Evidence map›Paper›PMID 22291037›Full record

ArticleThe Journal of cell biology2012

The small G protein Arl1 directs the trans-Golgi-specific targeting of the Arf1 exchange factors BIG1 and BIG2.

Chantal Christis, Sean Munro

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

44 citing papers in PubMed, 68 citations in OpenAlex.

  1. ARF GTPases Function at the Golgi.Sub-cellular biochemistry · 2026
    Review
  2. Review
  3. Arf1 and ARFGEF2/Sec71 control neuroblast polarity by anchoring nonmuscle myosin II.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  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. The Arf family GTPases: Regulation of vesicle biogenesis and beyond.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023
    Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Sec71 separates Golgi stacks inJournal of cell science · 2020
    Article
  14. Article
  15. Article
  16. Spatiotemporal dissection of theJournal of cell science · 2019
    Article
  17. Review
  18. Article
  19. Article
  20. Article
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 2 institutions in 1 country.

Chantal ChristisMedical Research Council Laboratory of Molecular Biology, Cambridge CB2 0QH, England, UK.
Sean Munro
Medical Research Council · GBMRC Laboratory of Molecular Biology · GB

Funding

Medical Research Council MC_U105178783
6 · The paper itself

Abstract

The small G protein Arf1 regulates Golgi traffic and is activated by two related types of guanine nucleotide exchange factor (GEF). GBF1 acts at the cis-Golgi, whereas BIG1 and its close paralog BIG2 act at the trans-Golgi. Peripheral membrane proteins such as these GEFs are often recruited to membranes by small G proteins, but the basis for specific recruitment of Arf GEFs, and hence Arfs, to Golgi membranes is not understood. In this paper, we report a liposome-based affinity purification method to identify effectors for small G proteins of the Arf family. We validate this with the Drosophila melanogaster Arf1 orthologue (Arf79F) and the related class II Arf (Arf102F), which showed a similar pattern of effector binding. Applying the method to the Arf-like G protein Arl1, we found that it binds directly to Sec71, the Drosophila ortholog of BIG1 and BIG2, via an N-terminal region. We show that in mammalian cells, Arl1 is necessary for Golgi recruitment of BIG1 and BIG2 but not GBF1. Thus, Arl1 acts to direct a trans-Golgi-specific Arf1 GEF, and hence active Arf1, to the trans side of the Golgi.

Indexed as

ADP-Ribosylation FactorsAnimalsDrosophila melanogasterGolgi ApparatusGuanine Nucleotide Exchange FactorsHeLa CellsHumansMembrane ProteinsADP-ribosylation factor related proteinsADP-Ribosylation FactorsARFGEF1 protein, humanARFGEF2 protein, humanGuanine Nucleotide Exchange FactorsMembrane Proteins

Identifiers

PMID22291037
PMCPMC3275380
OpenAlexW2114366125

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.