The E2 ubiquitin-conjugating enzyme UBE2J1 is required for spermiogenesis in mice

Paul Albert Koenig, Peter K. Nicholls, Florian I. Schmidt, Masatoshi Hagiwara, Takeshi Maruyama, Galit H. Frydman, Nicki Watson, David C. Page, Hidde L. Ploegh*

*この研究の対応する著者

研究成果: Article査読

18 被引用数 (Scopus)

抄録

ER-resident proteins destined for degradation are dislocated into the cytosol by components of the ER quality control machinery for proteasomal degradation. Dislocation substrates are ubiquitylated in the cytosol by E2 ubiquitin-conjugating/E3 ligase complexes. UBE2J1 is one of the well-characterized E2 enzymes that participate in this process. However, the physiological function of Ube2j1 is poorly defined. We find that Ube2j1-/- mice have reduced viability and fail to thrive early after birth. Male Ube2j1-/- mice are sterile due to a defect in late spermatogenesis. Ultrastructural analysis shows that removal of the cytoplasm is incomplete in Ube2j1-/- elongating spermatids, compromising the release of mature elongate spermatids into the lumen of the seminiferous tubule. Our findings identify an essential function for the ubiquitin-proteasome-system in spermiogenesis and define a novel, non-redundant physiological function for the dislocation step of ER quality control.

本文言語English
ページ(範囲)34490-34502
ページ数13
ジャーナルJournal of Biological Chemistry
289
50
DOI
出版ステータスPublished - 2014 12 12
外部発表はい

ASJC Scopus subject areas

  • 生化学
  • 分子生物学
  • 細胞生物学

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