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

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

The Journal of cell biology (2017-09-16)
Ralph T Böttcher, Maik Veelders, Pascaline Rombaut, Jan Faix, Marina Theodosiou, Theresa E Stradal, Klemens Rottner, Roy Zent, Franz Herzog, Reinhard Fässler
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.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Anti-Kindlin-2 Antibody, clone 3A3, clone 3A3, from mouse
Sigma-Aldrich
Anti-Integrin β1 Antibody, clone MB1.2, clone MB1.2, Chemicon®, from rat