USP14 inhibits ER-associated degradation via interaction with IRE1α

Atsushi Nagai, Hisae Kadowaki, Takeshi Maruyama, Kohsuke Takeda, Hideki Nishitoh*, Hidenori Ichijo

*この研究の対応する著者

研究成果: Article査読

29 被引用数 (Scopus)

抄録

Accumulation of unfolded proteins within the endoplasmic reticulum (ER) lumen induces ER stress. Eukaryotic cells possess the ER quality control systems, the unfolded protein response (UPR), to adapt to ER stress. IRE1α is one of the ER stress receptors and mediates the UPR. Here, we identified ubiquitin specific protease (USP) 14 as a binding partner of IRE1α. USP14 interacted with the cytoplasmic region of IRE1α, and the endogenous interaction between USP14 and IRE1α was inhibited by ER stress. Overexpression of USP14 inhibited the ER-associated degradation (ERAD) pathway, and USP14 depletion by small interfering RNA effectively activated ERAD. These findings suggest that USP14 is a novel player in the UPR by serving as a physiological inhibitor of ERAD under the non-stressed condition.

本文言語English
ページ(範囲)995-1000
ページ数6
ジャーナルBiochemical and Biophysical Research Communications
379
4
DOI
出版ステータスPublished - 2009 2 20
外部発表はい

ASJC Scopus subject areas

  • 生物理学
  • 生化学
  • 分子生物学
  • 細胞生物学

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