Protein kinase c in larval brain of wild-type and dunce memory-mutant drosophila

P. Dévay, M. Pintér, I. Kiss, A. Faragó, P. Friedrich

Research output: Contribution to journalArticle

11 Citations (Scopus)


Protein kinase C activity has been measured in extracts of larval brain of Drosophila melanogaster, with the synthetic nonapeptide substrate Ala-Ala-Ala-Ser-Phe-Lys-Ala-Lys-Lys-amide. Protein kinase C activity in such extracts is abolished in a Ca2+-dependent manner at 18°C, and partly converted to a form independent of effectors. The decay of protein kinase C activity can be prevented by leupeptin or a crude calpastatin preparation isolated from fly heads, indicating the presence of the Ca2+-dependent neutral protease, calpain, in larval brains. The total protein kinase C levels were nearly the same in wild type and three different dunce "memory-mutant" strains. In contrast, the soluble/particulate activity ratios were different: wild-type, 0.91; dunceM11, 0.46; dunceM11/Df(1)dm75,49, 1.23; dunce2, 0.88. These data suggest that the membrane adherence of protein kinase C in larval brain is governed by the actor of genes other than dunce.

Original languageEnglish
Pages (from-to)119-126
Number of pages8
JournalJournal of Neurogenetics
Issue number2
Publication statusPublished - Jan 1 1989


  • Calpain
  • Drosophila
  • Dunce memory mutant
  • Larval brain
  • Protein kinase C
  • Protein phosphorylation

ASJC Scopus subject areas

  • Genetics
  • Cellular and Molecular Neuroscience

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