Evidence map›Paper›PMID 15377783›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2004

Crystal structure of the clathrin adaptor protein 1 core.

Ekaterina E Heldwein, Eric Macia, Jing Wang, Helen L Yin, Tomas Kirchhausen, Stephen C Harrison

Open access · greenAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 118 papers.

0numbers the graph read from it
0cells of the map it votes in
118citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

118 citing papers in PubMed, 187 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. 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
  8. Article
  9. Article
  10. Article
  11. FgAP1Journal of fungi (Basel, Switzerland) · 2023
    Article
  12. Oligomer-to-monomer transition underlies the chaperone function of AAGAB in AP1/AP2 assembly.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  13. Article
  14. Article
  15. Article
  16. Membrane Lipids in Epithelial Polarity: Sorting out the PIPs.Frontiers in cell and developmental biology · 2022
    Review
  17. Article
  18. Review
  19. Review
  20. Article

58 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 3 institutions in 1 country.

Ekaterina E HeldweinChildren's Hospital, Howard Hughes Medical Institute, Department of Cell Biology, and CBR Institute for Biomedical Research, Harvard Medical School, Boston, MA 02115, USA.
Eric Macia
Jing Wang
Helen L Yin
Tomas Kirchhausen
Stephen C Harrison
Southwestern Medical Center · USThe University of Texas Southwestern Medical Center · USHoward Hughes Medical Institute · US

Funding

STRUCTURAL CHEMISTRY OF CLATHRIN &ASSOCIATED PROTEINSR01GM036548 · NIGMS · IMMUNE DISEASE INSTITUTE, INC. · PI KIRCHHAUSEN, TOMAS · 1986 to 2014
$9.8M
Phosphoinsitide Regulation of the GolgiR01GM066110 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI YIN, HELEN L · 2004 to 2011
$3.0M
NIGMS NIH HHS GM066110NIGMS NIH HHS GM36548NIGMS NIH HHS R01 GM036548NIGMS NIH HHS R01 GM066110
6 · The paper itself

Abstract

The heterotetrameric adaptor proteins (AP complexes) link the outer lattice of clathrin-coated vesicles with membrane-anchored cargo molecules. We report the crystal structure of the core of the AP-1 complex, which functions in the trans-Golgi network (TGN). Packing of complexes in the crystal generates an exceptionally long (1,135-A) unit-cell axis, but the 6-fold noncrystallographic redundancy yields an excellent map at 4-A resolution. The AP-1 core comprises N-terminal fragments of the two large chains, beta1 and gamma, and the intact medium and small chains, micro1 and sigma1. Its molecular architecture closely resembles that of the core of AP-2, the plasma-membrane-specific adaptor, for which a structure has been determined. Both structures represent an "inactive" conformation with respect to binding of cargo with a tyrosine-based sorting signal. TGN localization of AP-1 depends on the small GTPase, Arf1, and the phosphoinositide, PI-4-P. We show that directed mutations of residues at a particular corner of the gamma chain prevent recruitment to the TGN in cells and diminish PI-4-P-dependent, but not Arf1-dependent, liposome binding in vitro.

Indexed as

Adaptor Protein Complex 1Adaptor Protein Complex SubunitsAmino Acid SequenceAmino Acid SubstitutionAnimalsBinding SitesCrystallography, X-RayEscherichia coliHeLa CellsHumansMiceModels, MolecularMolecular Sequence DataPhosphatidylinositolsProtein BindingProtein Structure, QuaternaryAdaptor Protein Complex 1Adaptor Protein Complex SubunitsPhosphatidylinositolsRecombinant Proteins

Identifiers

PMID15377783
PMCPMC521094
OpenAlexW1972665490

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.