Evidence map›Paper›PMID 11707398›Full record

ArticleThe EMBO journal2001

Functional and physical interactions of the adaptor protein complex AP-4 with ADP-ribosylation factors (ARFs).

M Boehm, R C Aguilar, J S Bonifacino

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
2.1field-weighted citation impact, top 14% 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

52 citing papers in PubMed, 119 citations in OpenAlex.

  1. Review
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  4. A NovelIranian journal of medical sciences · 2026
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  6. Characterization of the malaria parasiteMicrobiology spectrum · 2025
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  7. Structural elucidation of how ARF small GTPases induce membrane tubulation for vesicle fission.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Article
  9. A structure-based mechanism for initiation of AP-3 coated vesicle formation.Proceedings of the National Academy of Sciences of the United States of America · 2024
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  20. A novel loss of function mutation in adaptor protein complex 4, subunit mu-1 causing autosomal recessive spastic paraplegia 50.Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology · 2021
    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

3 authors at 1 institution in 1 country.

M BoehmCell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA.
R C Aguilar
J S Bonifacino
National Institutes of Health · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

AP-4 is a member of the family of heterotetrameric adaptor protein (AP) complexes that mediate the sorting of integral membrane proteins in post-Golgi compartments. This complex consists of four subunits (epsilon, beta4, mu4 and sigma4) and localizes to the cytoplasmic face of the trans-Golgi network (TGN). Here, we show that the recruitment of endogenous AP-4 to the TGN in vivo is regulated by the small GTP-binding protein ARF1. In addition, we demonstrate a direct interaction of the epsilon and mu4 subunits of AP-4 with ARF1. epsilon binds only to ARF1-GTP and requires residues in the switch I and switch II regions of ARF1. In contrast, mu4 binds equally well to the GTP- and GDP-bound forms of ARF1 and is less dependent on switch I and switch II residues. These observations establish AP-4 as an ARF1 effector and suggest a novel mode of interaction between ARF1 and an AP complex involving both constitutive and regulated interactions.

Indexed as

Adaptor Proteins, Vesicular TransportADP-Ribosylation FactorsBinding SitesBrefeldin ACarrier ProteinsCell MembraneGolgi ApparatusHeLa CellsHumansImmunoblottingMembrane ProteinsMicroscopy, FluorescenceModels, BiologicalMutagenesis, Site-DirectedMutationPrecipitin TestsAdaptor Proteins, Vesicular TransportADP-Ribosylation FactorsBrefeldin ACarrier ProteinsMembrane Proteins

Identifiers

PMID11707398
PMCPMC125733
OpenAlexW2065896153

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.