Individual carboxypeptidase D domains have both redundant and unique functions in Drosophila development and behavior

Galyna Sidyelyeva, Christian Wegener, Brian P. Schoenfeld, Aaron J. Bell, Nicholas E. Baker, Sean M.J. McBride, Lloyd D. Fricker

Research output: Contribution to journalArticle

14 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)2991-3004
Number of pages14
JournalCellular and Molecular Life Sciences
Volume67
Issue number17
DOIs
StatePublished - Sep 1 2010

Keywords

  • Carboxypeptidase
  • Neuropeptide
  • Peptidase
  • Peptide processing
  • Protease

ASJC Scopus subject areas

  • Molecular Medicine
  • Molecular Biology
  • Pharmacology
  • Cellular and Molecular Neuroscience
  • Cell Biology

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