Life Sciences Institute, University of Michigan, Ann Arbor, MI, USA.
Autophagy. 2021 Aug;17(8):1805-1808. doi: 10.1080/15548627.2021.1954457. Epub 2021 Jul 31.
The Atg3 protein is highly homologous from yeast to human. Atg3 functions as an E2-like enzyme promoting conjugation of Atg8-family proteins to phosphatidylethanolamine (PE), a lipid molecule embedded in the growing phagophore membrane during stress-induced autophagy. Over the last decade, Atg3 became one of the most explored autophagy proteins, resulting in observations that provided specific insights into the structural mechanisms of its function. In this article, we describe a recent study by Ye et al. that reveals, using the human ATG3, how the membrane binding capability of the enzyme is tightly linked to its conjugation activity. We summarize the current knowledge on important mechanisms that involve protein-protein or protein-membrane interactions of Atg3 and that ultimately lead to efficient Atg8-PE conjugation. AH: amphipathic helix; FR: flexible region; HR: handle region; NMR: nuclear magnetic resonance.
Atg3 蛋白在从酵母到人之间具有高度同源性。Atg3 作为一种 E2 样酶，可促进 Atg8 家族蛋白与磷脂酰乙醇胺（PE）的缀合，PE 是应激诱导自噬过程中生长的吞噬体膜中的一种脂质分子。在过去的十年中，Atg3 成为研究最多的自噬蛋白之一，其观察结果提供了对其功能结构机制的具体见解。在本文中，我们描述了 Ye 等人的一项最新研究，该研究使用人 ATG3 揭示了酶的膜结合能力与其缀合活性如何紧密相关。我们总结了涉及 Atg3 的蛋白-蛋白或蛋白-膜相互作用的重要机制的最新知识，这些机制最终导致有效的 Atg8-PE 缀合。AH：两亲性螺旋；FR：柔性区域；HR：手柄区域；NMR：核磁共振。
