期刊
NATURE CELL BIOLOGY
卷 9, 期 9, 页码 1046-U15出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/ncb1626
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- Medical Research Council [G0100152] Funding Source: Medline
- MRC [G0100152] Funding Source: UKRI
- Medical Research Council [G0100152] Funding Source: researchfish
Networks of actin filaments, controlled by the Arp2/3 complex, drive membrane protrusion during cell migration. How integrins signal to the Arp2/3 complex is not well understood. Here, we show that focal adhesion kinase (FAK) and the Arp2/ 3 complex associate and colocalize at transient structures formed early after adhesion. Nascent lamellipodia, which originate at these structures, do not form in FAK-deficient cells, or in cells in which FAK mutants cannot be autophosphorylated after integrin engagement. The FERM domain of FAK binds directly to Arp3 and can enhance Arp2/3-dependent actin polymerization. Critically, Arp2/ 3 is not bound when FAK is phosphorylated on Tyr 397. Interfering peptides and FERM-domain point mutants show that FAK binding to Arp2/ 3 controls protrusive lamellipodia formation and cell spreading. This establishes a new function for the FAK FERM domain in forming a phosphorylation-regulated complex with Arp2/ 3, linking integrin signalling directly with the actin polymerization machinery.
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