VASP interaction with vinculin: a recurring theme of interactions with proline-rich motifs.

Abstract:

:VASP (vasodilator-stimulated phosphoprotein), a protein associated with microfilaments at cellular contact sites, has been identified as a ligand for profilin and zyxin, two proteins also involved in microfilament dynamics and organization at these regions. Here, we report that VASP also directly binds to vinculin, another component of adherens junctions. Competition experiments with a vinculin-derived peptide showed that a proline-rich motif, located in the hinge region that connects vinculin's head and tail domains, is involved in VASP binding. The same motif is present in zyxin but the interactions of VASP with vinculin and zyxin differ in detail. Hence, this motif may be recognized by VASP in different ways when presented in distinct cellular sites.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Reinhard M,Rüdiger M,Jockusch BM,Walter U

doi

10.1016/s0014-5793(96)01295-1

subject

Has Abstract

pub_date

1996-12-09 00:00:00

pages

103-7

issue

1-2

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(96)01295-1

journal_volume

399

pub_type

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