Evidence map›Paper›PMID 10436028›Full record

ArticleMolecular biology of the cell1999

Characterization of a fourth adaptor-related protein complex.

J Hirst, N A Bright, B Rous, M S Robinson

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 124 papers.

0numbers the graph read from it
0cells of the map it votes in
124citing papers in PubMed
8.8field-weighted citation impact, top 2% 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

124 citing papers in PubMed, 318 citations in OpenAlex.

  1. Article
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  5. Uncovering cargo clients and accessory factors of AP-1 and AP-4 through vesicle proteomics.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Characterization of the malaria parasiteMicrobiology spectrum · 2025
    Article
  7. Review
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  12. Review
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  17. Article
  18. Getting where you want to go.Molecular biology of the cell · 2022
    Article
  19. Article
  20. Article

64 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

4 authors at 1 institution in 1 country.

J HirstUniversity of Cambridge, Department of Clinical Biochemistry and Cambridge Institute for Medical Research, Cambridge CB2 2XY, England.
N A Bright
B Rous
M S Robinson
University of Cambridge · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

Adaptor protein complexes (APs) function as vesicle coat components in different membrane traffic pathways; however, there are a number of pathways for which there is still no candidate coat. To find novel coat components related to AP complexes, we have searched the expressed sequence tag database and have identified, cloned, and sequenced a new member of each of the four AP subunit families. We have shown by a combination of coimmunoprecipitation and yeast two-hybrid analysis that these four proteins (epsilon, beta4, mu4, and sigma4) are components of a novel adaptor-like heterotetrameric complex, which we are calling AP-4. Immunofluorescence reveals that AP-4 is localized to approximately 10-20 discrete dots in the perinuclear region of the cell. This pattern is disrupted by treating the cells with brefeldin A, indicating that, like other coat proteins, the association of AP-4 with membranes is regulated by the small GTPase ARF. Immunogold electron microscopy indicates that AP-4 is associated with nonclathrin-coated vesicles in the region of the trans-Golgi network. The mu4 subunit of the complex specifically interacts with a tyrosine-based sorting signal, indicating that, like the other three AP complexes, AP-4 is involved in the recognition and sorting of cargo proteins with tyrosine-based motifs. AP-4 is of relatively low abundance, but it is expressed ubiquitously, suggesting that it participates in a specialized trafficking pathway but one that is required in all cell types.

Indexed as

Adaptor Proteins, Vesicular TransportAmino Acid SequenceAnimalsBinding SitesCell LineCloning, MolecularHumansMicroscopy, ElectronMolecular Sequence DataNerve Tissue ProteinsPhosphoproteinsProteinsRatsRecombinant Fusion ProteinsSequence Homology, Amino AcidSignal TransductionAdaptor Proteins, Vesicular TransportNerve Tissue ProteinsPhosphoproteinsProteinsRecombinant Fusion ProteinsTyrosine

Identifiers

PMID10436028
PMCPMC25515
OpenAlexW2096973289

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.