Proteasome-independent functions of ubiquitin in endocytosis and signaling

被引：963

作者：

Mukhopadhyay, Debdyuti ^{[1
]}

Riezman, Howard ^{[1
]}

机构：

[1] Univ Geneva, Dept Biochem, CH-1211 Geneva, Switzerland

来源：

SCIENCE | 2007年 / 315卷 / 5809期

关键词：

D O I：

10.1126/science.1127085

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Ubiquitination is a reversible posttranslational modification of cellular proteins, in which a 76-amino acid polypeptide, ubiquitin, is primarily attached to the epsilon-amino group of lysines in target proteins. Ubiquitination is a major player in regulating a broad host of cellular processes, including cell division, differentiation, signal transduction, protein trafficking, and quality control. Aberrations in the ubiquitination system are implicated in pathogenesis of some diseases, certain malignancies, neurodegenerative disorders, and pathologies of the inflammatory immune response. Here, we discuss the proteasome-independent roles of ubiquitination in signaling and endocytosis.

引用

页码：201 / 205

页数：5

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