4.4 Article

Ubiquitin dependent and independent protein degradation in the regulation of cellular polyamines

Journal

AMINO ACIDS
Volume 33, Issue 2, Pages 225-230

Publisher

SPRINGER WIEN
DOI: 10.1007/s00726-007-0519-y

Keywords

ornithine decarboxylase; S-adenosylmethionine decarboxylase; antizyme; antizyme inhibitor; protein degradation; ubiquitin

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Protein degradation mediated by the ubiquitin/proteasome system is the major route for the degradation of cellular proteins. In this pathway the ubiquitination of the target proteins is manifested via the concerted action of several enzymes. The ubiquinated proteins are then recognized and degraded by the 26S proteasome. There are few reports of proteins degraded by the 26S protesome without ubiquitination, with ornithine decarboxylase being the most notable representative of this group. Interestingly, while the degradation of ODC is independent of ubiquitination, the degradation of other enzymes of the polyamine biosynthesis pathway is ubiquitin dependent. The present review describes the degradation of enzymes and regulators of the polyamine biosynthesis pathway.

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