3ZDL

Vinculin head (1-258) in complex with a RIAM fragment

3ZDL の概要

• エントリーDOI: 10.2210/pdb3zdl/pdb
• 分子名称: VINCULIN, AMYLOID BETA A4 PRECURSOR PROTEIN-BINDING FAMILY B MEMBER 1-INTERACTING PROTEIN (3 entities in total)
• 機能のキーワード: cell adhesion
• 由来する生物種: GALLUS GALLUS (CHICKEN); 詳細
• 細胞内の位置: Cytoplasm, cytoskeleton: P12003; Cell membrane; Peripheral membrane protein (By similarity): Q7Z5R6
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 34867.02

構造登録者

Zacharchenko, T.,Elliott, P.R.,Goult, B.T.,Bate, N.,Critchely, D.R.,Barsukov, I.L. (登録日: 2012-11-28, 公開日: 2013-02-13, 最終更新日: 2023-12-20)

主引用文献

Goult, B.T.,Zacharchenko, T.,Bate, N.,Tsang, R.,Hey, F.,Gingras, A.R.,Elliott, P.R.,Roberts, G.C.,Ballestrem, C.,Critchley, D.R.,Barsukov, I.L.
Riam and Vinculin Binding to Talin are Mutually Exclusive and Regulate Adhesion Assembly and Turnover.
J.Biol.Chem., 288:8238-, 2013

PubMed Abstract: Talin activates integrins, couples them to F-actin, and recruits vinculin to focal adhesions (FAs). Here, we report the structural characterization of the talin rod: 13 helical bundles (R1-R13) organized into a compact cluster of four-helix bundles (R2-R4) within a linear chain of five-helix bundles. Nine of the bundles contain vinculin-binding sites (VBS); R2R3 are atypical, with each containing two VBS. Talin R2R3 also binds synergistically to RIAM, a Rap1 effector involved in integrin activation. Biochemical and structural data show that vinculin and RIAM binding to R2R3 is mutually exclusive. Moreover, vinculin binding requires domain unfolding, whereas RIAM binds the folded R2R3 double domain. In cells, RIAM is enriched in nascent adhesions at the leading edge whereas vinculin is enriched in FAs. We propose a model in which RIAM binding to R2R3 initially recruits talin to membranes where it activates integrins. As talin engages F-actin, force exerted on R2R3 disrupts RIAM binding and exposes the VBS, which recruit vinculin to stabilize the complex.

PubMed: 23389036
DOI: 10.1074/JBC.M112.438119

実験手法

X-RAY DIFFRACTION (2.3 Å)