Individual carboxypeptidase D domains have both redundant and unique functions in Drosophila development and behavior |
| |
Authors: | Galyna Sidyelyeva Christian Wegener Brian P Schoenfeld Aaron J Bell Nicholas E Baker Sean M J McBride Lloyd D Fricker |
| |
Institution: | 1. Department of Molecular Pharmacology, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY, 10461, USA 3. Department of Biology, Animal Physiology, Philipps-University Marburg, Marburg, Germany 2. Department of Genetics, Albert Einstein College of Medicine, Bronx, NY, 10461, USA
|
| |
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. |
| |
Keywords: | |
本文献已被 SpringerLink 等数据库收录! |
|