3H2U

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

3H2U の概要

• エントリーDOI: 10.2210/pdb3h2u/pdb
• 関連するPDBエントリー: 1RKE 1tr2 3H2V
• 分子名称: Vinculin, Raver-1 (3 entities in total)
• 機能のキーワード: focal adhesion, actin cytoskeleton, rnp motif, rna binding, alternative splicing, cytoplasm, nucleus, phosphoprotein, rna-binding, cell adhesion
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Nucleus (By similarity): Q8IY67
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 105196.29

構造登録者

Lee, J.H.,Rangarajan, E.S.,Yogesha, S.D.,Izard, T. (登録日: 2009-04-14, 公開日: 2009-07-28, 最終更新日: 2024-10-16)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.75 Å)