Autophosphorylation and dephosphorylation of multifunctional Ca2+-calmodulin-dependent protein kinase from rat brain

Y. Saitoh, H. Yamamoto, K. Fukunaga

研究成果: Article査読

10 被引用数 (Scopus)

抄録

Both 49 K and 60 K subunits of brain Ca2+-calmodulin-dependent protein kinase (calmodulin-kinase) were autophosphorylated in a Ca2+-calmodulin-dependent manner with changes in apparent molecular weights to 53 K and 64 K on SDS-PAGE. The amounts of phosphate incorporated into the 49 K and 60 K subunits were 6.5 and 15.7 mol per mol subunit, respectively, on 5-min incubation. Protein phosphatase C from bovine brain dephosphorylated calmodulin-kinase with concomitant restoration of original molecular weights on SDS-PAGE. Inhibitor-2, an inhibitor protein for protein phosphatase 1, inhibited the dephosphorylation of the kinase by protein phosphatase C only by 10-20%, indicating that both protein phosphatases 1 and 2A are involved in the reaction. These results suggest that the calmodulin-kinase activity is regulated by the phosphorylation and dephosphorylation of the enzyme itself.

本文言語English
ページ(範囲)399-403
ページ数5
ジャーナルBiomedical Research
7
6
DOI
出版ステータスPublished - 1986
外部発表はい

ASJC Scopus subject areas

  • 生化学、遺伝学、分子生物学(全般)

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