Structural and functional insights to ubiquitin-like protein conjugation.

Structural and functional insights to ubiquitin-like protein conjugation.
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DOI:
10.1146/annurev-biophys-051013-022958
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发表时间:
2014
影响因子:
12.4
通讯作者:
Lima CD
Lima CD
中科院分区:
生物学1区
文献类型:
--
作者:
Streich FC Jr;Lima CD

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泛素(Ub)和泛素样蛋白(Ubls)附着在细胞蛋白上调节许多细胞过程,包括转录、细胞周期、应激反应、DNA修复、细胞凋亡、免疫反应和自噬等。机制上平行但功能上不同的偶联途径通常需要三种蛋白质的协同活动:E1 Ubl激活酶、E2 Ubl载体蛋白和E3 Ubl连接酶。E1酶通过识别和激活同源Ubl启动每个级联的通路特异性,然后催化Ubl转移到同源E2蛋白。在某些情况下,E2 Ubl复合物可以直接连接到目标蛋白,但大多数情况下需要E3连接酶的协同活性。本文回顾了最近的结构和功能研究,以提高我们对E1-, E2-和e3介导的Ubl偶联的机制理解。
Attachment of ubiquitin (Ub) and ubiquitin-like proteins (Ubls) to cellular proteins regulates numerous cellular processes including transcription, the cell cycle, stress responses, DNA repair, apoptosis, immune responses, and autophagy, to name a few. The mechanistically parallel but functionally distinct conjugation pathways typically require the concerted activities of three types of protein: E1 Ubl-activating enzymes, E2 Ubl carrier proteins, and E3 Ubl ligases. E1 enzymes initiate pathway specificity for each cascade by recognizing and activating cognate Ubls, followed by catalyzing Ubl transfer to cognate E2 protein(s). Under certain circumstances, the E2 Ubl complex can direct ligation to the target protein, but most often requires the cooperative activity of E3 ligases. Reviewed here are recent structural and functional studies that improve our mechanistic understanding of E1-, E2-, and E3-mediated Ubl conjugation.
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