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  Pathway choice between proteasomal and autophagic degradation.

Lu, K., den Brave, F., & Jentsch, S. (2017). Pathway choice between proteasomal and autophagic degradation. Autophagy, 13(10), 1799-1800. doi:10.1080/15548627.2017.1358851.

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Pathway choice between proteasomal and autophagic degradation.pdf (Publisher version), 2MB
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Pathway choice between proteasomal and autophagic degradation.pdf
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© 2017 The Author(s). Published with license byTaylor & Francis© Kefeng Lu, Fabian den Brave, and Stefan Jentsch This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivatives License.

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 Creators:
Lu, Kefeng1, Author              
den Brave, Fabian1, Author              
Jentsch, Stefan1, Author              
Affiliations:
1Jentsch, Stefan / Molecular Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565156              

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Free keywords: Cue5; Dsk2; autophagy; proteasome; ubiquitin
 Abstract: Efficient degradation of abnormal or aggregated proteins is crucial to protect the cell against proteotoxic stress. Selective targeting and disposal of such proteins usually occurs in a ubiquitin-dependent manner by proteasomes and macroautophagy/autophagy. Whereas proteasomes are efficient in degrading abnormal soluble proteins, protein aggregates are typically targeted for degradation by autophagic vesicles. Both processes require ubiquitin-binding receptors, which are targeted to proteasomes via ubiquitin-like domains or to phagophores (the precursors to autophagosomes) via Atg8/LC3 binding motifs, respectively. The use of substrate modification by ubiquitin in both pathways raised the question of how degradative pathway choice is achieved. In contrast to previous models, proposing different types of ubiquitin linkages for substrate targeting, we find that pathway choice is a late event largely determined by the oligomeric state of the receptors. Monomeric proteasome receptors bind soluble substrates more efficiently due to their higher affinity for ubiquitin. Upon substrate aggregation, autophagy receptors with lower ubiquitin binding affinity gain the upper hand due to higher avidity achieved by receptor bundling. Thus, our work suggests that ubiquitination is a shared signal of an adaptive protein quality control system, which targets substrates for the optimal proteolytic pathway.

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Language(s): eng - English
 Dates: 2017
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Type: -
 Identifiers: ISI: 28813181
DOI: 10.1080/15548627.2017.1358851
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Title: Autophagy
Source Genre: Journal
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Publ. Info: Georgetown, TX : Landes Bioscience
Pages: - Volume / Issue: 13 (10) Sequence Number: - Start / End Page: 1799 - 1800 Identifier: ISSN: 1554-8627
CoNE: https://pure.mpg.de/cone/journals/resource/1000000000238500