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  The nucleolus functions as a phase-separated protein quality control compartment

Frottin, F., Schueder, F., Tiwary, S., Gupta, R., Körner, R., Schlichthaerle, T., et al. (2019). The nucleolus functions as a phase-separated protein quality control compartment. Science, 365(6451), 342-347. doi:10.1126/science.aaw9157.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0004-5861-C Version Permalink: http://hdl.handle.net/21.11116/0000-0004-5862-B
Genre: Journal Article

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 Creators:
Frottin, F.1, Author              
Schueder, F.2, Author              
Tiwary, S.3, Author              
Gupta, R.1, Author
Körner, R.1, Author              
Schlichthaerle, T.2, Author              
Cox, J.3, Author              
Jungmann, R.2, Author              
Hartl, F. U.1, Author              
Hipp, M. S.1, Author              
Affiliations:
1Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565152              
2Jungmann, Ralf / Molecular Imaging and Bionanotechnology, Max Planck Institute of Biochemistry, Max Planck Society, ou_2149679              
3Cox, Jürgen / Computational Systems Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_2063284              

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 Abstract: The nuclear proteome is rich in stress-sensitive proteins, which suggests that effective protein quality control mechanisms are in place to ensure conformational maintenance. We investigated the role of the nucleolus in this process. In mammalian tissue culture cells under stress conditions, misfolded proteins entered the granular component (GC) phase of the nucleolus. Transient associations with nucleolar proteins such as NPM1 conferred low mobility to misfolded proteins within the liquid-like GC phase, avoiding irreversible aggregation. Refolding and extraction of proteins from the nucleolus during recovery from stress was Hsp70-dependent. The capacity of the nucleolus to store misfolded proteins was limited, and prolonged stress led to a transition of the nucleolar matrix from liquid-like to solid, with loss of reversibility and dysfunction in quality control. Thus, we suggest that the nucleolus has chaperone-like properties and can promote nuclear protein maintenance under stress.

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Language(s): eng - English
 Dates: 2019-07-26
 Publication Status: Published in print
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 Table of Contents: We acknowledge support by the MPIB Imaging facility and G. Cardone for providing the algorithm for image quantification.
 Rev. Method: -
 Identifiers: DOI: 10.1126/science.aaw9157
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Project name : ERC-2012-SyG_318987–ToPAG
Grant ID : 318987
Funding program : Funding Programme 7 (FP7)
Funding organization : European Commission (EC)
Project name : MolMap grant agreement 680241
Grant ID : 680241
Funding program : -
Funding organization : European Commission

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Title: Science
  Other : Science
Source Genre: Journal
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Publ. Info: Washington, D.C. : American Association for the Advancement of Science
Pages: - Volume / Issue: 365 (6451) Sequence Number: - Start / End Page: 342 - 347 Identifier: ISSN: 0036-8075
CoNE: https://pure.mpg.de/cone/journals/resource/991042748276600_1