USP5 Is Dispensable for Monoubiquitin Maintenance in Drosophila.

Journal Article (Journal Article)

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.

Full Text

Duke Authors

Cited Authors

  • Ristic, G; Tsou, W-L; Guzi, E; Kanack, AJ; Scaglione, KM; Todi, SV

Published Date

  • April 22, 2016

Published In

Volume / Issue

  • 291 / 17

Start / End Page

  • 9161 - 9172

PubMed ID

  • 26917723

Pubmed Central ID

  • PMC4861482

Electronic International Standard Serial Number (EISSN)

  • 1083-351X

Digital Object Identifier (DOI)

  • 10.1074/jbc.M115.703504


  • eng

Conference Location

  • United States