Evidence map›Paper›PMID 29361542›Full record

ArticleJournal of cell science2018

The ARF guanine nucleotide exchange factor GBF1 is targeted to Golgi membranes through a PIP-binding domain.

Justyna M Meissner, Jay M Bhatt, Eunjoo Lee, Melanie L Styers, Anna A Ivanova, Richard A Kahn, Elizabeth Sztul

Open access · bronzeAbstract read
In one paragraph

Article in Journal of cell science, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

26 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Article
  3. ARF GTPases Function at the Golgi.Sub-cellular biochemistry · 2026
    Review
  4. Phosphatidylinositol 4-phosphate; A minor lipid with multiple personalities.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2025
    Review
  5. Arfs on the Golgi: four conductors, one orchestra.Frontiers in molecular biosciences · 2025
    Review
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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

7 authors at 3 institutions in 1 country.

Justyna M MeissnerDepartment of Cell, Developmental and Integrative Biology, University of Alabama at Birmingham, Birmingham, AL 35294, USA meissner@uab.edu.ORCID 0000-0002-8667-908X
Jay M BhattDepartment of Cell, Developmental and Integrative Biology, University of Alabama at Birmingham, Birmingham, AL 35294, USA.
Eunjoo LeeDepartment of Cell, Developmental and Integrative Biology, University of Alabama at Birmingham, Birmingham, AL 35294, USA.
Melanie L StyersDepartment of Biology, Birmingham-Southern College, Birmingham, AL 35254, USA.
Anna A IvanovaDepartment of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322, USA.
Richard A KahnDepartment of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322, USA.
Elizabeth SztulDepartment of Cell, Developmental and Integrative Biology, University of Alabama at Birmingham, Birmingham, AL 35294, USA.
University of Alabama at Birmingham · USEmory University · USBirmingham–Southern College · US

Funding

Molecular mechanisms of ARF family GTPasesR35GM122568 · NIGMS · EMORY UNIVERSITY · PI KAHN, RICHARD A · 2017 to 2024
$3.7M
The Regulation and Cellular Activities of the ARL2 GTPaseR01GM090158 · NIGMS · EMORY UNIVERSITY · PI KAHN, RICHARD A · 2010 to 2017
$2.5M
Role of host protein GBF1 in organizing enterovirus replication complexesR01AI125561 · NIAID · UNIV OF MARYLAND, COLLEGE PARK · PI BELOV, GEORGE A. · 2016 to 2020
$1.9M
Spatio-temporal regulation of ARF signaling in vesicle formationR01GM122802 · NIGMS · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI SZTUL, ELIZABETH S · 2017 to 2020
$1.5M
NIAID NIH HHS R01 AI125561NIGMS NIH HHS R01 GM090158NIGMS NIH HHS R01 GM122802NIGMS NIH HHS R35 GM122568
6 · The paper itself

Abstract

ADP-ribosylation factors (ARF) GTPases are activated by guanine nucleotide exchange factors (GEFs) to support cellular homeostasis. Key to understanding spatio-temporal regulation of ARF signaling is the mechanism of GEF recruitment to membranes. Small GEFs are recruited through phosphoinositide (PIP) binding by a pleckstrin homology (PH) domain downstream from the catalytic Sec7 domain (Sec7d). The large GEFs lack PH domains, and their recruitment mechanisms are poorly understood. We probed Golgi recruitment of GBF1, a GEF catalyzing ARF activation required for Golgi homeostasis. We show that the homology downstream of Sec7d-1 (HDS1) regulates Golgi recruitment of GBF1. We document that GBF1 binds phosphoinositides, preferentially PI3P, PI4P and PI(4,5)P

Indexed as

Amino Acid MotifsAmino Acid SequenceGolgi ApparatusGuanine Nucleotide Exchange FactorsHeLa CellsHomeostasisHumansIntracellular MembranesPhosphatidylinositolsProtein BindingProtein DomainsGBF1 protein, humanGuanine Nucleotide Exchange FactorsPhosphatidylinositolsADP-ribosylation factorsGBF1GolgiHDS1 domainMembrane traffickingSec7 guanine nucleotide exchange factor

Identifiers

PMID29361542
PMCPMC5826047
OpenAlexW2779083329

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.