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- Title
Ubp2 Regulates Rsp5 Ubiquitination Activity <i>In Vivo</i> and <i>In Vitro</i>.
- Authors
Lam, Mandy H. Y.; Emili, Andrew
- Abstract
The yeast HECT-family E3 ubiquitin ligase Rsp5 has been implicated in diverse cell functions. Previously, we and others [1], [2] reported the physical and functional interaction of Rsp5 with the deubiquitinating enzyme Ubp2, and the ubiquitin associated (UBA) domain-containing cofactor Rup1. To investigate the mechanism and significance of the Rsp5-Rup1-Ubp2 complex, we examined Rsp5 ubiquitination status in the presence or absence of these cofactors. We found that, similar to its mammalian homologues, Rsp5 is auto-ubiquitinated in vivo. Association with a substrate or Rup1 increased Rsp5 self-ubiquitination, whereas Ubp2 efficiently deubiquitinates Rsp5 in vivo and in vitro. The data reported here imply an auto-modulatory mechanism of Rsp5 regulation common to other E3 ligases.
- Subjects
UBIQUITINATION; GENETIC regulation; UBIQUITIN ligases; CELL physiology; COFACTORS (Biochemistry); HOMOLOGY (Biology)
- Publication
PLoS ONE, 2013, Vol 8, Issue 9, p1
- ISSN
1932-6203
- Publication type
Article
- DOI
10.1371/journal.pone.0075372