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

研究成果: Article

9 引用 (Scopus)

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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.

元の言語English
ページ(範囲)34490-34502
ページ数13
ジャーナルJournal of Biological Chemistry
289
発行部数50
DOI
出版物ステータスPublished - 2014 12 12

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ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

これを引用

Koenig, P. A., Nicholls, P. K., Schmidt, F. I., Hagiwara, M., Maruyama, T., Frydman, G. H., Watson, N., Page, D. C., & Ploegh, H. L. (2014). The E2 ubiquitin-conjugating enzyme UBE2J1 is required for spermiogenesis in mice. Journal of Biological Chemistry, 289(50), 34490-34502. https://doi.org/10.1074/jbc.M114.604132