Individual Carboxypeptidase D Domains Have Both Redundant and Unique Functions in Drosophila Development and Behavior

Cell Mol Life Sci. 2010 Sep;67(17):2991-3004. doi: 10.1007/s00018-010-0369-8. Epub 2010 Apr 13.

Abstract

Metallocarboxypeptidase D (CPD) functions in protein and peptide processing. The Drosophila CPD svr gene undergoes alternative splicing, producing forms containing 1-3 active or inactive CP domains. To investigate the function of the various CP domains, we created transgenic flies expressing specific forms of CPD in the embryonic-lethal svr (PG33) mutant. All constructs containing an active CP domain rescued the lethality with varying degrees, and full viability required inactive CP domain-3. Transgenic flies overexpressing active CP domain-1 or -2 were similar to each other and to the viable svr mutants, with pointed wing shape, enhanced ethanol sensitivity, and decreased cold sensitivity. The transgenes fully compensated for a long-term memory deficit observed in the viable svr mutants. Overexpression of CP domain-1 or -2 reduced the levels of Lys/Arg-extended adipokinetic hormone intermediates. These findings suggest that CPD domains-1 and -2 have largely redundant functions in the processing of growth factors, hormones, and neuropeptides.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Alternative Splicing / physiology
  • Animals
  • Animals, Genetically Modified
  • Drosophila
  • Drosophila Proteins / genetics
  • Drosophila Proteins / physiology*
  • Gene Components
  • Memory / physiology
  • Phenotype*
  • Protein Structure, Tertiary / genetics
  • Protein Structure, Tertiary / physiology*
  • Proteins / genetics
  • Proteins / physiology*
  • Reverse Transcriptase Polymerase Chain Reaction
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
  • Wings, Animal / anatomy & histology

Substances

  • Drosophila Proteins
  • Proteins
  • metallocarboxypeptidase D