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泛素依赖性和非依赖性蛋白质降解在细胞多胺调节中的作用

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

作者信息

Kahana C

机构信息

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

出版信息

Amino Acids. 2007 Aug;33(2):225-30. doi: 10.1007/s00726-007-0519-y. Epub 2007 Apr 4.

Abstract

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.

摘要

由泛素/蛋白酶体系统介导的蛋白质降解是细胞蛋白质降解的主要途径。在这条途径中,靶蛋白的泛素化通过几种酶的协同作用得以体现。随后,泛素化的蛋白质被26S蛋白酶体识别并降解。关于26S蛋白酶体在没有泛素化的情况下降解蛋白质的报道很少,鸟氨酸脱羧酶是这一类中最著名的代表。有趣的是,虽然鸟氨酸脱羧酶的降解不依赖于泛素化,但多胺生物合成途径中其他酶的降解则依赖于泛素。本综述描述了多胺生物合成途径中酶和调节因子的降解。

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