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


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.

SUBMITTER: Bottcher RT 

PROVIDER: S-EPMC5674885 | biostudies-literature | 2017 Nov

REPOSITORIES: biostudies-literature

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

Böttcher Ralph T RT   Veelders Maik M   Rombaut Pascaline P   Faix Jan J   Theodosiou Marina M   Stradal Theresa E TE   Rottner Klemens K   Zent Roy R   Herzog Franz F   Fässler Reinhard R  

The Journal of cell biology 20170914 11


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  ...[more]

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