| First Author | Böttcher RT | Year | 2017 |
| Journal | J Cell Biol | Volume | 216 |
| Issue | 11 | Pages | 3785-3798 |
| PubMed ID | 28912124 | Mgi Jnum | J:249300 |
| Mgi Id | MGI:5921984 | Doi | 10.1083/jcb.201701176 |
| Citation | Bottcher RT, et al. (2017) Kindlin-2 recruits paxillin and Arp2/3 to promote membrane protrusions during initial cell spreading. J Cell Biol 216(11):3785-3798 |
| abstractText | 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. |
