Ubiquitin-like Protein Conjugation: Structures, Chemistry, and Mechanism.

Ubiquitin-like Protein Conjugation: Structures, Chemistry, and Mechanism.
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DOI:
10.1021/acs.chemrev.6b00737
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发表时间:
2018-02-14
期刊:
影响因子:
62.1
通讯作者:
Lima CD
Lima CD
中科院分区:
化学1区
文献类型:
--
作者:
Cappadocia L;Lima CD

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泛素样蛋白(Ubl‘s)与靶蛋白或脂类结合,调节其活性、稳定性、亚细胞定位或大分子相互作用。与泛素类似,结合是通过一系列的活性来实现的,这些活性是由E1激活酶、E2结合酶和E3连接酶催化的。在这篇综述中,我们将对参与Ub1共联级联的酶和蛋白质辅因子的结构和机制细节进行综述。准确地说,我们将重点关注相扑、NEDD8、ATG8、ATG12、URM1、UFM1、FAT10和ISG15途径中的接合机制,同时参考泛素途径来突出共同或对比的主题。我们还将回顾在UbL激活和接合过程中用于捕获中间体的各种策略。
Ubiquitin-like proteins (Ubl’s) are conjugated to target proteins or lipids to regulate their activity, stability, subcellular localization, or macromolecular interactions. Similar to ubiquitin, conjugation is achieved through a cascade of activities that are catalyzed by E1 activating enzymes, E2 conjugating enzymes, and E3 ligases. In this review, we will summarize structural and mechanistic details of enzymes and protein cofactors that participate in Ubl conjugation cascades. Precisely, we will focus on conjugation machinery in the SUMO, NEDD8, ATG8, ATG12, URM1, UFM1, FAT10, and ISG15 pathways while referring to the ubiquitin pathway to highlight common or contrasting themes. We will also review various strategies used to trap intermediates during Ubl activation and conjugation.
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