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  Autophagy ENDing unproductive phase-separated endocytic protein deposits

Wilfling, F., Lee, C.-W., Erdmann, P. S., & Baumeister, W. (2021). Autophagy ENDing unproductive phase-separated endocytic protein deposits. Autophagy, 17(10), 3264-3265. doi:10.1080/15548627.2021.1957567.

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Genre: Journal Article

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 Creators:
Wilfling, Florian1, Author              
Lee, Chia-Wei1, Author              
Erdmann, Philipp S.2, Author              
Baumeister, Wolfgang2, Author              
Affiliations:
1Jentsch, Stefan / Molecular Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565156              
2Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              

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Free keywords: Cell Biology; Cathrin-mediated endocytosis; selective autophagy; Ede1; intrinsic receptor; phase separation; budding yeast; Atg11
 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.

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Language(s): eng - English
 Dates: 2021-07-152021-07-152021-07-142021-08-022021-10
 Publication Status: Published in print
 Pages: 2
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: Autophagy
Source Genre: Journal
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Publ. Info: Georgetown, TX : Landes Bioscience
Pages: - Volume / Issue: 17 (10) Sequence Number: - Start / End Page: 3264 - 3265 Identifier: ISSN: 1554-8627
CoNE: https://pure.mpg.de/cone/journals/resource/1000000000238500