Article
The Highly Dynamic Nature of ERdj5 Is Key to Efficient Elimination of Aberrant Protein Oligomers through ER-Associated Degradation.
Structure (London, England : 1993) - 6 Jun 2017
Maegawa Ken-Ichi, Watanabe Satoshi, Noi Kentaro, Okumura Masaki, Amagai Yuta, Inoue Michio, Ushioda Ryo, Nagata Kazuhiro, Ogura Teru, Inaba Kenji
Abstract excerpt
ERdj5, composed of an N-terminal J domain followed by six thioredoxin-like domains, is the largest protein disulfide isomerase family member and functions as an ER-localized disulfide reductase that enhances ER-associated degradation (ERAD). Our previous studies indicated that ERdj5 comprises two regions, the N- and C-terminal clusters, separated by a linker loop and with distinct functional roles in ERAD. We...
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