Regulation of cellular polyamines by antizyme.
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?
Department of Microbiology and Immunology and Department of Medicine, University of California, San Francisco, San Francisco, California 94143-0414, USA. pcoffin@itsa.ucsf.edu
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D000818:Animals; D015317:Biogenic Polyamines / Q000378:metabolism*; D003546:Cysteine Endopeptidases / Q000378:metabolism; D004791:Enzyme Inhibitors / Q000378:metabolism*; D006801:Humans; D008954:Models, Biological; D009097:Multienzyme Complexes / Q000378:metabolism; D009955:Ornithine Decarboxylase / Q000378:metabolism*; D065108:Ornithine Decarboxylase Inhibitors; D046988:Proteasome Endopeptidase Complex
D015317:Biogenic Polyamines; D004791:Enzyme Inhibitors; D009097:Multienzyme Complexes; D065108:Ornithine Decarboxylase Inhibitors; D003546:Cysteine Endopeptidases; D046988:Proteasome Endopeptidase Complex; D009955:Ornithine Decarboxylase