Evidence map›Paper›PMID 12589059›Full record

ArticleMolecular biology of the cell2003

EpsinR: an ENTH domain-containing protein that interacts with AP-1.

Jennifer Hirst, Alison Motley, Kouki Harasaki, Sew Y Peak Chew, Margaret S Robinson

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2003. 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 86 papers.

0numbers the graph read from it
0cells of the map it votes in
86citing papers in PubMed
9.1field-weighted citation impact, top 1% 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

86 citing papers in PubMed, 212 citations in OpenAlex.

  1. Review
  2. Article
  3. Protein sorting from endosomes to the TGN.Frontiers in cell and developmental biology · 2023
    Review
  4. Article
  5. Article
  6. Article
  7. EPSIN1 and MTV1 define functionally overlapping but molecularly distinctProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  8. Review
  9. Review
  10. Visualization of Protein Sorting at theFrontiers in cell and developmental biology · 2019
    Article
  11. Review
  12. Review
  13. Article
  14. Review
  15. Conserved role for Gga proteins in phosphatidylinositol 4-kinase localization to theProceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  16. Regulation of αScientific reports · 2016
    Article
  17. Article
  18. Article
  19. Article
  20. Article

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

4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Jennifer HirstUniversity of Cambridge, Department of Clinical Biochemistry, Cambridge Institute for Medical Research, United Kingdom.
Alison Motley
Kouki Harasaki
Sew Y Peak Chew
Margaret S Robinson
University of Cambridge · GBMRC Laboratory of Molecular Biology · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

We have used GST pulldowns from A431 cell cytosol to identify three new binding partners for the gamma-adaptin appendage: Snx9, ARF GAP1, and a novel ENTH domain-containing protein, epsinR. EpsinR is a highly conserved protein that colocalizes with AP-1 and is enriched in purified clathrin-coated vesicles. However, it does not require AP-1 to get onto membranes and remains membrane-associated in AP-1-deficient cells. Moreover, although epsinR binds AP-1 via its COOH-terminal domain, its NH(2)-terminal ENTH domain can be independently recruited onto membranes, both in vivo and in vitro. Brefeldin A causes epsinR to redistribute into the cytosol, and recruitment of the ENTH domain requires GTPgammaS, indicating that membrane association is ARF dependent. In protein-lipid overlay assays, the epsinR ENTH domain binds to PtdIns(4)P, suggesting a possible mechanism for ARF-dependent recruitment onto TGN membranes. When epsinR is depleted from cells by RNAi, cathepsin D is still correctly processed intracellularly to the mature form. This indicates that although epsinR is likely to be an important component of the AP-1 network, it is not necessary for the sorting of lysosomal enzymes.

Indexed as

Adaptor Proteins, Vesicular TransportAnimalsBrefeldin ACarrier ProteinsCell LineCOS CellsCytosolGlutathione TransferaseHeLa CellsHumansImmunoblottingLysosomesMicroscopy, ElectronPlasmidsProtein BindingProtein Structure, TertiaryAdaptor Proteins, Vesicular TransportBrefeldin ACarrier ProteinsCLINT1 protein, humanGlutathione TransferaseTranscription Factor AP-1

Identifiers

PMID12589059
PMCPMC149997
OpenAlexW2103666428

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.