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  4. Autophagy ENDing unproductive phase-separated endocytic protein deposits
 
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Autophagy ENDing unproductive phase-separated endocytic protein deposits

Journal
Autophagy
Journal Volume
17
Journal Issue
10
Pages
3264-3265
Date Issued
2021-08-02
Author(s)
Florian Wilfling
CHIA-WEI LEE  
Philipp S. Erdmann
Wolfgang Baumeister
DOI
10.1080/15548627.2021.1957567
URI
https://scholars.lib.ntu.edu.tw/handle/123456789/634060
URL
http://dx.doi.org/10.1080/15548627.2021.1957567
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.
Subjects
Atg11; Cathrin-mediated endocytosis; Ede1; budding yeast; intrinsic receptor; phase separation; selective autophagy
Publisher
Informa {UK} Limited
Type
journal article

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