Taking it step by step: mechanistic insights from structural studies of ubiquitin/ubiquitin-like protein modification pathways

被引：93

作者：

Capili, Allan D. ^{[1
]}

Lima, Christopher D. ^{[1
]}

机构：

[1] Sloan Kettering Inst, Struct Biol Program, New York, NY 10065 USA

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2007年 / 17卷 / 06期

关键词：

D O I：

10.1016/j.sbi.2007.08.018

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Ubiquitin (Ub) and ubiquitin-like (Ubl) proteins regulate a diverse array of cellular pathways through post-translational attachment to protein substrates. Ub/Ubl-mediated signaling is initiated through E1, E2, and E3-mediated conjugation, transduced by proteins that recognize Ub/Ubl-modified substrates, and terminated by proteases which remove the Ub/Ubl from the substrate. Recent structural studies have elucidated mechanisms pertinent to Ub/Ubl conjugation, recognition, and deconjugation, highlighting essential steps during Ub/Ubl modification that illustrate common and divergent mechanistic themes within this important process.

引用

页码：726 / 735

页数：10

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