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

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)34490-34502
Number of pages13
JournalJournal of Biological Chemistry
Volume289
Issue number50
DOIs
Publication statusPublished - 2014 Dec 12
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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    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