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

FEBS Letters

Yamauchi, Takashi¹  Sogawa, Yoshimi¹  Yoshimura, Yoshiyuki¹ 

[1] Department of Biochemistry, Faculty of Pharmaceutical Sciences, The University of Tokushima, Shomachi 1, Tokushima 770, Japan

关键词: Ca2+/calmodulin-dependent protein kinase II;    Postsynaptic density;    Translocation;    Protein phosphatase 1;    Autophosphorylation;    Dissociation;    CaM kinase II;    Ca2+/calmodulin-dependent protein kinase II;    PSD;    postsynaptic density;    LTP;    long-term potentiation;    DTT;    dithiothreitol;    EGTA;    ethylene glycol bis(β-aminoethylether)-N;    N;    N′;    N′-tetraacetic acid;    SDS;    sodium dodecyl sulfate;    PAGE;    polyacrylamide gel electrophoresis;    PP1;    PP2A;    PP2B;    PP2C;    protein phosphatase 1;    2A;    2B and 2C;    respectively;    NMDA;    N-methyl-d-aspartic acid;    AMPA;    α-amino-3-hydroxy-5-methyl-4-isoxazole propionate;   

DOI  :  10.1016/S0014-5793(99)00226-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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 II from its complex with PSDs using phosphatase inhibitors and activators, and purified phosphatases. The kinase was released from PSDs after its dephosphorylation by PP1.

【 授权许可】

Unknown