Abstract:
:Homocysteine-inducible endoplasmic reticulum (ER) protein (Herp) is an ER stress-inducible membrane protein involved in ER-associated degradation. Herp expression is maintained at low levels through a strict regulatory mechanism, but the details of this mechanism and the reasons why Herp expression is restricted in this manner remain unclear. Here, we show that Herp degradation involves synoviolin, an ER-resident E3 ubiquitin ligase. Herp protein levels were found to be markedly elevated in synoviolin-null cells, and Herp expression decreased when synoviolin was overexpressed. However, the lysine residues of Herp, which are ubiquitinated by E3 ubiquitin ligase, were not sufficient for regulation of Herp degradation. These results suggest that Herp degradation is mediated via synoviolin and that Herp ubiquitination involves amino acids other than lysine.
journal_name
Biol Pharm Bulljournal_title
Biological & pharmaceutical bulletinauthors
Maeda T,Fujita Y,Tanabe-Fujimura C,Zou K,Liu J,Liu S,Kikuchi K,Shen X,Nakajima T,Komano Hdoi
10.1248/bpb.b18-00015subject
Has Abstractpub_date
2018-01-01 00:00:00pages
915-919issue
6eissn
0918-6158issn
1347-5215journal_volume
41pub_type
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