Evidence map›Paper›PMID 25220393›Full record

ArticleDevelopmental cell2014

Four GTPases differentially regulate the Sec7 Arf-GEF to direct traffic at the trans-golgi network.

Caitlin M McDonold, J Christopher Fromme

Open access · bronzeAbstract read
In one paragraph

Article in Developmental cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed
4.7field-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

74 citing papers in PubMed, 92 citations in OpenAlex.

  1. Article
  2. Article
  3. Knockout ofJournal of fungi (Basel, Switzerland) · 2026
    Article
  4. Article
  5. Review
  6. ARF GTPases Function at the Golgi.Sub-cellular biochemistry · 2026
    Review
  7. Endocytosis and trans-Golgi Network in Yeast.Sub-cellular biochemistry · 2026
    Review
  8. Article
  9. Review
  10. Regulation of yeast polarized exocytosis by phosphoinositide lipids.Cellular and molecular life sciences : CMLS · 2024
    Review
  11. Structural basis for Rab6 activation by the Ric1-Rgp1 complex.bioRxiv : the preprint server for biology · 2024
    Article
  12. Article
  13. Sec7 regulatory domains scaffold autoinhibited and active conformations.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. The Arf family GTPases: Regulation of vesicle biogenesis and beyond.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023
    Review

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

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

2 authors at 1 institution in 1 country.

Caitlin M McDonoldDepartment of Molecular Biology and Genetics, Weill Institute for Cell and Molecular Biology, Cornell University, Ithaca, NY 14853, USA.
J Christopher FrommeDepartment of Molecular Biology and Genetics, Weill Institute for Cell and Molecular Biology, Cornell University, Ithaca, NY 14853, USA. Electronic address: jcf14@cornell.edu.
Cornell University · US

Funding

PREDOCTORAL TRAINING IN CELLULAR AND MOLECULAR BIOLOGYT32GM007273 · NIGMS · CORNELL UNIVERSITY ITHACA · PI BRETSCHER, ANTHONY P. · 1985 to 2019
$11.6M
Regulation of Arf GTPase activation at the trans-Golgi networkR01GM098621 · NIGMS · CORNELL UNIVERSITY · PI FROMME, J CHRISTOPHER · 2012 to 2020
$2.9M
NIGMS NIH HHS R01 GM098621NIGMS NIH HHS R01GM098621NIGMS NIH HHS T32 GM007273NIGMS NIH HHS T32GM007273
6 · The paper itself

Abstract

Traffic through the Golgi complex is controlled by small GTPases of the Arf and Rab families. Guanine nucleotide exchange factor (GEF) proteins activate these GTPases to control Golgi function, yet the full assortment of signals regulating these GEFs is unknown. The Golgi Arf-GEF Sec7 and the homologous BIG1/2 proteins are effectors of the Arf1 and Arl1 GTPases. We demonstrate that Sec7 is also an effector of two Rab GTPases, Ypt1 (Rab1) and Ypt31/32 (Rab11), signifying unprecedented signaling crosstalk between GTPase pathways. The molecular basis for the role of Ypt31/32 and Rab11 in vesicle formation has remained elusive. We find that Arf1, Arl1, and Ypt1 primarily affect the membrane localization of Sec7, whereas Ypt31/32 exerts a dramatic stimulatory effect on the nucleotide exchange activity of Sec7. The convergence of multiple signaling pathways on a master regulator reveals a mechanism for balancing incoming and outgoing traffic at the Golgi.

Indexed as

ADP-Ribosylation Factor 1Guanine Nucleotide Exchange FactorsMonomeric GTP-Binding ProteinsProtein Transportrab GTP-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae Proteinstrans-Golgi NetworkTransport VesiclesVesicular Transport ProteinsADP-Ribosylation Factor 1ARL1 protein, S cerevisiaeGuanine Nucleotide Exchange FactorsMonomeric GTP-Binding Proteinsrab GTP-Binding ProteinsSaccharomyces cerevisiae ProteinsSec7 guanine nucleotide exchange factorsVesicular Transport ProteinsYPT1 protein, S cerevisiaeYPT31 protein, S cerevisiaeYPT32 protein, S cerevisiae

Identifiers

PMID25220393
PMCPMC4182139
OpenAlexW2010728666

What OpenQuestion holds

Textmetadata
LicenceTDM
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.