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VASP interaction with vinculin: a recurring theme of interactions with proline‐rich motifs
Author(s) -
Reinhard Matthias,
Rüdiger Manfred,
Jockusch Brigitte M.,
Walter Ulrich
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(96)01295-1
Subject(s) - vinculin , adherens junction , microbiology and biotechnology , actin , chemistry , biology , biochemistry , focal adhesion , signal transduction , cadherin , cell
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.