Scaffold proteins in bulk and selective autophagy

被引:14
作者
Eickhorst, Christopher [1 ,2 ,3 ]
Licheva, Mariya [1 ,2 ]
Kraft, Claudine [1 ,4 ]
机构
[1] Univ Freiburg, Fac Med, Inst Biochem & Mol Biol, ZBMZ, Freiburg, Germany
[2] Univ Freiburg, Fac Biol, Freiburg, Germany
[3] Univ Freiburg, Spemann Grad Sch Biol & Med SGBM, Freiburg, Germany
[4] Univ Freiburg, CIBSS Ctr Integrat Biol Signalling Studies, Freiburg, Germany
来源
AUTOPHAGY IN HEALTH AND DISEASE | 2020年 / 172卷
基金
欧盟地平线“2020”; 欧洲研究理事会; 奥地利科学基金会;
关键词
ATG17-ATG31-ATG29; COMPLEX; ULK1; EARLY STEPS; SYNTAXIN; 17; KINASE; FIP200; CARGO; PHOSPHORYLATION; MECHANISM; ATG11;
D O I
10.1016/bs.pmbts.2020.01.009
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Autophagy is a crucial cellular degradation and recycling pathway. During autophagy double-membrane vesicles, called autophagosomes, encapsulate cellular components and deliver their cargo to the lytic compartment for degradation. Formation of autophagosomes is regulated by the Atg1 kinase complex in yeast and the homologous ULK1 kinase complex in mammals. While research on Atg1 and ULK1 has advanced our understanding of how these protein kinases function in autophagy, the other Atg1/ULK1 kinase complex members have received much less attention. Here, we focus on the functions of the Atg1 kinase complex members Atg11 and Atg17 as well as the ULK1 kinase complex member FIP200 in autophagy. These three proteins act as scaffolds in their respective complexes. Recent studies have made it evident that they have similar but also distinct functions. In this article, we review our current understanding of how these scaffold proteins function from autophagosome formation to fusion and also discuss their possible roles in diseases.
引用
收藏
页码:15 / 35
页数:21
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