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?
Coffino
P
P
Department of Microbiology and Immunology and Department of Medicine, University of California, San Francisco, San Francisco, California 94143-0414, USA. pcoffin@itsa.ucsf.edu
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