Evidence map›Paper›PMID 16790491›Full record

ArticleMolecular biology of the cell2006

Distinct roles for TGN/endosome epsin-like adaptors Ent3p and Ent5p.

Giancarlo Costaguta, Mara C Duncan, G Esteban Fernández, Grace H Huang, Gregory S Payne

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

33 citing papers in PubMed, 58 citations in OpenAlex.

  1. Endocytosis and trans-Golgi Network in Yeast.Sub-cellular biochemistry · 2026
    Review
  2. Review
  3. Rethinking the Yeast Endomembrane System.Sub-cellular biochemistry · 2026
    Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Visualization of Protein Sorting at theFrontiers in cell and developmental biology · 2019
    Article
  16. 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
  17. Article
  18. Article
  19. Article
  20. Review
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

5 authors at 1 institution in 1 country.

Giancarlo CostagutaDepartment of Biological Chemistry, David Geffen School of Medicine at UCLA, Los Angeles, CA 90095, USA.
Mara C Duncan
G Esteban Fernández
Grace H Huang
Gregory S Payne
University of California, Los Angeles · US

Funding

MOLECULAR STUDIES OF SELECTIVE PROTEIN TRANSPORTR01GM039040 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI PAYNE, GREGORY S · 1988 to 2016
$6.4M
Clathrin adaptor function at the trans Golgi network and endosomesR01GM067911 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI PAYNE, GREGORY S · 2004 to 2007
$1.1M
Chemical inhibition of post Golgi trafficF32DK062608 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI DUNCAN, MARA C · 2004 to 2006
$154k
MINORITY PREDOCTORAL FELLOWSHIP PROGRAMF31GM072119 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI FERNANDEZ, GERARDO E · 2004 to 2005
$58k
NIDDK NIH HHS DK062608NIDDK NIH HHS F32 DK062608NIGMS NIH HHS F31 GM072119NIGMS NIH HHS GM072119NIGMS NIH HHS GM39040NIGMS NIH HHS GM67911NIGMS NIH HHS R01 GM039040NIGMS NIH HHS R01 GM067911
6 · The paper itself

Abstract

Clathrin adaptors are key factors in clathrin-coated vesicle formation, coupling clathrin to cargo and/or the lipid bilayer. A physically interacting network of three classes of adaptors participate in clathrin-mediated traffic between the trans-Golgi network (TGN) and endosomes: AP-1, Gga proteins, and epsin-like proteins. Here we investigate functional relationships within this network through transport assays and protein localization analysis in living yeast cells. We observed that epsin-like protein Ent3p preferentially localized with Gga2p, whereas Ent5p distributed equally between AP-1 and Gga2p. Ent3p was mislocalized in Gga-deficient but not in AP-1-deficient cells. In contrast, Ent5p retained localization in cells lacking either or both AP-1 and Gga proteins. The Ent proteins were dispensable for AP-1 or Gga localization. Synthetic genetic growth and alpha-factor maturation defects were observed when ent5Delta but not ent3Delta was introduced together with deletions of the GGA genes. In AP-1-deficient cells, ent3Delta and to a lesser extent ent5Delta caused minor alpha-factor maturation defects, but together resulted in a near-lethal phenotype. Deletions of ENT3 and ENT5 also displayed synthetic defects similar to, but less severe than, synthetic effects of AP-1 and Gga inactivation. These results differentiate Ent3p and Ent5p function in vivo, suggesting that Ent3p acts primarily with Gga proteins, whereas Ent5p acts with both AP-1 and Gga proteins but is more critical for AP-1-mediated transport. The data also support a model in which the Ent adaptors provide important accessory functions to AP-1 and Gga proteins in TGN/endosome traffic.

Indexed as

Adaptor Protein Complex 1Adaptor Proteins, Vesicular TransportADP-Ribosylation FactorsAllelesAmino Acid SequenceEndosomesGene DeletionModels, BiologicalMolecular Sequence DataProtein Structure, TertiaryProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTemperaturetrans-Golgi NetworkAdaptor Protein Complex 1Adaptor Proteins, Vesicular TransportADP-Ribosylation FactorsEnt3 protein, S cerevisiaeEnt5 protein, S cerevisiaeepsinGga2 protein, S cerevisiaeGGA adaptor proteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID16790491
PMCPMC1624859
OpenAlexW2140316038

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.