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

Ubiquitin dependent and independent protein degradation in the regulation of cellular polyamines. Research Abstract Details 

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Ubiquitin dependent and independent protein degradation in the regulation of cellular polyamines. Abstract Text:

C Kahana,C Kahana,C Kahana,

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.

Ubiquitin dependent and independent protein degradation in the regulation of cellular polyamines. Publishing Authors By Initials

C Kahana,C Kahana,C Kahana,

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Ubiquitin dependent and independent protein degradation in the regulation of cellular polyamines. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Amino acids

VOLUME: 33

Page Numbers: 225-30

Journal Abbreviation: Amino Acids

ISSN: 0939-4451

DAY: 4

MONTH: 04

YEAR: 2007

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

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LANGUAGE: eng

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Grant and Affiliation Information for Ubiquitin dependent and independent protein degradation in the regulation of cellular polyamines.

AFFILIATION: Department of Molecular Genetics, The Weizmann Institute of Science, Rehovot, Israel.

Country: Austria

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MEDLINETA: Amino Acids

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