Evidence map›Paper›PMID 11157985›Full record

ArticleThe Journal of cell biology2001

Distribution and function of AP-1 clathrin adaptor complexes in polarized epithelial cells.

H Fölsch, M Pypaert, P Schu, I Mellman

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 131 papers.

0numbers the graph read from it
0cells of the map it votes in
131citing papers in PubMed
7.6field-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

131 citing papers in PubMed, 244 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. FgAP1Journal of fungi (Basel, Switzerland) · 2023
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Novel function for AP-1B during cell migration.Molecular biology of the cell · 2020
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. The Journal of biological chemistry · 2019
    Article
  20. Article

71 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 3 institutions in 2 countries.

H FölschDepartment of Cell Biology and Ludwig Institute for Cancer Research, Yale University School of Medicine, New Haven, Connecticut 06520, USA.
M Pypaert
P Schu
I Mellman
Ludwig Cancer Research · USUniversity of Göttingen · DEYale 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

Expression of the epithelial cell-specific heterotetrameric adaptor complex AP-1B is required for the polarized distribution of many membrane proteins to the basolateral surface of LLC-PK1 kidney cells. AP-1B is distinguished from the ubiquitously expressed AP-1A by exchange of its single 50-kD mu subunit, mu1A, being replaced by the closely related mu1B. Here we show that this substitution is sufficient to couple basolateral plasma membrane proteins, such as a low-density lipoprotein receptor (LDLR), to the AP-1B complex and to clathrin. The interaction between LDLR and AP-1B is likely to occur in the trans-Golgi network (TGN), as was suggested by the localization of functional, epitope-tagged mu1 by immunofluorescence and immunoelectron microscopy. Tagged AP-1A and AP-1B complexes were found in the perinuclear region close to the Golgi complex and recycling endosomes, often in clathrin-coated buds and vesicles. Yet, AP-1A and AP-1B localized to different subdomains of the TGN, with only AP-1A colocalizing with furin, a membrane protein that uses AP-1 to recycle between the TGN and endosomes. We conclude that AP-1B functions by interacting with its cargo molecules and clathrin in the TGN, where it acts to sort basolateral proteins from proteins destined for the apical surface and from those selected by AP-1A for transport to endosomes and lysosomes.

Indexed as

Adaptor Protein Complex 1Adaptor Protein Complex 2Adaptor Protein Complex mu SubunitsCell PolarityAdaptor Protein Complex alpha SubunitsAdaptor Protein Complex gamma SubunitsAdaptor Proteins, Vesicular TransportAdenoviridaeAnimalsClathrinEpithelial CellsFurinGolgi ApparatusMembrane ProteinsProtein SubunitsProtein TransportAdaptor Protein Complex 1adaptor protein complex 1, mu 1 subunitadaptor protein complex 1, mu 2 subunitAdaptor Protein Complex 2adaptor protein complex 2, mu 1 subunitAdaptor Protein Complex alpha SubunitsAdaptor Protein Complex gamma SubunitsAdaptor Protein Complex mu SubunitsAdaptor Proteins, Vesicular TransportClathrinFurinMembrane ProteinsProtein SubunitsReceptors, LDLSubtilisins

Identifiers

PMID11157985
PMCPMC2195989
OpenAlexW2116537957

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.