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Comparison of calmodulin‐dependent glycogen synthase kinase from skeletal muscle and calmodulin‐dependent protein kinase‐II from brain
Author(s) -
Woodgett James R.,
Cohen Philip,
Yamauchi Takashi,
Fujisawa Hitoshi
Publication year - 1984
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(84)81366-6
Subject(s) - calmodulin , gsk 3 , protein kinase a , glycogen synthase , biochemistry , biology , phosphorylase kinase , mitogen activated protein kinase kinase , synapsin i , adenylate kinase , map2k7 , cyclin dependent kinase 2 , kinase , microbiology and biotechnology , chemistry , phosphorylation , enzyme , vesicle , membrane , synaptic vesicle
Calmodulin‐dependent glycogen synthase kinase from rabbit skeletal muscle and calmodulin‐dependent protein kinase‐II from rat brain were found to have remarkably similar substrate specificities. Both protein kinases phosphorylated synapsin‐I, glycogen synthase, smooth muscle myosin light chains, histone H1 and acetyl‐CoA carboxylase at the same relative rates. Site‐2 of glycogen synthase was preferentially phosphorylated by both enzymes, followed by a slower phosphorylation of site‐1b. Each protein kinase catalysed a 2‐fold activation of tryptophan 5‐monooxygenase. Calmodulin‐dependent protein kinase‐II and glycogen synthase kinase exhibited similar immunological cross‐reactivity in the presence of Ca 2+ and calmodulin, using monoclonal antibody raised against the rat brain enzyme. In the absence of Ca 2+ and calmodulin, cross‐reactivity of glycogen synthase kinase was decreased, whereas that of calmodulin‐dependent protein kinase‐II was not. The two enzymes appear to represent different isoenzymes of a multifunctional calmodulin‐dependent protein kinase that may mediate many of the actions of Ca 2+ in mammalian tissues. The results demonstrate that calmodulin‐dependent protein kinase‐II is identical to calmodulin‐dependent synapsin‐I kinase‐II, previously shown to be very similar to calmodulin‐dependent glycogen synthase kinase [(1983) FEBS Lett. 163, 329–334].