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Autophagy ENDing unproductive phase-separated endocytic protein deposits
Autophagy ( IF 13.3 ) Pub Date : 2021-08-02 , DOI: 10.1080/15548627.2021.1957567
Florian Wilfling 1, 2, 3 , Chia-Wei Lee 1, 2 , Philipp S Erdmann 2 , Wolfgang Baumeister 2
Affiliation  

ABSTRACT

Selective disposal of a wide range of cellular entities by macroautophagy/autophagy is achieved through a special class of proteins called autophagy receptors, which link corresponding cargo to the membrane-bound autophagosomal protein Atg8/LC3. In pursuit of novel autophagy receptors and their cargo, we uncovered a previously undescribed autophagy pathway for removal of aberrant clathrin-mediated endocytosis (CME) protein condensates in S. cerevisiae. Of these CME proteins, Ede1 functions as an autophagy receptor, harboring distinct Atg8-binding domains and driving phase separation into condensates. The aberrant CME condensates at the plasma membrane (PM) exhibit a drop-like structure surrounded by a fenestrated ER, which are engulfed in pieces in an Ede1-dependent manner by autophagy. Thus, our work suggests that aberrant CME is a target for autophagic degradation, with the scaffold protein Ede1 serving as a built-in autophagy receptor that monitors the assembly status of the CME machinery.



中文翻译:

自噬结束非生产性相分离的内吞蛋白沉积

摘要

通过巨自噬/自噬对多种细胞实体的选择性处理是通过一类称为自噬受体的特殊蛋白质实现的,该蛋白质将相应的货物与膜结合的自噬体蛋白 Atg8/LC3 连接起来。为了追求新的自噬受体及其货物,我们发现了一种以前未描述的自噬途径,用于去除酿酒酵母中异常网格蛋白介导的内吞 (CME) 蛋白缩合物. 在这些 CME 蛋白中,Ede1 作为自噬受体发挥作用,具有不同的 Atg8 结合结构域并驱动相分离形成凝聚物。质膜 (PM) 处的异常 CME 冷凝物呈现出被有孔 ER 包围的滴状结构,其被自噬以依赖 Ede1 的方式吞噬成碎片。因此,我们的工作表明异常 CME 是自噬降解的靶标,支架蛋白 Ede1 作为一种内置的自噬受体,可监测 CME 机器的组装状态。

更新日期:2021-08-02
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