Evidence map›Paper›PMID 26765562›Full record

ArticleeLife2016

The Sec7 N-terminal regulatory domains facilitate membrane-proximal activation of the Arf1 GTPase.

Brian C Richardson, Steve L Halaby, Margaret A Gustafson, J Christopher Fromme

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in eLife, 2016. 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 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.5field-weighted citation impact, top 13% 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

18 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Sec7 regulatory domains scaffold autoinhibited and active conformations.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. In Silico Analysis of Huntingtin Homologs in Lower Eukaryotes.International journal of molecular sciences · 2021
    Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
4 · The record

Corrections and comments

  • Erratum issued
    2016
5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Brian C RichardsonDepartment of Molecular Biology and Genetics, Cornell University, Ithaca, United States.ORCID http://orcid.org/0000-0002-5434-1500
Steve L HalabyDepartment of Molecular Biology and Genetics, Cornell University, Ithaca, United States.
Margaret A GustafsonDepartment of Molecular Biology and Genetics, Cornell University, Ithaca, United States.
J Christopher FrommeDepartment of Molecular Biology and Genetics, Cornell University, Ithaca, United States.ORCID http://orcid.org/0000-0002-8837-0473
Cornell University · US

Funding

Overall (pp. 40-62)P41GM103485 · NIGMS · CORNELL UNIVERSITY · PI CERIONE, RICHARD A. · 2012 to 2018
$15.5M
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 P41 GM103485NIGMS NIH HHS R01 GM098621NIGMS NIH HHS R01GM098621NIGMS NIH HHS T32 GM007273
6 · The paper itself

Abstract

The Golgi complex is the central sorting compartment of eukaryotic cells. Arf guanine nucleotide exchange factors (Arf-GEFs) regulate virtually all traffic through the Golgi by activating Arf GTPase trafficking pathways. The Golgi Arf-GEFs contain multiple autoregulatory domains, but the precise mechanisms underlying their function remain largely undefined. We report a crystal structure revealing that the N-terminal DCB and HUS regulatory domains of the Arf-GEF Sec7 form a single structural unit. We demonstrate that the established role of the N-terminal region in dimerization is not conserved; instead, a C-terminal autoinhibitory domain is responsible for dimerization of Sec7. We find that the DCB/HUS domain amplifies the ability of Sec7 to activate Arf1 on the membrane surface by facilitating membrane insertion of the Arf1 amphipathic helix. This enhancing function of the Sec7 N-terminal domains is consistent with the high rate of Arf1-dependent trafficking to the plasma membrane necessary for maximal cell growth.

Indexed as

ADP-Ribosylation Factor 1Crystallography, X-RayGuanine Nucleotide Exchange FactorsMembrane ProteinsProtein ConformationProtein Interaction Domains and MotifsSaccharomyces cerevisiaeADP-Ribosylation Factor 1Guanine Nucleotide Exchange FactorsMembrane ProteinsSec7 guanine nucleotide exchange factorsbiophysicscell biologyGolgiGTPase<i>s. cerevisiae</i>structural biologyT. terrestrisvesicle traffic

Identifiers

PMID26765562
PMCPMC4764562
OpenAlexW2248874129

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.