Degradation of ornithine decarboxylase by the 26S proteasome
- PMID: 10623564
- DOI: 10.1006/bbrc.1999.1706
Degradation of ornithine decarboxylase by the 26S proteasome
Abstract
Ornithine decarboxylase (ODC) is a key enzyme in polyamine biosynthesis. Turnover of ODC is extremely rapid and highly regulated, and is accelerated when polyamine levels increase. Polyamine-stimulated ODC degradation is mediated by association with antizyme (AZ), an ODC inhibitory protein induced by polyamines. ODC, in association with AZ, is degraded by the 26S proteasome in an ATP-dependent, but ubiquitin-independent, manner. The 26S proteasome irreversibly inactivates ODC prior to its degradation. The inactivation, possibly due to unfolding, is coupled to sequestration of ODC within the 26S proteasome. This process requires AZ and ATP, but not proteolytic activity of the 26S proteasome. The carboxyl-terminal region of ODC presumably exposed by interaction with AZ plays a critical role for being trapped by the 26S proteasome. Thus, the degradation pathway of ODC proceeds as a sequence of multiple distinct processes, including recognition, sequestration, unfolding, translocation, and ultimate degradation mediated by the 26S proteasome.
Copyright 2000 Academic Press.
Similar articles
-
Nuclear translocation of antizyme and expression of ornithine decarboxylase and antizyme are developmentally regulated.Dev Dyn. 2001 Mar;220(3):259-75. doi: 10.1002/1097-0177(20010301)220:3<259::AID-DVDY1100>3.0.CO;2-#. Dev Dyn. 2001. PMID: 11241834
-
Ornithine decarboxylase is degraded by the 26S proteasome without ubiquitination.Nature. 1992 Dec 10;360(6404):597-9. doi: 10.1038/360597a0. Nature. 1992. PMID: 1334232
-
Ornithine decarboxylase antizyme: a novel type of regulatory protein.Trends Biochem Sci. 1996 Jan;21(1):27-30. Trends Biochem Sci. 1996. PMID: 8848835 Review.
-
ATP-Dependent inactivation and sequestration of ornithine decarboxylase by the 26S proteasome are prerequisites for degradation.Mol Cell Biol. 1999 Oct;19(10):7216-27. doi: 10.1128/MCB.19.10.7216. Mol Cell Biol. 1999. PMID: 10490656 Free PMC article.
-
Regulation of cellular polyamine levels and cellular proliferation by antizyme and antizyme inhibitor.Essays Biochem. 2009 Nov 4;46:47-61. doi: 10.1042/bse0460004. Essays Biochem. 2009. PMID: 20095969 Review.
Cited by
-
Regulation of Immunogen Processing: Signal Sequences and Their Application for the New Generation of DNA-Vaccines.Acta Naturae. 2010 Apr;2(1):53-60. Acta Naturae. 2010. PMID: 22649628 Free PMC article.
-
The midnolin-proteasome pathway catches proteins for ubiquitination-independent degradation.Science. 2023 Aug 25;381(6660):eadh5021. doi: 10.1126/science.adh5021. Epub 2023 Aug 25. Science. 2023. PMID: 37616343 Free PMC article.
-
Two Degradation Pathways of the p35 Cdk5 (Cyclin-dependent Kinase) Activation Subunit, Dependent and Independent of Ubiquitination.J Biol Chem. 2016 Feb 26;291(9):4649-57. doi: 10.1074/jbc.M115.692871. Epub 2015 Dec 2. J Biol Chem. 2016. PMID: 26631721 Free PMC article.
-
Growth-inhibitory effects of the chemopreventive agent indole-3-carbinol are increased in combination with the polyamine putrescine in the SW480 colon tumour cell line.BMC Cancer. 2003 Jan 14;3:2. doi: 10.1186/1471-2407-3-2. Epub 2003 Jan 14. BMC Cancer. 2003. PMID: 12525265 Free PMC article.
-
Ubiquitination is essential for human cytomegalovirus US11-mediated dislocation of MHC class I molecules from the endoplasmic reticulum to the cytosol.Biochem J. 2001 Sep 1;358(Pt 2):369-77. doi: 10.1042/0264-6021:3580369. Biochem J. 2001. PMID: 11513735 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases
Research Materials
