The role of ubiquitylation for the control of cell death in Drosophila.

The role of ubiquitylation for the control of cell death in Drosophila.
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DOI:
10.1038/cdd.2009.70
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发表时间:
2010-01
影响因子:
12.4
通讯作者:
--
中科院分区:
生物学1区
文献类型:
--
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泛素化描述了一个过程,其中泛素,一个76个氨基酸的多肽,共价连接到靶蛋白。传统上,泛素缀合蛋白被26S蛋白酶体靶向降解。然而,非蛋白水解作用的组蛋白调节,DNA修复和信号转导已被报道。本文就泛素化在果蝇细胞死亡途径中的作用进行综述。有趣的是,泛素化同时具有促凋亡和抗凋亡的功能。虽然促凋亡泛素化导致蛋白水解降解,最近的证据表明,抗凋亡泛素化可能涉及,至少部分,非蛋白水解功能。
Ubiquitylation describes a process in which ubiquitin, a 76-amino-acid polypeptide, is covalently attached to target proteins. Traditionally, ubiquitin-conjugated proteins are targeted for degradation by the 26S proteasome. However, non-proteolytic roles in histone regulation, DNA repair and signal transduction have been reported. Here, the role of ubiquitylation in the cell death pathway in Drosophila is reviewed. Interestingly, ubiquitylation serves both pro- and anti-apoptotic functions. Although pro-apoptotic ubiquitylation leads to proteolytic degradation, recent evidence suggests that anti-apoptotic ubiquitylation may involve, at least in part, non-proteolytic functions.
DOI: 10.1038/sj.cdd.4402079
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