Evidence map›Paper›PMID 26389662›Full record

ArticleNature cell biology2015

Systematic proteomics of the VCP-UBXD adaptor network identifies a role for UBXN10 in regulating ciliogenesis.

Malavika Raman, Mikhail Sergeev, Maija Garnaas, John R Lydeard, Edward L Huttlin, Wolfram Goessling, Jagesh V Shah, J Wade Harper

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Nature cell biology, 2015. 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 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
6.9field-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

64 citing papers in PubMed, 108 citations in OpenAlex.

  1. Article
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  11. AAA+ ATPase chaperone p97/VCPNature communications · 2024
    Article
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  13. Article
  14. Article
  15. Review
  16. Review
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  20. Review

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 1 country.

Malavika RamanDepartment of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA.
Mikhail SergeevDepartment of Systems Biology, Harvard Institutes of Medicine, 4 Blackfan Circle, Boston, Massachusetts 02115, USA.
Maija GarnaasDepartment of Medicine, New Research Building, 77 Avenue Louis Pasteur, Boston, Massachusetts 02115, USA.
John R LydeardDepartment of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA.
Edward L HuttlinDepartment of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA.
Wolfram GoesslingDepartment of Medicine, New Research Building, 77 Avenue Louis Pasteur, Boston, Massachusetts 02115, USA.
Jagesh V ShahDepartment of Systems Biology, Harvard Institutes of Medicine, 4 Blackfan Circle, Boston, Massachusetts 02115, USA.
J Wade HarperDepartment of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA.
Harvard University · USMassachusetts Department of Public Health · USBrigham and Women's Hospital · US

Funding

Ubiquitin Mediated Proteolysis and Cell Cycle ControlR01AG011085 · NIA · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI JEFFREY W HARPER · 1993 to 2026
$10.9M
Systematic discovery and functional analysis of the PARKIN modified proteomeR37NS083524 · NINDS · HARVARD MEDICAL SCHOOL · PI HARPER, JEFFREY W · 2013 to 2019
$3.0M
NIA NIH HHS R01 AG011085NIA NIH HHS R01-AG011085NINDS NIH HHS R37 NS083524NINDS NIH HHS R37-NS083524
6 · The paper itself

Abstract

The AAA-ATPase VCP (also known as p97 or CDC48) uses ATP hydrolysis to 'segregate' ubiquitylated proteins from their binding partners. VCP acts through UBX-domain-containing adaptors that provide target specificity, but the targets and functions of UBXD proteins remain poorly understood. Through systematic proteomic analysis of UBXD proteins in human cells, we reveal a network of over 195 interacting proteins, implicating VCP in diverse cellular pathways. We have explored one such complex between an unstudied adaptor UBXN10 and the intraflagellar transport B (IFT-B) complex, which regulates anterograde transport into cilia. UBXN10 localizes to cilia in a VCP-dependent manner and both VCP and UBXN10 are required for ciliogenesis. Pharmacological inhibition of VCP destabilized the IFT-B complex and increased trafficking rates. Depletion of UBXN10 in zebrafish embryos causes defects in left-right asymmetry, which depends on functional cilia. This study provides a resource for exploring the landscape of UBXD proteins in biology and identifies an unexpected requirement for VCP-UBXN10 in ciliogenesis.

Indexed as

Protein Interaction MapsAdaptor Proteins, Signal TransducingAdenosine TriphosphatasesAnimalsCell Cycle ProteinsCiliaCytoskeletal ProteinsHEK293 CellsHeLa CellsHumansImmunoblottingLLC-PK1 CellsMicroscopy, ConfocalMicroscopy, FluorescenceMorphogenesisProtein BindingAdaptor Proteins, Signal TransducingAdenosine TriphosphatasesCell Cycle ProteinsCytoskeletal ProteinsIFT74 protein, humanIFT88 protein, humanTumor Suppressor ProteinsUBXN10 protein, humanValosin Containing ProteinVCP protein, human

Identifiers

PMID26389662
PMCPMC4610257
OpenAlexW3133907395

What OpenQuestion holds

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Registered trials

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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.