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. Author manuscript; available in PMC: 2010 Jun 10.
Published in final edited form as: Structure. 2009 Jun 10;17(6):833–842. doi: 10.1016/j.str.2009.04.010

Figure 7. Vinculin Functions as a Scaffold for the Production of Adhesion Components by the Translational Machinery at Nascent Focal Adhesions.

Figure 7

The activation of vinculin (blue), by talin and perhaps other signals (Izard et al., 2004; Weis, 2004; del Rio et al., 2009), following the engagement of integrin receptors (α and β subunits) provokes alterations in the structure of its head (VH) domain that disrupt the head-tail interaction that holds vinculin in its inactive conformation. Activated vinculin then binds to the RRM1 domain of raver1 (red) through the agency of its tail (Vt) domain. This interaction is permissive for the interactions of the three tandem RRM domains of raver1 with their mRNA cargo (combs), which might include vinculin mRNA and transcripts encoding other components of adhesion complexes. The vinculin-raver1 interaction is also permissive for binding to actin filaments (white spheres). This feed-forward delivery system would ensure rapid and coordinated production of components of adhesion complexes by the translational machinery at these adhesion microcompartments, as seen in vivo (Chicurel et al., 1998; Rodriguez et al., 2006).