Multisite phosphorylation of the glycogen-binding subunit of protein phosphatase-1G by cyclic AMP-dependent protein kinase and glycogen synthase kinase-3

Paul Dent, David G. Campbell, Michael J. Hubbard, Philip Cohen

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62 Citations (Scopus)

Abstract

The glycogen-binding (G) subunit of protein phosphatase-1G is phosphorylated stoichiometrically by glycogen synthase kinase-3 (GSK3), and with a greater catalytic efficiency than glycogen synthase, but only after prior phosphorylation by cyclic AMP-dependent protein kinase (A-kinase) at site 1. The residues phosphorylated are the first two serines in the sequence AIFKPGFSPQPSRRGS-, while the C-terminal serine (site 1) is one of the two residues phosphorylated by A-kinase. These findings demonstrate that (i) the G subunit undergoes multisite phosphorylation in vitro; (ii) phosphorylation by GSK3 requires the presence of a C-terminal phosphoserine residue; (iii) GSK3 can synergise with protein kinases other than casein kinase-2.

Original languageEnglish
Pages (from-to)67-72
Number of pages6
JournalFEBS Letters
Volume248
Issue number1-2
DOIs
Publication statusPublished - 8 May 1989

Keywords

  • cyclic AMP
  • Glycogen metabolism
  • Glycogen synthase
  • Protein kinase
  • Protein phosphatase

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