Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 451, Issue 3, Pages 361-366Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2014.07.099
Keywords
Unfolded protein response (UPR); ER associated degradation (ERAD); Ubiquitin conjugating enzyme; Ube2J2 (Ubc6); Ube2G2 (Ubc7)
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Funding
- Portuguese Fundacao para Ciencia e a Technologia [POCI/SAU-MMO/61129/2004]
- Irish Health Research Board [RP/2006/294]
- Irish Research Council for Science Engineering and Technology studentship
- Health Research Board Cancer Scholars programme at UCC [PhD/2007/4]
- Science Foundation Ireland [02/IN.1/BO70]
- Fundação para a Ciência e a Tecnologia [POCI/SAU-MMO/61129/2004] Funding Source: FCT
- Health Research Board (HRB) [PHD-2007-4] Funding Source: Health Research Board (HRB)
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The human Ube2J2 enzyme functions in the ubiquitination of proteins at the ER. Here we demonstrate that it, and a second ubiquitin conjugating (Ubc) enzyme Ube2G2, are unstable, and incubation of transfected cells with proteasome inhibitors increased steady-state protein levels. For Ube2J2, pharmacological induction of the unfolded protein response (UPR) did not significantly alter ectopic protein levels, however the effect of proteasomal inhibition was abolished if the enzyme was inactivated or truncated to disrupt its ER-localization. These results suggest for the first time that the steady state expression of Ubcs' may be important in regulating the degradation of ER proteins in mammalian cells. (C) 2014 Elsevier Inc. All rights reserved.
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