期刊
CELL DEATH AND DIFFERENTIATION
卷 18, 期 9, 页码 1393-1402出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/cdd.2011.16
关键词
ubiquitin; E3 ligase; self-ubiquitination; proteasomal degradation
资金
- Dr. Miriam and Sheldon Adelson Foundation for Medical research (AMRF)
- Israel Science Foundation (ISF)
- German-Israeli Foundation for Research and Scientific Development (GIF)
- Rubicon European Union (EU) Network of Excellence
- Israel Cancer Research Fund (ICRF) USA Professorship
- Foundation for Promotion of Research in the Technion
Ubiquitin modification of many cellular proteins targets them for proteasomal degradation, but in addition can also serve non-proteolytic functions. Over the last years, a significant progress has been made in our understanding of how modification of the substrates of the ubiquitin system is regulated. However, little is known on how the ubiquitin system that is comprised of similar to 1500 components is regulated. Here, we discuss how the biggest subfamily within the system, that of the E3 ubiquitin ligases that endow the system with its high specificity towards the numerous substrates, is regulated and in particular via self-regulation mediated by ubiquitin modification. Ligases can be targeted for degradation in a self-catalyzed manner, or through modification mediated by an external ligase(s). In addition, non-proteolytic functions of self-ubiquitination, for example activation of the ligase, of E3s are discussed. Cell Death and Differentiation (2011) 18, 1393-1402; doi:10.1038/cdd.2011.16; published online 4 March 2011
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