Protein phosphatase 1 is involved in the dissociation of Ca2+ calmodulin-dependent protein kinase II from postsynaptic densities

被引:45
作者
Yoshimura, Y [1 ]
Sogawa, Y [1 ]
Yamauchi, T [1 ]
机构
[1] Univ Tokushima, Fac Pharmaceut Sci, Dept Biochem, Tokushima 770, Japan
来源
FEBS LETTERS | 1999年 / 446卷 / 2-3期
关键词
Ca2+/calmodulin-dependent protein kinase II; postsynaptic density; translocation; protein phosphatase 1; autophosphorylation; dissociation;
D O I
10.1016/S0014-5793(99)00226-4
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Autophosphorylation-dependent translocation of Ca2+/calmodulin-dependent protein kinase II (CaM kinase II) to postsynaptic densities (PSDs) from cytosol may be a physiologically important process during synaptic activation. We investigated a protein phosphatase responsible for dephosphorylation of the kinase. CaM kinase II was shown to be targeted to two sites using the gel overlay method in two-dimensional gel electrophoresis. Protein phosphatase 1 (PP1) was identified to dephosphorylate CaM kinase Tr from its complex with PSDs using phosphatase inhibitors and activators, and purified phosphatases, The kinase was released from PSDs after its dephosphorylation by PP1. (C) 1999 Federation of European Biochemical Societies.
引用
收藏
页码:239 / 242
页数:4
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