Evidence map›Paper›PMID 23326640›Full record

ArticleeLife2013

A novel GTP-binding protein-adaptor protein complex responsible for export of Vangl2 from the trans Golgi network.

Yusong Guo, Giulia Zanetti, Randy Schekman

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in eLife, 2013. 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 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

59 citing papers in PubMed, 78 citations in OpenAlex.

  1. Deubiquitination of Vangl by USP6 and USP32 Regulates Planar Cell Polarity Signaling.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  2. Review
  3. Uncovering cargo clients and accessory factors of AP-1 and AP-4 through vesicle proteomics.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Article
  5. Article
  6. Core planar cell polarity genesProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. TMED10 mediates the trafficking of insulin-like growth factor 2 along the secretory pathway for myoblast differentiation.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  11. Article
  12. Article
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  15. A SURF4-to-proteoglycan relay mechanism that mediates the sorting and secretion of a tagged variant of sonic hedgehog.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  16. Review
  17. Review
  18. Article
  19. An in vitro vesicle formation assay reveals cargo clients and factors that mediate vesicular trafficking.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  20. Review
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

3 authors at 2 institutions in 1 country.

Yusong GuoDepartment of Molecular and Cell Biology , Howard Hughes Medical Institute, University of California-Berkeley , Berkeley , United States.
Giulia Zanetti
Randy Schekman
University of California, Berkeley · USHoward Hughes Medical Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Planar cell polarity (PCP) requires the asymmetric sorting of distinct signaling receptors to distal and proximal surfaces of polarized epithelial cells. We have examined the transport of one PCP signaling protein, Vangl2, from the trans Golgi network (TGN) in mammalian cells. Using siRNA knockdown experiments, we find that the GTP-binding protein, Arfrp1, and the clathrin adaptor complex 1 (AP-1) are required for Vangl2 transport from the TGN. In contrast, TGN export of Frizzled 6, which localizes to the opposing epithelial surface from Vangl2, does not depend on Arfrp1 or AP-1. Mutagenesis studies identified a YYXXF sorting signal in the C-terminal cytosolic domain of Vangl2 that is required for Vangl2 traffic and interaction with the μ subunit of AP-1. We propose that Arfrp1 exposes a binding site on AP-1 that recognizes the Vangl2 sorting motif for capture into a transport vesicle destined for the proximal surface of a polarized epithelial cell.DOI:http://dx.doi.org/10.7554/eLife.00160.001.

Indexed as

Cell PolarityAdaptor Protein Complex 1Adaptor Protein Complex gamma SubunitsAdaptor Protein Complex mu SubunitsADP-Ribosylation FactorsAmino Acid SequenceAnimalsBinding SitesCadherinsCell Adhesion MoleculesChlorocebus aethiopsCOS CellsEpithelial CellsFrizzled ReceptorsHeLa CellsHumansAdaptor Protein Complex 1Adaptor Protein Complex gamma SubunitsAdaptor Protein Complex mu SubunitsADP-Ribosylation FactorsARFRP1 protein, humanCadherinsCell Adhesion MoleculesCELSR1 cadherin, humanFrizzled ReceptorsFZD6 protein, humanIntracellular Signaling Peptides and ProteinsMembrane ProteinsProtein Kinase Cprotein kinase DPTK7 protein, humanReceptor Protein-Tyrosine KinasesVANGL2 protein, humanArf proteinsHumanTGN sortingVesicle coat proteins

Identifiers

PMID23326640
PMCPMC3539332
OpenAlexW2133871547

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.