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

Ralph T. Böttcher, Maik Veelders, Pascaline Rombaut, Jan Faix, Marina Theodosiou, Theresa E. Stradal, Klemens Rottner, Roy Zent, Franz Herzog, Reinhard Fässler

Publikation: Beitrag in FachzeitschriftArtikelBegutachtung

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.

OriginalspracheEnglisch
Seiten (von - bis)3785-3798
Seitenumfang14
FachzeitschriftJournal of Cell Biology
Jahrgang216
Ausgabenummer11
DOIs
PublikationsstatusVeröffentlicht - 6 Nov. 2017
Extern publiziertJa

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