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Actomyosin cross‐linking by caldesmon in non‐muscle cells
Author(s) -
Goncharova Elena A.,
Shirinsky Vladimir P.,
Shevelev Alexander Ya.,
Marston Steven B.,
Vorotnikov Alexander V.
Publication year - 2001
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(01)02445-0
Subject(s) - caldesmon , myosin , actin , cytoskeleton , microbiology and biotechnology , phosphorylation , myosin light chain kinase , chemistry , calmodulin , biology , biochemistry , cell , enzyme
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.