Evidence map›Paper›PMID 10430869›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1999

Crystal structure of the alpha appendage of AP-2 reveals a recruitment platform for clathrin-coat assembly.

L M Traub, M A Downs, J L Westrich, D H Fremont

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
5.4field-weighted citation impact, top 4% 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

62 citing papers in PubMed, 178 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Diversity, Origin and Evolution of the ESCRT Systems.bioRxiv : the preprint server for biology · 2024
    Article
  5. Article
  6. Synaptic tau: A pathological or physiological phenomenon?Acta neuropathologica communications · 2021
    Review
  7. Article
  8. Linton Mark Traub (1962-2020).The Journal of cell biology · 2021
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Weak Molecular Interactions in Clathrin-Mediated Endocytosis.Frontiers in molecular biosciences · 2017
    Review
  16. Article
  17. Review
  18. Review
  19. Article
  20. Article

2 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

L M TraubDepartment of Internal Medicine, Washington University School of Medicine, 660 South Euclid Avenue, St. Louis, MO 63110, USA.
M A Downs
J L Westrich
D H Fremont
Washington University in St. Louis · US

Funding

CLATHRIN COATED VESICLES AND LYSOSOME FUNCTIONR01DK053249 · NIDDK · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI TRAUB, LINTON M. · 1998 to 2011
$3.0M
NIDDK NIH HHS DK53249NIDDK NIH HHS R01 DK053249Wellcome Trust
6 · The paper itself

Abstract

AP-2 adaptors regulate clathrin-bud formation at the cell surface by recruiting clathrin trimers to the plasma membrane and by selecting certain membrane proteins for inclusion within the developing clathrin-coat structure. These functions are performed by discrete subunits of the adaptor heterotetramer. The carboxyl-terminal appendage of the AP-2 alpha subunit appears to regulate the translocation of several endocytic accessory proteins to the bud site. We have determined the crystal structure of the alpha appendage at 1.4-A resolution by multiwavelength anomalous diffraction phasing. It is composed of two distinct structural modules, a beta-sandwich domain and a mixed alpha-beta platform domain. Structure-based mutagenesis shows that alterations to the molecular surface of a highly conserved region on the platform domain differentially affect associations of the appendage with amphiphysin, eps15, epsin, and AP180, revealing a common protein-binding interface.

Indexed as

Monomeric Clathrin Assembly ProteinsAdaptor Proteins, Vesicular TransportAmino Acid SequenceAnimalsClathrinCrystallography, X-RayHumansMacromolecular SubstancesMiceModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedNerve Tissue ProteinsPhosphoproteinsProtein Structure, SecondaryRecombinant Fusion ProteinsAdaptor Proteins, Vesicular TransportClathrinclathrin assembly protein AP180Macromolecular SubstancesMonomeric Clathrin Assembly ProteinsNerve Tissue ProteinsPhosphoproteinsRecombinant Fusion Proteins

Identifiers

PMID10430869
PMCPMC17706
OpenAlexW2032675576

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.