The ubiquitin system
- PMID: 9759494
- DOI: 10.1146/annurev.biochem.67.1.425
The ubiquitin system
Abstract
The selective degradation of many short-lived proteins in eukaryotic cells is carried out by the ubiquitin system. In this pathway, proteins are targeted for degradation by covalent ligation to ubiquitin, a highly conserved small protein. Ubiquitin-mediated degradation of regulatory proteins plays important roles in the control of numerous processes, including cell-cycle progression, signal transduction, transcriptional regulation, receptor down-regulation, and endocytosis. The ubiquitin system has been implicated in the immune response, development, and programmed cell death. Abnormalities in ubiquitin-mediated processes have been shown to cause pathological conditions, including malignant transformation. In this review we discuss recent information on functions and mechanisms of the ubiquitin system. Since the selectivity of protein degradation is determined mainly at the stage of ligation to ubiquitin, special attention is focused on what we know, and would like to know, about the mode of action of ubiquitin-protein ligation systems and about signals in proteins recognized by these systems.
Similar articles
-
Ubiquitination and deubiquitination: targeting of proteins for degradation by the proteasome.Semin Cell Dev Biol. 2000 Jun;11(3):141-8. doi: 10.1006/scdb.2000.0164. Semin Cell Dev Biol. 2000. PMID: 10906270 Review.
-
Modes of regulation of ubiquitin-mediated protein degradation.J Cell Physiol. 2000 Jan;182(1):1-11. doi: 10.1002/(SICI)1097-4652(200001)182:13.0.CO;2-V. J Cell Physiol. 2000. PMID: 10567911 Review.
-
Ubiquitin-mediated protein modification and degradation.Am J Respir Cell Mol Biol. 1992 Nov;7(5):463-8. doi: 10.1165/ajrcmb/7.5.463. Am J Respir Cell Mol Biol. 1992. PMID: 1329865 Review.
-
The ubiquitin-mediated proteolytic pathway: mode of action and clinical implications.J Cell Biochem Suppl. 2000;34:40-51. doi: 10.1002/(sici)1097-4644(2000)77:34+3.0.co;2-6. J Cell Biochem Suppl. 2000. PMID: 10762014 Review.
-
The ubiquitin-proteasome pathway: on protein death and cell life.EMBO J. 1998 Dec 15;17(24):7151-60. doi: 10.1093/emboj/17.24.7151. EMBO J. 1998. PMID: 9857172 Free PMC article. Review. No abstract available.
Cited by
-
Inhibition of DNA damage-induced apoptosis through Cdc7-mediated stabilization of Tob.J Biol Chem. 2012 Nov 23;287(48):40256-65. doi: 10.1074/jbc.M112.353805. Epub 2012 Oct 12. J Biol Chem. 2012. PMID: 23066029 Free PMC article.
-
Structural Insights into the Phosphorylation-Enhanced Deubiquitinating Activity of UCHL3 and Ubiquitin Chain Cleavage Preference Analysis.Int J Mol Sci. 2022 Sep 15;23(18):10789. doi: 10.3390/ijms231810789. Int J Mol Sci. 2022. PMID: 36142702 Free PMC article.
-
A Novel Strategy to Track Lysine-48 Ubiquitination by Fluorescence Resonance Energy Transfer.Methods Mol Biol. 2021;2267:91-102. doi: 10.1007/978-1-0716-1217-0_7. Methods Mol Biol. 2021. PMID: 33786787 Free PMC article.
-
The E3 Ligase APIP10 Connects the Effector AvrPiz-t to the NLR Receptor Piz-t in Rice.PLoS Pathog. 2016 Mar 31;12(3):e1005529. doi: 10.1371/journal.ppat.1005529. eCollection 2016 Mar. PLoS Pathog. 2016. PMID: 27031246 Free PMC article.
-
New perspective on the stabilization and degradation of the F-box protein COI1 in Arabidopsis.Plant Signal Behav. 2013 Aug;8(8):e24973. doi: 10.4161/psb.24973. Epub 2013 May 15. Plant Signal Behav. 2013. PMID: 23733061 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
