4.4 Article

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

期刊

AMINO ACIDS
卷 33, 期 2, 页码 225-230

出版社

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

关键词

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

向作者/读者索取更多资源

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.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.4
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据