Evidence map›Paper›PMID 33067463›Full record

ArticleNature communications2020

ATP hydrolysis by yeast Hsp104 determines protein aggregate dissolution and size in vivo.

Udhayabhaskar Sathyanarayanan, Marina Musa, Peter Bou Dib, Nuno Raimundo, Ira Milosevic, Anita Krisko

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.5field-weighted citation impact, top 10% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

25 citing papers in PubMed, 47 citations in OpenAlex.

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  11. Genetic inactivation of essentialMolecular biology of the cell · 2023
    Article
  12. Review
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  14. Article
  15. Identification of Genes Promoting Growth ofJournal of fungi (Basel, Switzerland) · 2022
    Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 3 countries.

Udhayabhaskar SathyanarayananEuropean Neuroscience Institute (ENI) - A Joint Initiative of the University Medical Center Göttingen and the Max-Planck-Society, Göttingen, Germany.
Marina MusaEuropean Neuroscience Institute (ENI) - A Joint Initiative of the University Medical Center Göttingen and the Max-Planck-Society, Göttingen, Germany.
Peter Bou DibUniversitätsmedizin Göttingen, Institut für Zellbiochemie, Göttingen, Germany.ORCID http://orcid.org/0000-0002-7146-8271
Nuno RaimundoUniversitätsmedizin Göttingen, Institut für Zellbiochemie, Göttingen, Germany.ORCID http://orcid.org/0000-0002-5988-9129
Ira MilosevicEuropean Neuroscience Institute (ENI) - A Joint Initiative of the University Medical Center Göttingen and the Max-Planck-Society, Göttingen, Germany.
Anita KriskoDepartment of Experimental Neurodegeneration, University Medical Center Göttingen, Göttingen, Germany. anita.krisko@med.uni-goettingen.de.ORCID http://orcid.org/0000-0002-9951-6685
Universitätsmedizin Göttingen · DEMax Planck Society · DECentre for Human Genetics · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Signs of proteostasis failure often entwine with those of metabolic stress at the cellular level. Here, we study protein sequestration during glucose deprivation-induced ATP decline in Saccharomyces cerevisiae. Using live-cell imaging, we find that sequestration of misfolded proteins and nascent polypeptides into two distinct compartments, stress granules, and Q-bodies, is triggered by the exhaustion of ATP. Both compartments readily dissolve in a PKA-dependent manner within minutes of glucose reintroduction and ATP level restoration. We identify the ATP hydrolase activity of Hsp104 disaggregase as the critical ATP-consuming process determining compartments abundance and size, even in optimal conditions. Sequestration of proteins into distinct compartments during acute metabolic stress and their retrieval during the recovery phase provide a competitive fitness advantage, likely promoting cell survival during stress.

Indexed as

Adenosine TriphosphateGlucoseHeat-Shock ProteinsHydrolysisProtein AggregatesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSolubilityAdenosine TriphosphateGlucoseHeat-Shock ProteinsHsP104 protein, S cerevisiaeProtein AggregatesSaccharomyces cerevisiae Proteins

Identifiers

PMID33067463
PMCPMC7568574
OpenAlexW3093081069

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.