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Phosphorylation of smooth muscle myosin light chain by five different kinases
Author(s) -
Singh Toolsee J.,
Akatsuka Akira,
Huang Kuo-Ping
Publication year - 1983
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 - 10.1016/0014-5793(83)80449-9
Subject(s) - casein kinase 2 , casein kinase 2, alpha 1 , glycogen phosphorylase , phosphorylase kinase , casein kinase 1 , myosin light chain kinase , mitogen activated protein kinase kinase , biochemistry , map2k7 , cyclin dependent kinase 2 , cyclin dependent kinase 9 , phosphorylation , map kinase kinase kinase , kinase , chemistry , gsk 3 , protein kinase a , biology , glycogen
Phosphorylation of the 20 kDa myosin light chain from smooth muscle by five different kinases was investigated. Three of the kinases (myosin light chain kinase, phosphorylase kinase, and cAMP‐dependent protein kinase) phosphorylate serine residues, the fourth (casein‐kinase‐2) mainly threonine, and the fifth (glycogen synthase (casein) kinase‐1) both serine and threonine. Isoelectric focusing analyses of 32 P‐labelled chymotryptic peptides indicate that phosphorylase kinase and cAMP‐dependent protein kinase phosphorylate the same site as myosin light chain kinase. However, both casein kinase‐2 and glycogen synthase (casein) kinase‐1 phosphorylate different sites.