Journal
SCIENTIFIC REPORTS
Volume 6, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/srep36780
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Funding
- Ministry of Education, Culture, Sports, Science, and Technology
- Takeda Science Foundation
- Mochida Memorial Foundation for Medical and Pharmaceutical Research
- Daiichi Sankyo Foundation of Life Science
- MEXT/JSPS KAKENHI [25460946, 26221307, 15H04808, 16K15423]
- Research Center Network Program for Realization of Regenerative Medicine from the Japan Science and Technology Agency (JST)
- Japan Agency for Medical Research and Development (AMED)
- Practical Research Project for Rare/Intractable Diseases from AMED [15AeK0109047h0002]
- Practical Research Project for Innovative Cancer Control from AMED [15Ack0106017h0002]
- Grants-in-Aid for Scientific Research [15K15288, 15H04808, 25460946, 16H05286, 16K15423] Funding Source: KAKEN
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Ubiquitination is a crucial post-translational modification; however, the functions of ubiquitin-coding genes remain unclear. UBA52 encodes a fusion protein comprising ubiquitin at the N-terminus and ribosomal protein L40 (RPL40) at the C-terminus. Here we showed that Uba52-deficient mice die during embryogenesis. UBA52-deficient cells exhibited normal levels of total ubiquitin. However, UBA52-deficient cells displayed decreased protein synthesis and cell-cycle arrest. The overexpression of UBA52 ameliorated the cell-cycle arrest caused by UBA52 deficiency. Surprisingly, RPL40 expression itself is insufficient to regulate cyclin D expression. The cleavage of RPL40 from UBA52 was required for maintaining protein synthesis. Furthermore, we found that RPL40 formed a ribosomal complex with ubiquitin cleaved from UBA52. UBA52 supplies RPL40 and ubiquitin simultaneously to the ribosome. Our study demonstrated that the ubiquitin-coding gene UBA52 is not just an ubiquitin supplier to the ubiquitin pool but is also a regulator of the ribosomal protein complex. These findings provide novel insights into the regulation of ubiquitin-dependent translation and embryonic development.
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