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The E2 Ubiquitin-conjugating Enzyme UBE2J1 Is Required for Spermiogenesis in Mice

Author(s)
Koenig, Paul-Albert; Hagiwara, Masatoshi; Maruyama, Takeshi; Watson, Nicki; Page, David C; Nicholls, Peter; Schmidt, Florian Ingo; Ploegh, Hidde; Frydman, Galit H.; ... Show more Show less
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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.
Date issued
2014-10
URI
http://hdl.handle.net/1721.1/108038
Department
Massachusetts Institute of Technology. Department of Biology; Massachusetts Institute of Technology. Division of Comparative Medicine; Whitehead Institute for Biomedical Research
Journal
Journal of Biological Chemistry
Publisher
American Society for Biochemistry and Molecular Biology (ASBMB)
Citation
Koenig, Paul-Albert, Peter K. Nicholls, Florian I. Schmidt, Masatoshi Hagiwara, Takeshi Maruyama, Galit H. Frydman, Nicki Watson, David C. Page, and Hidde L. Ploegh. “The E2 Ubiquitin-Conjugating Enzyme UBE2J1 Is Required for Spermiogenesis in Mice.” Journal of Biological Chemistry 289, no. 50 (October 15, 2014): 34490–34502. © 2014 American Society for Biochemistry and Molecular Biology, Inc. (ASBMB)
Version: Author's final manuscript
ISSN
0021-9258
1083-351X

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