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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Brzovic, Peter S. Vittal, Vinayak Stewart, Mikaela D. Klevit, Rachel E. |
| Description | Author Affiliation: Vittal V ( From the Department of Biochemistry, University of Washington, Seattle, Washington 98195-7742.); Stewart MD ( From the Department of Biochemistry, University of Washington, Seattle, Washington 98195-7742.); Brzovic PS ( From the Department of Biochemistry, University of Washington, Seattle, Washington 98195-7742.); Klevit RE ( From the Department of Biochemistry, University of Washington, Seattle, Washington 98195-7742 klevit@uw.edu.) |
| Abstract | Since its discovery as a post-translational signal for protein degradation, our understanding of ubiquitin (Ub) has vastly evolved. Today, we recognize that the role of Ub signaling is expansive and encompasses diverse processes including cell division, the DNA damage response, cellular immune signaling, and even organismal development. With such a wide range of functions comes a wide range of regulatory mechanisms that control the activity of the ubiquitylation machinery. Ub attachment to substrates occurs through the sequential action of three classes of enzymes, E1s, E2s, and E3s. In humans, there are 2 E1s, â ¼ 35 E2s, and hundreds of E3s that work to attach Ub to thousands of cellular substrates. Regulation of ubiquitylation can occur at each stage of the stepwise Ub transfer process, and substrates can also impact their own modification. Recent studies have revealed elegant mechanisms that have evolved to control the activity of the enzymes involved. In this minireview, we highlight recent discoveries that define some of the various mechanisms by which the activities of E3-Ub ligases are regulated. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 35 |
| Volume Number | 290 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2015-08-28 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Ubiquitin-Protein Ligases Metabolism Animals Cullin Proteins Models, Molecular Ubiquitin Chemistry Ubiquitination Research Support, N.I.H., Extramural Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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