Regulation of cellular polyamines by antizyme
- 1 March 2001
- journal article
- review article
- Published by Springer Nature in Nature Reviews Molecular Cell Biology
- Vol. 2 (3), 188-194
- https://doi.org/10.1038/35056508
Abstract
Proteins that are degraded by the proteasome are first modified by a set of enzymes that attach multiple copies of ubiquitin to substrate lysines, but a tiny minority, including the polyamine-synthesizing enzyme ornithine decarboxylase, is handled differently. This enzyme is targeted for destruction by another protein ? antizyme. Why does ornithine decarboxylase have its own dedicated destruction mechanism, how does it work, and is it the only protein to be targeted to the proteasome in this way?Keywords
This publication has 38 references indexed in Scilit:
- Exportin 4: a mediator of a novel nuclear export pathway in higher eukaryotesThe EMBO Journal, 2000
- Functional interaction between GCN5 and polyamines: a new role for core histone acetylationThe EMBO Journal, 1999
- Structure of mammalian ornithine decarboxylase at 1.6 Å resolution: stereochemical implications of PLP-dependent amino acid decarboxylasesStructure, 1999
- Autoregulatory frameshifting in decoding mammalian ornithine decarboxylase antizymeCell, 1995
- Potassium channel block by cytoplasmic polyamines as the mechanism of intrinsic rectificationNature, 1994
- Is hypusine essential for eukaryotic cell proliferation?Trends in Biochemical Sciences, 1993
- POLYAMINESAnnual Review of Biochemistry, 1984
- The Preparation and Properties of Gel-Filtered Rabbit-Reticulocyte Lysate Protein-Synthesis SystemsEuropean Journal of Biochemistry, 1983
- Cadaverine and putrescine initiate the burial of dead conspecifics by ratsPhysiology & Behavior, 1981
- Induction of a protein inhibitor to ornithine decarboxylase by the end products of its reaction.Proceedings of the National Academy of Sciences, 1976