Ubp2 regulates Rsp5 ubiquitination activity in vivo and in vitro.
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 inve...
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doaj-675ba5b16fe84ec6894c2298750992bb2020-11-25T00:42:28ZengPublic Library of Science (PLoS)PLoS ONE1932-62032013-01-0189e7537210.1371/journal.pone.0075372Ubp2 regulates Rsp5 ubiquitination activity in vivo and in vitro.Mandy H Y LamAndrew EmiliThe 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.http://europepmc.org/articles/PMC3777918?pdf=render |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Mandy H Y Lam Andrew Emili |
spellingShingle |
Mandy H Y Lam Andrew Emili Ubp2 regulates Rsp5 ubiquitination activity in vivo and in vitro. PLoS ONE |
author_facet |
Mandy H Y Lam Andrew Emili |
author_sort |
Mandy H Y Lam |
title |
Ubp2 regulates Rsp5 ubiquitination activity in vivo and in vitro. |
title_short |
Ubp2 regulates Rsp5 ubiquitination activity in vivo and in vitro. |
title_full |
Ubp2 regulates Rsp5 ubiquitination activity in vivo and in vitro. |
title_fullStr |
Ubp2 regulates Rsp5 ubiquitination activity in vivo and in vitro. |
title_full_unstemmed |
Ubp2 regulates Rsp5 ubiquitination activity in vivo and in vitro. |
title_sort |
ubp2 regulates rsp5 ubiquitination activity in vivo and in vitro. |
publisher |
Public Library of Science (PLoS) |
series |
PLoS ONE |
issn |
1932-6203 |
publishDate |
2013-01-01 |
description |
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. |
url |
http://europepmc.org/articles/PMC3777918?pdf=render |
work_keys_str_mv |
AT mandyhylam ubp2regulatesrsp5ubiquitinationactivityinvivoandinvitro AT andrewemili ubp2regulatesrsp5ubiquitinationactivityinvivoandinvitro |
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