Comparison of calmodulin‐dependent glycogen synthase kinase from skeletal muscle and calmodulin‐dependent protein kinase‐II from brain

FEBS Letters

Yamauchi, Takashi¹  Fujisawa, Hitoshi¹  Woodgett, James R.¹  Cohen, Philip¹ 

[1] Department of Biochemistry, University of Dundee, Dundee DD1 4HN, Scotland

关键词: Ca2+;    Calmodulin;    Protein phosphorylation;    Glycogen synthesis;    Neurotransmitter;    Catecholamine;   

DOI  :  10.1016/0014-5793(84)81366-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 Ca²⁺ and calmodulin, using monoclonal antibody raised against the rat brain enzyme. In the absence of Ca²⁺ 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 Ca²⁺ 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].

【 授权许可】

Unknown