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

13 Citations (Scopus)

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 2010

Fingerprint

Diptera
Drosophila
Long-Term Memory
Memory Disorders
Alternative Splicing
Neuropeptides
Transgenes
Growth Hormone
Intercellular Signaling Peptides and Proteins
Ethanol
Peptides
Genes
Proteins
carboxypeptidase D
adipokinetic hormone
metallocarboxypeptidase D

Keywords

  • Carboxypeptidase
  • Neuropeptide
  • Peptidase
  • Peptide processing
  • Protease

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology
  • Molecular Medicine
  • Pharmacology
  • Cellular and Molecular Neuroscience
  • Medicine(all)

Cite this

Individual carboxypeptidase D domains have both redundant and unique functions in Drosophila development and behavior. / Sidyelyeva, Galyna; Wegener, Christian; Schoenfeld, Brian P.; Bell, Aaron J.; Baker, Nicholas E.; McBride, Sean M J; Fricker, Lloyd D.

In: Cellular and Molecular Life Sciences, Vol. 67, No. 17, 09.2010, p. 2991-3004.

Research output: Contribution to journalArticle

Sidyelyeva, Galyna ; Wegener, Christian ; Schoenfeld, Brian P. ; Bell, Aaron J. ; Baker, Nicholas E. ; McBride, Sean M J ; Fricker, Lloyd D. / Individual carboxypeptidase D domains have both redundant and unique functions in Drosophila development and behavior. In: Cellular and Molecular Life Sciences. 2010 ; Vol. 67, No. 17. pp. 2991-3004.
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