Regulatory subunit of type II cAMP-dependent protein kinase as substrate and inhibitor of protein phosphatase-1 and -2A

György Vereb, Ferenc Erdodi, Béla Tóth, György Bot

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

The dissociated regulatory subunit (RII) of autophosphorylated cAMP-dependent protein kinase II was dephosphorylated by the catalytic subunits of protein phosphatase-1 and -2A (phosphatase-1c and -2Ac) and by a high-Mr, polycation-dependent form of phosphatase-2A (2A0) with Km values of 5,0.3 and 1 μM, respectively. Dissociation of protein kinase by cAMP preferentially increased the dephosphorylation of RII by phosphatase-1c, whereas polycations (histone H1 or polybrene) markedly stimulated phosphatase-2Ac and -2Ao even in the absence of cAMP. Thiophosphorylated RII inhibited the dephosphorylation of phosphorylase a by these phosphatases with half-maximum inhibitory concentrations of 0.1-0.36 μM.

Original languageEnglish
Pages (from-to)139-142
Number of pages4
JournalFEBS letters
Volume197
Issue number1-2
DOIs
Publication statusPublished - Mar 3 1986

Keywords

  • cyclic AMP dependence Protein kinase Phosphorylase a Protein phosphatase Polybrene

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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