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The human ubiquitin conjugating enzyme UBE2J2 (Ubc6) is a substrate for proteasomal degradation.

Abstract：

: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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Lam SY,Murphy C,Foley LA,Ross SA,Wang TC,Fleming JV

doi

10.1016/j.bbrc.2014.07.099

subject

Has Abstract

pub_date

2014-08-29 00:00:00

pages

361-6

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(14)01348-5

journal_volume

451

pub_type

杂志文章

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