In vivo protein phosphorylation in Drosophila mutants defective in learning and memory

Neurosci Lett. 1989 Oct 9;104(3):351-5. doi: 10.1016/0304-3940(89)90602-2.

Abstract

Polypeptides phosphorylated in vivo in Drosophila mutants defective in learning and memory, were characterized by polyacrylamide gel electrophoresis of subcellular fractions obtained by phase partitioning in Triton X-114 [3]. In the mutants turnip, dunce and Shaker, one or more bands at a molecular weight range of 50-80 kDa had altered 32P incorporation. Some of these bands were altered in more than one mutant. In the mutant rutabaga no significant differences from wild-type were observed. The data suggest that phosphoproteins that could be potentially related to learning mechanisms might be identified in some learning mutants.

MeSH terms

  • Animals
  • Drosophila / genetics*
  • Drosophila / metabolism
  • Drosophila / physiology
  • Learning / physiology*
  • Memory / physiology*
  • Molecular Weight
  • Mutation*
  • Phosphoproteins / metabolism
  • Phosphoproteins / physiology*
  • Phosphorylation

Substances

  • Phosphoproteins