Intramolecular interactions in vinculin control α‐actinin binding to the vinculin head

FEBS Letters

Rüdiger, Angelika-H.²  Rüdiger, Manfred¹  Kroemker, Martina¹  Jockusch, Brigitte M.¹ 

[1] Department of Cell Biology, Zoological Institute, Technical University Braunschweig, Spielmannstraße 7, 38092 Braunschweig, Germany;Gesellschaft für biotechnologische Forschung (GBF), Mascheroder Weg 1, 38124 Braunschweig, Germany

关键词: Vinculin;    α-Actinin;    Intramolecular interaction;    Cytoskeleton;   

DOI  :  10.1016/0014-5793(94)01216-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Using blot overlay techniques we have investigated the interaction of vinculin with α-actinin. We show that an α-actinin binding site is located in the 90 kDa vinculin head and confirm a vinculin binding site in the C-terminal rod of α-actinin, as recently reported by McGregor et al. [(1994) Biochem. J. 310, 225–233]. The isolated vinculin head binds much more strongly to α-actinin than intact vinculin. Using a proteolytic 81 kDa head fragment, we show that vinculin residues 1–107 are required for α-actinin binding. Antibodies directed against vinculin residues 808–850 inhibit the vinculin-α-actinin binding, suggesting that this sequence is directly involved in, or topographically related to, the α-actinin binding site.

【 授权许可】

Unknown