Kindlin-2 recruits paxillin and Arp2/3 to promote membrane protrusions during initial cell spreading.

2.50
Hdl Handle:
http://hdl.handle.net/10033/621164
Title:
Kindlin-2 recruits paxillin and Arp2/3 to promote membrane protrusions during initial cell spreading.
Authors:
Böttcher, Ralph T; Veelders, Maik; Rombaut, Pascaline; Faix, Jan; Theodosiou, Marina; Stradal, Theresia E B ( 0000-0002-0352-9474 ) ; Rottner, Klemens ( 0000-0003-4244-4198 ) ; Zent, Roy; Herzog, Franz; Fässler, Reinhard
Abstract:
Cell 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.
Affiliation:
Helmholtz-Zentrum für Infektionsforschung GmbH, Inhoffenstr.7, 38124 Braunschweig, Germany.
Citation:
Kindlin-2 recruits paxillin and Arp2/3 to promote membrane protrusions during initial cell spreading. 2017 J. Cell Biol.
Journal:
The Journal of cell biology
Issue Date:
14-Sep-2017
URI:
http://hdl.handle.net/10033/621164
DOI:
10.1083/jcb.201701176
PubMed ID:
28912124
Type:
Article
Language:
en
ISSN:
1540-8140
Appears in Collections:
publications of the central unit for microscopy (ZEIM); publications of the Research group: molecular cell biology (MZBI)

Full metadata record

DC FieldValue Language
dc.contributor.authorBöttcher, Ralph Ten
dc.contributor.authorVeelders, Maiken
dc.contributor.authorRombaut, Pascalineen
dc.contributor.authorFaix, Janen
dc.contributor.authorTheodosiou, Marinaen
dc.contributor.authorStradal, Theresia E Ben
dc.contributor.authorRottner, Klemensen
dc.contributor.authorZent, Royen
dc.contributor.authorHerzog, Franzen
dc.contributor.authorFässler, Reinharden
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.en
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

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