Journal
MOLECULAR BIOLOGY OF THE CELL
Volume 24, Issue 9, Pages 1354-1362Publisher
AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.E12-09-0695
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- National Institutes of Health
- Agency for Science, Technology and Research (AstarSTAR), Singapore
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Talin-mediated integrin activation drives integrin-based adhesions. Here we examine the roles of two proteins that induce talin-integrin interactions-vinculin and Rap1-GTP-interacting adaptor molecule (RIAM)-in the formation and maturation of integrin-based adhesions. RIAM-containing adhesions are primarily in the lamellipodium; RIAM is subsequently reduced in mature focal adhesions due to direct competition with vinculin for talin-binding sites. We show that vinculin binding to talin induces Rap1-independent association of talin with integrins and resulting integrin activation, in sharp contrast to Rap1-dependent RIAM-induced activation. Vinculin stabilizes adhesions, increasing their ability to transmit force, whereas RIAM played a critical role in lamellipodial protrusion. Thus displacement of RIAM by vinculin acts as a molecular switch that mediates the transition of integrin-based adhesions from drivers of lamellipodial protrusion to stable, force-bearing adhesions. Consequently changes in the abundance of two multiprotein modules within maturing adhesions, one regulated by Rap1 and one by tension, result in the temporal evolution of adhesion functions.
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