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Kindlin-2 recruits paxillin and Arp2/3 to promote membrane protrusions during initial cell spreading.
Böttcher, Ralph T Veelders, Maik Rombaut, Pascaline Faix, Jan Theodosiou, Marina Stradal, Theresia E B Rottner, Klemens Zent, Roy Herzog, Franz Fässler, Reinhard
Böttcher, Ralph T
Veelders, Maik
Rombaut, Pascaline
Faix, Jan
Theodosiou, Marina
Stradal, Theresia E B
Rottner, Klemens
Zent, Roy
Herzog, Franz
Fässler, Reinhard
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2017-09-14
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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.
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Kindlin-2 recruits paxillin and Arp2/3 to promote membrane protrusions during initial cell spreading. 2017 J. Cell Biol.
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en
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1540-8140