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Autophagic Clearance of PolyQ Proteins Mediated by Ubiquitin-Atg8 Adaptors of the Conserved CUET Protein Family

Lu, Kefeng, Psakhye, Ivan, Jentsch, Stefan·2014·Cell
DOI 10.1016/j.cell.2014.05.048
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Abstract

Selective ubiquitin-dependent autophagy plays a pivotal role in the elimination of protein aggregates, assemblies, or organelles and counteracts the cytotoxicity of proteins linked to neurodegenerative diseases. Following substrate ubiquitylation, the cargo is delivered to autophagosomes involving adaptors like human p62 that bind ubiquitin and the autophagosomal ubiquitin-like protein Atg8/LC3; however, whether similar pathways exist in lower eukaryotes remained unclear. Here, we identify by a screen in yeast a new class of ubiquitin-Atg8 adaptors termed CUET proteins, comprising the ubiquitin-binding CUE-domain protein Cue5 from yeast and its human homolog Tollip. Cue5 collaborates with Rsp5 ubiquitin ligase, and the corresponding yeast mutants accumulate aggregation-prone proteins and are vulnerable to polyQ protein expression. Similarly, Tollip depletion causes cytotoxicity toward polyQ proteins, whereas Tollip overexpression clears human cells from Huntington's disease-linked polyQ proteins by autophagy. We thus propose that CUET proteins play a critical and ancient role in autophagic clearance of cytotoxic protein aggregates.

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  • Studies with mammalian immune cells indicate that TOLLIP is primarily responsible for the final step of autophagy, and facilitates fusion of lysosomes with autophagosomes, lipid droplets, or peroxisomes.

    “Studies with mammalian immune cells indicate that TOLLIP is primarily responsible for the final step of autophagy, and facilitates the fusion of lysosomes with autophagosomes, lipid droplets, or peroxisomes [627] [628].”

    From Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition) 1 (2021) · cites this paper as [627]

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Metadata

Authors
Lu, K., Psakhye, I., & Jentsch, S.
Venue
Cell
Publisher
Elsevier BV
Published
2014-07
Volume
158
Issue
3
Pages
549-563
ISSN
0092-8674
DOI
10.1016/j.cell.2014.05.048
Cited by
346
References
11
Language
en
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