Evidence map›Paper›PMID 15051738›Full record

ArticleThe Journal of cell biology2004

Localization of the AP-3 adaptor complex defines a novel endosomal exit site for lysosomal membrane proteins.

Andrew A Peden, Viola Oorschot, Boris A Hesser, Cary D Austin, Richard H Scheller, Judith Klumperman

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Journal of cell biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 185 papers.

0numbers the graph read from it
0cells of the map it votes in
185citing papers in PubMed
9.4field-weighted citation impact, top 1% 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

185 citing papers in PubMed, 353 citations in OpenAlex.

  1. Oncogenic Gα signaling requires AP-3-dependent recruitment to the endolysosomal compartment.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
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  6. NPC1 trafficking via VPS41-dependent LAMP carriers regulates endosomal cholesterol homeostasis.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
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  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
    Article
  10. Article
  11. Article
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  13. The p53 target DRAM1 modulates calcium homeostasis and ER stress by promoting contact between lysosomes and the ER through STIM1.Proceedings of the National Academy of Sciences of the United States of America · 2024
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  18. Review
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  20. Adaptor protein-3 produces synaptic vesicles that release phasic dopamine.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article

125 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

6 authors at 1 institution in 1 country.

Andrew A PedenGenentech Inc., South San Francisco, CA 94080, USA.
Viola Oorschot
Boris A Hesser
Cary D Austin
Richard H Scheller
Judith Klumperman
University Medical Center Utrecht · NL

Funding

Wellcome Trust
6 · The paper itself

Abstract

The adaptor protein (AP) 3 adaptor complex has been implicated in the transport of lysosomal membrane proteins, but its precise site of action has remained controversial. Here, we show by immuno-electron microscopy that AP-3 is associated with budding profiles evolving from a tubular endosomal compartment that also exhibits budding profiles positive for AP-1. AP-3 colocalizes with clathrin, but to a lesser extent than does AP-1. The AP-3- and AP-1-bearing tubular compartments contain endocytosed transferrin, transferrin receptor, asialoglycoprotein receptor, and low amounts of the cation-independent mannose 6-phosphate receptor and the lysosome-associated membrane proteins (LAMPs) 1 and 2. Quantitative analysis revealed that of these distinct cargo proteins, only LAMP-1 and LAMP-2 are concentrated in the AP-3-positive membrane domains. Moreover, recycling of endocytosed LAMP-1 and CD63 back to the cell surface is greatly increased in AP-3-deficient cells. Based on these data, we propose that AP-3 defines a novel pathway by which lysosomal membrane proteins are transported from tubular sorting endosomes to lysosomes.

Indexed as

Adaptor Protein Complex 3Adaptor Protein Complex beta SubunitsAnimalsCell LineCell MembraneEndosomesKineticsLysosomesMembrane ProteinsProtein TransportTranscription Factor AP-1Transcription Factorstrans-Golgi NetworkAdaptor Protein Complex 3Adaptor Protein Complex beta SubunitsAp3d1 protein, mouseMembrane ProteinsTranscription Factor AP-1Transcription Factors

Identifiers

PMID15051738
PMCPMC2172074
OpenAlexW2098485024

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.