Kindlin-2 recruits paxillin and Arp2/3 to promote membrane protrusions during initial cell spreading.
dc.contributor.author | Böttcher, Ralph T | |
dc.contributor.author | Veelders, Maik | |
dc.contributor.author | Rombaut, Pascaline | |
dc.contributor.author | Faix, Jan | |
dc.contributor.author | Theodosiou, Marina | |
dc.contributor.author | Stradal, Theresia E B | |
dc.contributor.author | Rottner, Klemens | |
dc.contributor.author | Zent, Roy | |
dc.contributor.author | Herzog, Franz | |
dc.contributor.author | Fässler, Reinhard | |
dc.date.accessioned | 2017-11-07T12:37:33Z | |
dc.date.available | 2017-11-07T12:37:33Z | |
dc.date.issued | 2017-09-14 | |
dc.identifier.citation | Kindlin-2 recruits paxillin and Arp2/3 to promote membrane protrusions during initial cell spreading. 2017 J. Cell Biol. | en |
dc.identifier.issn | 1540-8140 | |
dc.identifier.pmid | 28912124 | |
dc.identifier.doi | 10.1083/jcb.201701176 | |
dc.identifier.uri | http://hdl.handle.net/10033/621164 | |
dc.description.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. | |
dc.language.iso | en | en |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-sa/4.0/ | * |
dc.title | Kindlin-2 recruits paxillin and Arp2/3 to promote membrane protrusions during initial cell spreading. | en |
dc.type | Article | en |
dc.contributor.department | Helmholtz-Zentrum für Infektionsforschung GmbH, Inhoffenstr.7, 38124 Braunschweig, Germany. | en |
dc.identifier.journal | The Journal of cell biology | en |
refterms.dateFOA | 2018-06-13T07:37:08Z | |
html.description.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. |