlin-2 as a key protein that couples cell adhesion by activating integrins and the induction of membrane protrusions by activating Rac1 and supplying Rac1 with the Arp2/3 complex.
dc.language.isoenen
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.titleKindlin-2 recruits paxillin and Arp2/3 to promote membrane protrusions during initial cell spreading.en
dc.typeArticleen
dc.contributor.departmentHelmholtz-Zentrum für Infektionsforschung GmbH, Inhoffenstr.7, 38124 Braunschweig, Germany.en
dc.identifier.journalThe Journal of cell biologyen
refterms.dateFOA2018-06-13T07:37:08Z
html.description.abstractCell spreading requires the coupling of actin-driven membrane protrusion and integrin-mediated adhesion to the extracellular matrix. The integrin-activating adaptor protein kindlin-2 plays a central role for cell adhesion and membrane protrusion by directly binding and recruiting paxillin to nascent adhesions. Here, we report that kindlin-2 has a dual role during initial cell spreading: it binds paxillin via the pleckstrin homology and F0 domains to activate Rac1, and it directly associates with the Arp2/3 complex to induce Rac1-mediated membrane protrusions. Consistently, abrogation of kindlin-2 binding to Arp2/3 impairs lamellipodia formation and cell spreading. Our findings identify kindlin-2 as a key protein that couples cell adhesion by activating integrins and the induction of membrane protrusions by activating Rac1 and supplying Rac1 with the Arp2/3 complex.


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