3H2U

Human raver1 RRM1, RRM2, and RRM3 domains in complex with human vinculin tail domain Vt

Summary for 3H2U

• Entry DOI: 10.2210/pdb3h2u/pdb
• Related: 1RKE 1tr2 3H2V
• Descriptor: Vinculin, Raver-1 (3 entities in total)
• Functional Keywords: focal adhesion, actin cytoskeleton, rnp motif, rna binding, alternative splicing, cytoplasm, nucleus, phosphoprotein, rna-binding, cell adhesion
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus (By similarity): Q8IY67
• Total number of polymer chains: 4
• Total formula weight: 105196.29

Authors

Lee, J.H.,Rangarajan, E.S.,Yogesha, S.D.,Izard, T. (deposition date: 2009-04-14, release date: 2009-07-28, Last modification date: 2024-10-16)

Primary citation

Lee, J.H.,Rangarajan, E.S.,Yogesha, S.D.,Izard, T.
Raver1 interactions with vinculin and RNA suggest a feed-forward pathway in directing mRNA to focal adhesions
Structure, 17:833-842, 2009

PubMed Abstract: 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.

PubMed: 19523901
DOI: 10.1016/j.str.2009.04.010

Experimental method

X-RAY DIFFRACTION (2.75 Å)