Peer-Reviewed Journal Details
Mandatory Fields
Lam, SY,Murphy, C,Foley, LA,Ross, SA,Wang, TC,Fleming, JV
2014
August
Biochemical and Biophysical Research Communications
The human ubiquitin conjugating enzyme UBE2J2 (Ubc6) is a substrate for proteasomal degradation
Validated
WOS: 9 ()
Optional Fields
Unfolded protein response (UPR) ER associated degradation (ERAD) Ubiquitin conjugating enzyme Ube2J2 (Ubc6) Ube2G2 (Ubc7) ENDOPLASMIC-RETICULUM STRESS UNFOLDED PROTEIN RESPONSE ER MEMBRANE LOCALIZATION DETERMINES EXPRESSION STABILITY HOMOLOGS RECEPTOR COMPLEX
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361
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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.
10.1016/j.bbrc.2014.07.099
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