Evidence map›Paper›PMID 37264685›Full record

ArticleThe EMBO journal2023

Structural basis of ubiquitin-independent PP1 complex disassembly by p97.

Johannes van den Boom, Guendalina Marini, Hemmo Meyer, Helen R Saibil

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
6.3field-weighted citation impact, top 3% 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

28 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
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  8. Review
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  10. Molecular Tweezers Block the Functional Pore of a Protein Machine.Journal of the American Chemical Society · 2025
    Article
  11. Article
  12. Review
  13. 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
  14. Article
  15. Article
  16. Article
  17. Allosteric activation of VCP, an AAA unfoldase, by small molecule mimicry.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  18. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 3 institutions in 2 countries.

Johannes van den BoomMolecular Biology I, Center of Medical Biotechnology, Faculty of Biology, University of Duisburg-Essen, Essen, Germany.
Guendalina MariniCentre for Structural Systems Biology, Leibniz-Institute of Virology and University Medical Center Hamburg-Eppendorf (UKE), Hamburg, Germany.
Hemmo MeyerMolecular Biology I, Center of Medical Biotechnology, Faculty of Biology, University of Duisburg-Essen, Essen, Germany.ORCID 0000-0003-1883-1796
Helen R SaibilBiological Sciences, Institute of Structural and Molecular Biology, Birkbeck University of London, London, UK.ORCID 0000-0002-2266-8891
University of Duisburg-Essen · DEInstitute of Structural and Molecular Biology · GBUniversität Hamburg · DE

Funding

Biotechnology and Biological Sciences Research CouncilMedical Research CouncilWellcome TrustWellcome Trust 106249/Z/14/ZWellcome Trust 202679/Z/16/ZWellcome Trust 206166/Z/17/Z
6 · The paper itself

Abstract

The AAA+-ATPase p97 (also called VCP or Cdc48) unfolds proteins and disassembles protein complexes in numerous cellular processes, but how substrate complexes are loaded onto p97 and disassembled is unclear. Here, we present cryo-EM structures of p97 in the process of disassembling a protein phosphatase-1 (PP1) complex by extracting an inhibitory subunit from PP1. We show that PP1 and its partners SDS22 and inhibitor-3 (I3) are loaded tightly onto p97, surprisingly via a direct contact of SDS22 with the p97 N-domain. Loading is assisted by the p37 adapter that bridges two adjacent p97 N-domains underneath the substrate complex. A stretch of I3 is threaded into the central channel of the spiral-shaped p97 hexamer, while other elements of I3 are still attached to PP1. Thus, our data show how p97 arranges a protein complex between the p97 N-domain and central channel, suggesting a hold-and-extract mechanism for p97-mediated disassembly.

Indexed as

Cell Cycle ProteinsUbiquitinATPases Associated with Diverse Cellular ActivitiesModels, MolecularProtein Phosphatase 1Valosin Containing ProteinATPases Associated with Diverse Cellular ActivitiesCell Cycle ProteinsProtein Phosphatase 1UbiquitinValosin Containing ProteinAAA ATPasecryo-EMprotein phosphatase-1protein unfolding

Identifiers

PMID37264685
PMCPMC10350818
OpenAlexW4379094563

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.