Interaction of iodinated vinculin, metavinculin and α‐actinin with cytoskeletal proteins

FEBS Letters

Koteliansky, V.E.¹  Belkin, A.M.¹ 

[1] Institute of Experimental Cardiology, USSR Cardiology Research Center, Academy of Medical Sciences, 3rd Cherepkovskaya str. 15 A, Moscow 121552, USSR

关键词: Vinculin;    Metavinculin;    α-Actinin;    Microfilament-membrane interaction;   

DOI  :  10.1016/0014-5793(87)80832-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Iodinated vinculin, metavinculin and α-actinin were used to probe the interaction of these proteins with electrophoretically separated cytoskeletal proteins. Using the gel overlay technique, we detected strong binding of ¹²⁵I-vinculin and ¹²⁵I-metavinculin to α-actinin, 175 kDa polypeptide, talin, vinculin and metavinculin themselves, and moderate binding to actin.¹²⁵I-α-actinin was capable of interacting with vinculin and metavinculin. The specific binding of ¹²⁵-I-α-actinin to vinculin and metavinculin immobilized on a polysterene surface was also demonstrated. We suggest that the ability of vinculin and α-actinin to form a complex may be realized in microfilament-membrane linkages.

【 授权许可】

Unknown