<br>Atg8-家族蛋白质-自噬及其他领域的结构特征和分子相互作用。,Cells

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Atg8-家族蛋白质-自噬及其他领域的结构特征和分子相互作用。
Cells ( IF 5.1 ) Pub Date : 2020-09-01 , DOI: 10.3390/cells9092008
Nicole Wesch ₁ , Vladimir Kirkin ₂ , Vladimir V Rogov _{1,

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Affiliation

自噬是许多分解代谢过程的通用名称，它通过去除受损和功能失调的细胞内成分来保持细胞稳态。自噬受损或失衡可导致多种疾病，如神经退行性疾病、感染性疾病和癌症。自噬的中心轴是沿着自噬修饰剂（Atg8 家族蛋白）与其各种细胞反配体相互作用形成的。除了自噬之外，Atg8 蛋白还参与许多其他途径，其中最著名的是膜运输和神经元信号传导。尽管自噬修饰剂已得到充分研究，但由于小球状蛋白在结构水平上与泛素相似，但它们相互作用的机制仍不完全清楚。对 Atg8-蛋白质相互作用的所有已知机制进行彻底分析和分类可以揭示它们的功能并连接涉及 Atg8-蛋白质的途径。在这篇综述中，我们提出了对 Atg8 蛋白关键特征的看法，并描述了它们被相互作用伙伴识别和结合的基本原理。我们讨论了它们相互作用的亲和力和选择性，并为发现新的 Atg8 相互作用蛋白和解决人类主要疾病的治疗方法提供了前景。

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Atg8-Family Proteins-Structural Features and Molecular Interactions in Autophagy and Beyond.

Autophagy is a common name for a number of catabolic processes, which keep the cellular homeostasis by removing damaged and dysfunctional intracellular components. Impairment or misbalance of autophagy can lead to various diseases, such as neurodegeneration, infection diseases, and cancer. A central axis of autophagy is formed along the interactions of autophagy modifiers (Atg8-family proteins) with a variety of their cellular counter partners. Besides autophagy, Atg8-proteins participate in many other pathways, among which membrane trafficking and neuronal signaling are the most known. Despite the fact that autophagy modifiers are well-studied, as the small globular proteins show similarity to ubiquitin on a structural level, the mechanism of their interactions are still not completely understood. A thorough analysis and classification of all known mechanisms of Atg8-protein interactions could shed light on their functioning and connect the pathways involving Atg8-proteins. In this review, we present our views of the key features of the Atg8-proteins and describe the basic principles of their recognition and binding by interaction partners. We discuss affinity and selectivity of their interactions as well as provide perspectives for discovery of new Atg8-interacting proteins and therapeutic approaches to tackle major human diseases.

更新日期：2020-09-01

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