Faculty Collaboration Database

USP5 Is Dispensable for Monoubiquitin Maintenance in Drosophila. J Biol Chem 2016 Apr 22;291(17):9161-72

Date

02/27/2016

Pubmed ID

26917723

Pubmed Central ID

PMC4861482

DOI

10.1074/jbc.M115.703504

Scopus ID

2-s2.0-84965003027 (requires institutional sign-in at Scopus site)   12 Citations

Abstract

Ubiquitination is a post-translational modification that regulates most cellular pathways and processes, including degradation of proteins by the proteasome. Substrate ubiquitination is controlled at various stages, including through its reversal by deubiquitinases (DUBs). A critical outcome of this process is the recycling of monoubiquitin. One DUB whose function has been proposed to include monoubiquitin recycling is USP5. Here, we investigated whether Drosophila USP5 is important for maintaining monoubiquitin in vivo We found that the fruit fly orthologue of USP5 has catalytic preferences similar to its human counterpart and that this DUB is necessary during fly development. Our biochemical and genetic experiments indicate that reduction of USP5 does not lead to monoubiquitin depletion in developing flies. Also, introduction of exogenous ubiquitin does not suppress developmental lethality caused by loss of endogenous USP5. Our work indicates that a primary physiological role of USP5 is not to recycle monoubiquitin for reutilization, but that it may involve disassembly of conjugated ubiquitin to maintain proteasome function.

Author List

Ristic G, Tsou WL, Guzi E, Kanack AJ, Scaglione KM, Todi SV

MESH terms used to index this publication - Major topics in bold

Animals
Drosophila Proteins
Drosophila melanogaster
Proteasome Endopeptidase Complex
Ubiquitin
Ubiquitin-Specific Proteases
Ubiquitination