The predator becomes the prey: regulating the ubiquitin system by ubiquitylation and degradation

Key Points Monomeric ubiquitin is relatively stable; however, it appears to be degraded by the proteasome following its own ubiquitylation, which is mediated by the thyroid receptor-interacting protein 12 (TRIP12) ligase. Ubiquitin is also degraded through two other mechanisms: along with the target...

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Bibliographic Details
Published in:	Nature reviews. Molecular cell biology Vol. 12; no. 9; pp. 605 - 620
Main Authors:	Weissman, Allan M., Shabek, Nitzan, Ciechanover, Aaron
Format:	Journal Article
Language:	English
Published:	London Nature Publishing Group UK 01.09.2011 Nature Publishing Group
Subjects:	631/337/474/2085 631/337/474/582 631/45/612/645 Animals Biochemistry Biomedical and Life Sciences Cancer Research Cell Biology Cell cycle Cellular proteins Developmental Biology Enzymes Food Chain Humans Life Sciences Models, Biological Physiological aspects Proteasome Endopeptidase Complex - metabolism Proteasome Endopeptidase Complex - physiology Protein Processing, Post-Translational - physiology Proteins review-article Stem Cells Ubiquitin Ubiquitin - metabolism Ubiquitin-proteasome system Ubiquitination - physiology Wit and Humor as Topic United States Israel
ISSN:	1471-0072, 1471-0080, 1471-0080
Online Access:	Get full text
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