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  An aberrant phase transition of stress granules triggered by misfolded protein and prevented by chaperone function.

Mateju, D., Franzmann, T., Patel, A., Kopach, A., Boczek, E., Maharana, S., et al. (2017). An aberrant phase transition of stress granules triggered by misfolded protein and prevented by chaperone function. The EMBO journal, 36(12), 1669-1687. doi:10.15252/embj.201695957.

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 Creators:
Mateju, Daniel1, Author           
Franzmann, Titus1, Author           
Patel, Avinash1, Author           
Kopach, Andrii1, Author           
Boczek, Edgar1, Author           
Maharana, Shovamayee1, Author           
Lee, Hyun-Ok Kate1, Author           
Carra, Serena, Author
Hyman, Anthony1, Author           
Alberti, Simon1, Author           
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1Max Planck Institute for Molecular Cell Biology and Genetics, ou_2340692              

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 Abstract: Stress granules (SG) are membrane-less compartments involved in regulating mRNAs during stress. Aberrant forms of SGs have been implicated in age-related diseases, such as amyotrophic lateral sclerosis (ALS), but the molecular events triggering their formation are still unknown. Here, we find that misfolded proteins, such as ALS-linked variants of SOD1, specifically accumulate and aggregate within SGs in human cells. This decreases the dynamics of SGs, changes SG composition, and triggers an aberrant liquid-to-solid transition ofin vitroreconstituted compartments. We show that chaperone recruitment prevents the formation of aberrant SGs and promotes SG disassembly when the stress subsides. Moreover, we identify a backup system for SG clearance, which involves transport of aberrant SGs to the aggresome and their degradation by autophagy. Thus, cells employ a system of SG quality control to prevent accumulation of misfolded proteins and maintain the dynamic state of SGs, which may have relevance for ALS and related diseases.

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 Dates: 2017-04-04
 Publication Status: Issued
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 Identifiers: DOI: 10.15252/embj.201695957
Other: cbg-6825
PMID: 28377462
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Title: The EMBO journal
  Other : EMBO J
Source Genre: Journal
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Pages: - Volume / Issue: 36 (12) Sequence Number: - Start / End Page: 1669 - 1687 Identifier: -