Evidence map›Paper›PMID 24619421›Full record

ArticleThe Journal of biological chemistry2014

The p97-FAF1 protein complex reveals a common mode of p97 adaptor binding.

Caroline A Ewens, Silvia Panico, Patrik Kloppsteck, Ciaran McKeown, Ima-Obong Ebong, Carol Robinson, Xiaodong Zhang, Paul S Freemont

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

22 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
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  7. A protein-lipid complex that detoxifies free fatty acids.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023
    Article
  8. Article
  9. USP7 and VCPCell reports · 2021
    Article
  10. Article
  11. Article
  12. The AAA+ ATPase p97, a cellular multitool.The Biochemical journal · 2017
    Review
  13. Article
  14. Article
  15. Review
  16. Review
  17. Review
  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

8 authors at 2 institutions in 1 country.

Caroline A EwensCentre for Structural Biology, Department of Life Sciences, Imperial College London, South Kensington Campus, London SW7 2AZ, United Kingdom.
Silvia PanicoCentre for Structural Biology, Department of Life Sciences, Imperial College London, South Kensington Campus, London SW7 2AZ, United Kingdom.
Patrik KloppsteckCentre for Structural Biology, Department of Life Sciences, Imperial College London, South Kensington Campus, London SW7 2AZ, United Kingdom.
Ciaran McKeownCentre for Structural Biology, Department of Life Sciences, Imperial College London, South Kensington Campus, London SW7 2AZ, United Kingdom.
Ima-Obong EbongDepartment of Chemistry, University of Oxford, South Parks Road, Oxford OX1 3TA, United Kingdom.
Carol RobinsonDepartment of Chemistry, University of Oxford, South Parks Road, Oxford OX1 3TA, United Kingdom.
Xiaodong ZhangCentre for Structural Biology, Department of Life Sciences, Imperial College London, South Kensington Campus, London SW7 2AZ, United Kingdom.
Paul S FreemontCentre for Structural Biology, Department of Life Sciences, Imperial College London, South Kensington Campus, London SW7 2AZ, United Kingdom. Electronic address: p.freemont@imperial.ac.uk.
Imperial College London · GBUniversity of Oxford · GB

Funding

Biotechnology and Biological Sciences Research CouncilCancer Research UK 13449Wellcome Trust
6 · The paper itself

Abstract

p97, also known as valosin-containing protein, is a versatile participant in the ubiquitin-proteasome system. p97 interacts with a large network of adaptor proteins to process ubiquitylated substrates in different cellular pathways, including endoplasmic reticulum-associated degradation and transcription factor activation. p97 and its adaptor Fas-associated factor-1 (FAF1) both have roles in the ubiquitin-proteasome system during NF-κB activation, although the mechanisms are unknown. FAF1 itself also has emerging roles in other cell-cycle pathways and displays altered expression levels in various cancer cell lines. We have performed a detailed study the p97-FAF1 interaction. We show that FAF1 binds p97 stably and in a stoichiometry of 3 to 6. Cryo-EM analysis of p97-FAF1 yielded a 17 Å reconstruction of the complex with FAF1 above the p97 ring. Characteristics of p97-FAF1 uncovered in this study reveal common features in the interactions of p97, providing mechanistic insight into how p97 mediates diverse functionalities.

Indexed as

Adaptor Proteins, Signal TransducingAdenosine TriphosphatasesApoptosis Regulatory ProteinsCalorimetryCell Cycle ProteinsCryoelectron MicroscopyProtein BindingUltracentrifugationValosin Containing ProteinAdaptor Proteins, Signal TransducingAdenosine TriphosphatasesApoptosis Regulatory ProteinsCell Cycle ProteinsFAF1 protein, humanValosin Containing ProteinVCP protein, humanATPasesElectron Microscopy (EM)FAF1FasIsothermal Titration Calorimetryp97Protein Cross-linking

Identifiers

PMID24619421
PMCPMC4002113
OpenAlexW2042787861

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.