Actomyosin cross‐linking by caldesmon in non‐muscle cells

FEBS Letters

Shevelev, Alexander Ya.²  Goncharova, Elena A.¹  Vorotnikov, Alexander V.¹  Shirinsky, Vladimir P.¹  Marston, Steven B.³ 

[1] Laboratory of Cell Motility, Institute of Experimental Cardiology, Cardiology Research Center, 3rd Cherepkovskaya Street 15a, Moscow 121552, Russia;Laboratory of Cell Engineering, Institute of Experimental Cardiology, Cardiology Research Center, 3rd Cherepkovskaya Street 15a, Moscow 121552, Russia;Laboratory of Cardiac Medicine, Imperial College School of Medicine at National Heart and Lung Institute, Dovehouse St., London SW3 6LY, UK

关键词: Caldesmon;    Cytoskeleton;    Mitogen-activated protein kinase;    Phosphorylation;    MAP-kinase;    mitogen-activated protein kinase;    SDS–PAGE;    sodium dodecyl sulfate–polyacrylamide gel electrophoresis;   

DOI  :  10.1016/S0014-5793(01)02445-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The role of myosin-binding in cytoskeletal arrangement of non-muscle low molecular weight caldesmon (l-caldesmon) was studied. The N-terminal myosin-binding domain of caldesmon (N152) colocalized with myosin in transiently transfected chicken fibroblasts. When added exogenously to the Triton-insoluble cytoskeleton, N152 enhanced l-caldesmon displacement by exogenous C-terminal actin-binding fragment (H1). Thus, a significant fraction of l-caldesmon cross-links actin and myosin. In contrast, in epithelioid HeLa cells most of l-caldesmon was only actin-bound as H1 alone was enough for its displacement. Phosphorylation by mitogen-activated protein kinase reduced the capability of H1 to displace endogenous l-caldesmon, suggesting it may represent a regulatory mechanism for actin–caldesmon interaction in vivo.

【 授权许可】

Unknown