at8和Atg12偶联体系的结构生物学

Nobuo N. Noda
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引用次数: 0

摘要

at8和Atg12是泛素样蛋白,分别通过类似泛素化的酶促反应与磷脂酰乙醇胺(PE)和Atg5结合。由此产生的Atg8-PE和Atg12-Atg5偶联物在自噬中起着至关重要的作用。对所有参与这些偶联系统的Atg蛋白(Atg3, Atg4, Atg5, Atg7, Atg8, Atg10, Atg12, Atg16)进行了广泛的结构研究。本文综述了at8和Atg12偶联体系的结构研究,讨论了at8和Atg12偶联体系的偶联和解偶联反应机制以及自噬功能。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Structural biology of the Atg8 and Atg12 conjugation systems
Atg8 and Atg12 are ubiquitin-like proteins, conjugated to phosphatidylethanolamine (PE) and Atg5, respectively, through enzymatic reactions similar to ubiquitylation. The resultant Atg8–PE and Atg12–Atg5 conjugates play crucial roles in autophagy. Structural studies have been extensively performed on all Atg proteins (Atg3, Atg4, Atg5, Atg7, Atg8, Atg10, Atg12, Atg16) involved in these conjugation systems. This review summarizes structural studies and discusses mechanisms of conjugation and deconjugation reactions, as well as autophagic functions of the Atg8 and Atg12 conjugation systems.
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