人类泛素结合酶UBE2J2（Ubc6）是蛋白酶体降解的底物。
The human ubiquitin conjugating enzyme UBE2J2 (Ubc6) is a substrate for proteasomal degradation.
作者信息
Lam Shuet Y, Murphy Claire, Foley Louise A, Ross Sarah A, Wang Timothy C, Fleming John V
机构信息
School of Biochemistry and Cell Biology, University College Cork, Cork, Ireland; School of Pharmacy, University College Cork, Cork, Ireland; Analytical and Biological Chemistry Research Facility, University College Cork, Cork, Ireland.
Department of Medicine, Columbia University, New York, NY 10032, USA.
出版信息
Biochem Biophys Res Commun. 2014 Aug 29;451(3):361-6. doi: 10.1016/j.bbrc.2014.07.099. Epub 2014 Jul 30.
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.
人类Ube2J2酶在内质网（ER）中参与蛋白质的泛素化过程。在此我们证明，它以及另一种泛素结合（Ubc）酶Ube2G2是不稳定的，用蛋白酶体抑制剂处理转染细胞可提高其稳态蛋白水平。对于Ube2J2而言，药理学诱导的未折叠蛋白反应（UPR）并未显著改变异位蛋白水平，然而，如果该酶被灭活或截短以破坏其在内质网的定位，蛋白酶体抑制的作用就会消失。这些结果首次表明，泛素结合酶（Ubcs）的稳态表达可能在调节哺乳动物细胞内质网蛋白的降解中起重要作用。
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