Evidence map›Paper›PMID 14581457›Full record

ArticleThe Journal of cell biology2003

The AP-1A and AP-1B clathrin adaptor complexes define biochemically and functionally distinct membrane domains.

Heike Fölsch, Marc Pypaert, Sandra Maday, Laurence Pelletier, Ira Mellman

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 128 papers.

0numbers the graph read from it
0cells of the map it votes in
128citing papers in PubMed
6.2field-weighted citation impact, top 3% 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

128 citing papers in PubMed, 198 citations in OpenAlex.

  1. Article
  2. Article
  3. Virus infection and vesicle trafficking.Frontiers in immunology · 2025
    Review
  4. Article
  5. Article
  6. Protein sorting from endosomes to the TGN.Frontiers in cell and developmental biology · 2023
    Review
  7. Review
  8. Review
  9. Article
  10. Article
  11. Membrane Lipids in Epithelial Polarity: Sorting out the PIPs.Frontiers in cell and developmental biology · 2022
    Review
  12. Article
  13. Novel function for AP-1B during cell migration.Molecular biology of the cell · 2020
    Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. Article

68 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

5 authors at 2 institutions in 1 country.

Heike FölschDepartment of Cell Biology, Ludwig Institute for Cancer Research, Yale University School of Medicine, New Haven, CT 06520, USA. h-folsch@northwestern.edu
Marc Pypaert
Sandra Maday
Laurence Pelletier
Ira Mellman
Ludwig Cancer Research · USNorthwestern University · US

Funding

MOLECULAR SORTING DURING INTRACELLULAR TRANSPORTR01GM029765 · NIGMS · YALE UNIVERSITY · PI MELLMAN, IRA S · 1985 to 2006
$2.6M
NIGMS NIH HHS GM29765NIGMS NIH HHS R01 GM029765
6 · The paper itself

Abstract

Most epithelial cells contain two AP-1 clathrin adaptor complexes. AP-1A is ubiquitously expressed and involved in transport between the TGN and endosomes. AP-1B is expressed only in epithelia and mediates the polarized targeting of membrane proteins to the basolateral surface. Both AP-1 complexes are heterotetramers and differ only in their 50-kD mu1A or mu1B subunits. Here, we show that AP-1A and AP-1B, together with their respective cargoes, define physically and functionally distinct membrane domains in the perinuclear region. Expression of AP-1B (but not AP-1A) enhanced the recruitment of at least two subunits of the exocyst complex (Sec8 and Exo70) required for basolateral transport. By immunofluorescence and cell fractionation, the exocyst subunits were found to selectively associate with AP-1B-containing membranes that were both distinct from AP-1A-positive TGN elements and more closely apposed to transferrin receptor-positive recycling endosomes. Thus, despite the similarity of the two AP-1 complexes, AP-1A and AP-1B exhibit great specificity for endosomal transport versus cell polarity.

Indexed as

Saccharomyces cerevisiae ProteinsAdaptor Protein Complex 1Adaptor Protein Complex mu SubunitsAdenoviridaeAnimalsCaco-2 CellsCarrier ProteinsCell CompartmentationCell Line, TransformedCell PolarityClathrinCoated Pits, Cell-MembraneEndosomesEpithelial CellsExocytosisFungal ProteinsAdaptor Protein Complex 1adaptor protein complex 1, mu 1 subunitAdaptor Protein Complex mu SubunitsAP1M1 protein, humanCarrier ProteinsClathrinEXO70 protein, S cerevisiaeEXOC4 protein, humanFungal ProteinsMembrane ProteinsReceptors, TransferrinSaccharomyces cerevisiae ProteinsVesicular Transport Proteins

Identifiers

PMID14581457
PMCPMC2173537
OpenAlexW2039979410

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.