3VF0

Raver1 in complex with metavinculin L954 deletion mutant

3VF0 の概要

• エントリーDOI: 10.2210/pdb3vf0/pdb
• 分子名称: Vinculin, Ribonucleoprotein PTB-binding 1, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, ... (5 entities in total)
• 機能のキーワード: cytoskeletal f-actin binding protein, ribonucleoprotein, cell adhesion-protein binding complex, cell adhesion/protein binding
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasm, cytoskeleton: P18206; Nucleus (By similarity): Q8IY67
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 64205.13

構造登録者

Lee, J.H.,Vonrhein, C.,Bricogne, G.,Izard, T. (登録日: 2012-01-09, 公開日: 2012-07-25, 最終更新日: 2024-10-30)

主引用文献

Lee, J.H.,Rangarajan, E.S.,Vonrhein, C.,Bricogne, G.,Izard, T.
The Metavinculin Tail Domain Directs Constitutive Interactions with Raver1 and vinculin RNA.
J.Mol.Biol., 422:697-704, 2012

PubMed Abstract: Vinculin is a key regulator of the actin cytoskeleton attachment to the cell membrane at cellular adhesion sites, which is crucial for processes such as cell motility and migration, development, survival, and wound healing. Vinculin loss results in embryonic lethality, cardiovascular diseases, and cancer. Its tail domain, Vt, is crucial for vinculin activation and focal adhesion turnover and binds to the actin cytoskeleton and acidic phospholipids upon which it unfurls. The RNA binding protein raver1 regulates the assembly of focal adhesions transcriptionally by binding to vinculin. The muscle-specific splice form, metavinculin, is characterized by a 68-residue insert in the tail domain (MVt) and correlates with hereditary idiopathic dilated cardiomyopathy. Here, we report that metavinculin can bind to raver1 in its inactive state. Our crystal structure explains this permissivity, where an extended coil unique to MVt is unfurled in the MVtΔ954:raver1 complex structure. Our binding assays show that raver1 forms a ternary complex with MVt and vinculin mRNA. These findings suggest that the metavinculin:raver1:RNA complex is constitutively recruited to adhesion complexes.

PubMed: 22709580
DOI: 10.1016/j.jmb.2012.06.015

実験手法

X-RAY DIFFRACTION (2.54 Å)