Evidence map›Paper›PMID 17344475›Full record

ArticleMolecular biology of the cell2007

Ent3p and Ent5p exhibit cargo-specific functions in trafficking proteins between the trans-Golgi network and the endosomes in yeast.

Alenka Copic, Trevor L Starr, Randy Schekman

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

37 citing papers in PubMed, 59 citations in OpenAlex.

  1. Review
  2. Rethinking the Yeast Endomembrane System.Sub-cellular biochemistry · 2026
    Review
  3. Fungal Chitin Synthases: Structure, Function, and Regulation.Journal of fungi (Basel, Switzerland) · 2025
    Review
  4. Article
  5. Chitin Synthesis in Yeast: A Matter of Trafficking.International journal of molecular sciences · 2022
    Review
  6. Article
  7. Exomer complex regulates protein traffic at the TGN through differential interactions with cargos and clathrin adaptor complexes.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021
    Article
  8. Article
  9. Article
  10. Article
  11. Visualization of Protein Sorting at theFrontiers in cell and developmental biology · 2019
    Article
  12. Article
  13. 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

3 authors at 1 institution in 1 country.

Alenka CopicHoward Hughes Medical Institute and Department of Molecular and Cell Biology, University of California at Berkeley, CA 94720, USA.
Trevor L Starr
Randy Schekman
Howard Hughes Medical Institute · US

Funding

MOLECULAR STUDIES OF EUKARYOTIC CELL SURFACE GROWTHR01GM026755 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI SCHEKMAN, RANDY W. · 1985 to 2005
$1.1M
NIGMS NIH HHS GM-26755NIGMS NIH HHS R01 GM026755
6 · The paper itself

Abstract

The phosphoinositide-binding proteins Ent3p and Ent5p are required for protein transport from the trans-Golgi network (TGN) to the vacuole in Saccharomyces cerevisiae. Both proteins interact with the monomeric clathrin adaptor Gga2p, but Ent5p also interacts with the clathrin adaptor protein 1 (AP-1) complex, which facilitates retention of proteins such as Chs3p at the TGN. When both ENT3 and ENT5 are mutated, Chs3p is diverted from an intracellular reservoir to the cell surface. However, Ent3p and Ent5p are not required for the function of AP-1, but rather they seem to act in parallel with AP-1 to retain proteins such as Chs3p at the TGN. They have all the properties of clathrin adaptors, because they can both bind to clathrin and to cargo proteins. Like AP-1, Ent5p binds to Chs3p, whereas Ent3p facilitates the interaction between Gga2p and the endosomal syntaxin Pep12p. Thus, Ent3p has an additional function in Gga-dependent transport to the late endosome. Ent3p also facilitates the association between Gga2p and clathrin; however, Ent5p can partially substitute for this function. We conclude that the clathrin adaptors AP-1, Ent3p, Ent5p, and the Ggas cooperate in different ways to sort proteins between the TGN and the endosomes.

Indexed as

Adaptor Protein Complex 1Adaptor Proteins, Vesicular TransportBiological Transport, ActiveChitin SynthaseClathrinEndosomesGenes, FungalGreen Fluorescent ProteinsModels, BiologicalMutationProtein BindingRecombinant Fusion ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae Proteinstrans-Golgi NetworkAdaptor Protein Complex 1Adaptor Proteins, Vesicular TransportChitin SynthaseCHS3 protein, S cerevisiaeClathrinEnt3 protein, S cerevisiaeEnt5 protein, S cerevisiaeGreen Fluorescent ProteinsRecombinant Fusion ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID17344475
PMCPMC1855026
OpenAlexW2168163553

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.