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

FEBS Letters

Rüdiger, Manfred¹  Reinhard, Matthias²  Jockusch, Brigitte M.¹  Walter, Ulrich² 

[1] Zoologisches Institut, Abteilung Zellbiologie, Spielmannstraße 7, D-38106 Braunschweig, Germany;Medizinische Universitätsklinik, Institut für Klinische Biochemie und Pathobiochemie, Josef-Schneider-Straße 2, D-97080 Würzburg, Germany

关键词: ActA;    Focal adhesion;    Focal contact;    Microfilament regulation;    Zyxin;    EVH1;    Ena-VASP homology 1;    EVL;    Ena-VASP-like;    MBP-Vinc8;    fusion protein of maltose binding protein and vinculin (aa 809–1063);    Mena;    mammalian enabled (Ena);    VASP;    vasodilator-stimulated phosphoprotein;   

DOI  :  10.1016/S0014-5793(96)01295-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown