Raver1 Interactions with Vinculin and RNA Suggest a Feed-Forward Pathway in Directing mRNA to Focal Adhesions

Journal Article · Fri Sep 11 04:00:00 EDT 2009 · Structure

DOI:https://doi.org/10.1016/j.str.2009.04.010· OSTI ID:1005737

Lee, Jun Hyuck; Rangarajan, Erumbi S; Yogesha, S D; Izard, Tina; Scripps,

The translational machinery of the cell relocalizes to focal adhesions following the activation of integrin receptors. This response allows for rapid, local production of components needed for adhesion complex assembly and signaling. Vinculin links focal adhesions to the actin cytoskeleton following its activation by integrin signaling, which severs intramolecular interactions of vinculin's head and tail (Vt) domains. Our vinculin:raver1 crystal structures and binding studies show that activated Vt selectively interacts with one of the three RNA recognition motifs of raver1, that the vinculin:raver1 complex binds to F-actin, and that raver1 binds selectively to RNA, including a sequence found in vinculin mRNA. Further, mutation of residues that mediate interaction of raver1 with vinculin abolish their colocalization in cells. These findings suggest a feed-forward model where vinculin activation at focal adhesions provides a scaffold for recruitment of raver1 and its mRNA cargo to facilitate the production of components of adhesion complexes.

• Research Organization: Argonne National Laboratory (ANL)
• Sponsoring Organization: USDOE
• OSTI ID: 1005737
• Journal Information: Structure, Journal Name: Structure Journal Issue: (6) ; 06, 2009 Vol. 17
• Country of Publication: United States
• Language: ENGLISH

Related Subjects

36 MATERIALS SCIENCE
ACTIN
ADHESION
CARGO
CRYSTAL STRUCTURE
MACHINERY
MUTATIONS
PRODUCTION
RESIDUES
RNA