期刊
EMBO REPORTS
卷 16, 期 2, 页码 192-201出版社
WILEY-BLACKWELL
DOI: 10.15252/embr.201439152
关键词
acetylation; mechanism; post-translational modification; ubiquitin
资金
- JSPS KAKENHI [24112004, 23657112, 24112008, 24112005, 26000014]
- MEXT
- Grants-in-Aid for Scientific Research [26870853, 26670730, 26000014, 24112008, 24112004, 23657112, 26291035, 24112005, 26290042] Funding Source: KAKEN
Ubiquitylation is a versatile post-translational modification (PTM). The diversity of ubiquitylation topologies, which encompasses different chain lengths and linkages, underlies its widespread cellular roles. Here, we show that endogenous ubiquitin is acetylated at lysine (K)-6 (AcK6) or K48. Acetylated ubiquitin does not affect substrate monoubiquitylation, but inhibits K11-, K48-, and K63-linked polyubiquitin chain elongation by several E2 enzymes in vitro. In cells, AcK6-mimetic ubiquitin stabilizes the monoubiquitylation of histone H2B-which we identify as an endogenous substrate of acetylated ubiquitin-and of artificial ubiquitin fusion degradation substrates. These results characterize a mechanism whereby ubiquitin, itself a PTM, is subject to another PTM to modulate mono-and polyubiquitylation, thus adding a new regulatory layer to ubiquitin biology.
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