PKCα reduces the lipid kinase activity of the p110α/p85α PI3K through the phosphorylation of the catalytic subunit

Szabolcs Sipeki, Erzsébet Bander, Peter J. Parker, A. Faragó

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

The modulation of phosphoinositide 3-kinase (PI3K) activity influences the quality of cellular responses triggered by various receptor tyrosine kinases. Protein kinase C (PKC) has been reported to phosphorylate signalling molecules upstream of PI3K and thereby it may affect the activation of PI3K. Here, we provide the first evidence for a direct effect of a PKC isoenzyme on the activity of PI3K. PKCα but not PKCε phosphorylated the catalytic subunit of the p110α/p85α PI3K in vitro in a manner inhibited by the PKC inhibitor bisindolylmaleimide I (BIM I). The incubation of PI3K with active PKCα resulted in a significant decrease in its lipid kinase activity and this effect was also attenuated by BIM I. We conclude that PKCα is able to modulate negatively the lipid kinase activity of the p110α/p85α PI3K through the phosphorylation of the catalytic subunit.

Original languageEnglish
Pages (from-to)122-125
Number of pages4
JournalBiochemical and Biophysical Research Communications
Volume339
Issue number1
DOIs
Publication statusPublished - Jan 6 2006

Fingerprint

Phosphorylation
1-Phosphatidylinositol 4-Kinase
Phosphatidylinositols
Protein Kinase C
Catalytic Domain
Phosphotransferases
Lipids
Protein C Inhibitor
Receptor Protein-Tyrosine Kinases
Protein Kinase Inhibitors
Isoenzymes
Chemical activation
Modulation
Molecules

Keywords

  • Isoenzyme-specific functions
  • Isoenzymes
  • PI3K
  • PKC
  • Signal transduction

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

PKCα reduces the lipid kinase activity of the p110α/p85α PI3K through the phosphorylation of the catalytic subunit. / Sipeki, Szabolcs; Bander, Erzsébet; Parker, Peter J.; Faragó, A.

In: Biochemical and Biophysical Research Communications, Vol. 339, No. 1, 06.01.2006, p. 122-125.

Research output: Contribution to journalArticle

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