期刊
CRITICAL REVIEWS IN BIOCHEMISTRY AND MOLECULAR BIOLOGY
卷 47, 期 1, 页码 17-28出版社
TAYLOR & FRANCIS LTD
DOI: 10.3109/10409238.2011.620943
关键词
Ubiquitin; monoubiquitination; ubiquitin conjugating enzymes/E2; histone; coupled monoubiquitination; ubiquitin-like proteins; ubiquitin chain; endocytosis
资金
- NIH
- National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK)
Post-translational modification of proteins with ubiquitin regulates a variety of eukaryotic cellular processes. Ubiquitin can be conjugated to substrates either as a single moiety (monoubiquitination) or as isopeptide bond-linked chains (polyubiquitination), creating an array of ubiquitin signals. It has been established that monoubiquitination can serve important functions in many biological processes such as the regulation of gene transcription, protein trafficking, and DNA repair. Surprisingly, little is known about the mechanisms by which monoubiquitin signals are produced in the cell. Here, we discuss the potential cellular strategies for generating monoubiquitinated proteins using a few, relatively well characterized examples of monoubiquitinated proteins. These strategies include coupling ubiquitination to low affinity ubiquitin binding, using monoubiquitination-dedicated E2 conjugating enzymes, and restricting ubiquitin chain elongation. Some of these principles may be applicable to protein modifications involving ubiquitin like proteins (UBLs), which often occur in monomeric form.
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