Evidence map›Paper›PMID 30344098›Full record

ArticleMolecular cell2018

Ubiquitin-Independent Disassembly by a p97 AAA-ATPase Complex Drives PP1 Holoenzyme Formation.

Matthias Weith, Jonas Seiler, Johannes van den Boom, Matthias Kracht, Julia Hülsmann, Ivana Primorac, Javier Del Pino Garcia, Farnusch Kaschani, Markus Kaiser, Andrea Musacchio and 2 more

Open access · bronzeAbstract read
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In one paragraph

Article in Molecular cell, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing 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

63 citing papers in PubMed, 89 citations in OpenAlex.

  1. Article
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  9. Molecular Tweezers Block the Functional Pore of a Protein Machine.Journal of the American Chemical Society · 2025
    Article
  10. Article
  11. Review
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  13. Article
  14. Alternating binding and p97-mediated dissociation of SDS22 and I3 recycles active PP1 between holophosphatases.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  15. Article
  16. P-NADs:Heliyon · 2024
    Article
  17. Article
  18. Article
  19. Discovering optimal kinetic pathways for self-assembly using automatic differentiation.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  20. Article

3 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors at 3 institutions in 2 countries.

Matthias WeithCentre for Medical Biotechnology, Faculty of Biology, University of Duisburg-Essen, 45117 Essen, Germany.
Jonas SeilerCentre for Medical Biotechnology, Faculty of Biology, University of Duisburg-Essen, 45117 Essen, Germany.
Johannes van den BoomCentre for Medical Biotechnology, Faculty of Biology, University of Duisburg-Essen, 45117 Essen, Germany.
Matthias KrachtCentre for Medical Biotechnology, Faculty of Biology, University of Duisburg-Essen, 45117 Essen, Germany.
Julia HülsmannCentre for Medical Biotechnology, Faculty of Biology, University of Duisburg-Essen, 45117 Essen, Germany.
Ivana PrimoracCentre for Medical Biotechnology, Faculty of Biology, University of Duisburg-Essen, 45117 Essen, Germany; Department of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany.
Javier Del Pino GarciaLaboratory of Biosignaling and Therapeutics, KU Leuven, Department of Cellular and Molecular Medicine, University of Leuven, 3000 Leuven, Belgium.
Farnusch KaschaniAnalytics Core Facility, Centre for Medical Biotechnology, Faculty of Biology, University of Duisburg-Essen, 45117 Essen, Germany.
Markus KaiserAnalytics Core Facility, Centre for Medical Biotechnology, Faculty of Biology, University of Duisburg-Essen, 45117 Essen, Germany.
Andrea MusacchioCentre for Medical Biotechnology, Faculty of Biology, University of Duisburg-Essen, 45117 Essen, Germany; Department of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany.
Mathieu BollenLaboratory of Biosignaling and Therapeutics, KU Leuven, Department of Cellular and Molecular Medicine, University of Leuven, 3000 Leuven, Belgium.
Hemmo MeyerCentre for Medical Biotechnology, Faculty of Biology, University of Duisburg-Essen, 45117 Essen, Germany. Electronic address: hemmo.meyer@uni-due.de.
University of Duisburg-Essen · DEKU Leuven · BEMax Planck Institute of Molecular Physiology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The functional diversity of protein phosphatase-1 (PP1), with its countless substrates, relies on the ordered assembly of alternative PP1 holoenzymes. Here, we show that newly synthesized PP1 is first held by its partners SDS22 and inhibitor-3 (I3) in an inactive complex, which needs to be disassembled by the p97 AAA-ATPase to promote exchange to substrate specifiers. Unlike p97-mediated degradative processes that require the Ufd1-Npl4 ubiquitin adapters, p97 is targeted to PP1 by p37 and related adapter proteins. Reconstitution with purified components revealed direct interaction of the p37 SEP domain with I3 without the need for ubiquitination, and ATP-driven pulling of I3 into the central channel of the p97 hexamer, which triggers dissociation of I3 and SDS22. Thus, we establish regulatory ubiquitin-independent protein complex disassembly as part of the functional arsenal of p97 and define an unanticipated essential step in PP1 biogenesis that illustrates the molecular challenges of ordered subunit exchange.

Indexed as

Adaptor Proteins, Signal TransducingAdenosine TriphosphatasesCell Cycle ProteinsHEK293 CellsHeLa CellsHoloenzymesHumansModels, MolecularNuclear Pore Complex ProteinsNuclear ProteinsNucleocytoplasmic Transport ProteinsProtein BindingProtein Phosphatase 1Proton-Translocating ATPasesUbiquitinAdaptor Proteins, Signal TransducingAdenosine TriphosphatasesCell Cycle ProteinsHoloenzymesNuclear Pore Complex ProteinsNuclear ProteinsNucleocytoplasmic Transport Proteinsp37 protein, humanp97 ATPasePPP1R7 protein, humanProtein Phosphatase 1Proton-Translocating ATPasesUbiquitinAAA ATPaseprotein biogenesisprotein phosphatase-1protein unfoldingubiquitinVCP/p97

Identifiers

PMID30344098
OpenAlexW2896967591

What OpenQuestion holds

Textmetadata
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.