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The metavinculin tail domain directs constitutive interactions with raver1 and vinculin RNA.

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.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Lee JH,Rangarajan ES,Vonrhein C,Bricogne G,Izard T

doi

10.1016/j.jmb.2012.06.015

subject

Has Abstract

pub_date

2012-10-05 00:00:00

pages

697-704

issue

5

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(12)00488-3

journal_volume

422

pub_type

杂志文章

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