Evidence map›Paper›PMID 10459011›Full record

ArticleThe Journal of cell biology1999

Phosphoinositide-AP-2 interactions required for targeting to plasma membrane clathrin-coated pits.

I Gaidarov, J H Keen

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 104 papers.

0numbers the graph read from it
0cells of the map it votes in
104citing papers in PubMed
9.2field-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

104 citing papers in PubMed, 309 citations in OpenAlex.

  1. Article
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  8. Stepwise assembly of the AP2 endocytic clathrin adaptor complex.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
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  10. Review
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  14. A PtdIns(3,4,5)PDevelopmental cell · 2021
    Article
  15. Review
  16. Article
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  19. Article
  20. Review

44 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

2 authors at 1 institution in 1 country.

I GaidarovKimmel Cancer Institute and the Department of Microbiology and Immunology, Thomas Jefferson University, Philadelphia, Pennsylvania 19107, USA.
J H Keen
Thomas Jefferson University · US

Funding

Regulation of Clathrin and Adaptor FunctionR01GM049217 · NIGMS · THOMAS JEFFERSON UNIVERSITY · PI KEEN, JAMES H · 1994 to 2016
$3.8M
NIGMS NIH HHS GM-49217NIGMS NIH HHS R01 GM049217
6 · The paper itself

Abstract

The clathrin-associated AP-2 adaptor protein is a major polyphosphoinositide-binding protein in mammalian cells. A high affinity binding site has previously been localized to the NH(2)-terminal region of the AP-2 alpha subunit (Gaidarov et al. 1996. J. Biol. Chem. 271:20922-20929). Here we used deletion and site- directed mutagenesis to determine that alpha residues 21-80 comprise a discrete folding and inositide-binding domain. Further, positively charged residues located within this region are involved in binding, with a lysine triad at positions 55-57 particularly critical. Mutant peptides and protein in which these residues were changed to glutamine retained wild-type structural and functional characteristics by several criteria including circular dichroism spectra, resistance to limited proteolysis, and clathrin binding activity. When expressed in intact cells, mutated alpha subunit showed defective localization to clathrin-coated pits; at high expression levels, the appearance of endogenous AP-2 in coated pits was also blocked consistent with a dominant-negative phenotype. These results, together with recent work indicating that phosphoinositides are also critical to ligand-dependent recruitment of arrestin-receptor complexes to coated pits (Gaidarov et al. 1999. EMBO (Eur. Mol. Biol. Organ.) J. 18:871-881), suggest that phosphoinositides play a critical and general role in adaptor incorporation into plasma membrane clathrin-coated pits.

Indexed as

Adaptor Protein Complex alpha SubunitsAdaptor Proteins, Vesicular TransportAmino Acid SequenceAmino Acid SubstitutionAnimalsBinding SitesBiological TransportBrainCattleCell LineCell MembraneCircular DichroismClathrinCoated Pits, Cell-MembraneGlutamineLysineAdaptor Protein Complex alpha SubunitsAdaptor Proteins, Vesicular TransportClathrinGlutamineLysineMembrane ProteinsPhosphatidylinositols

Identifiers

PMID10459011
PMCPMC2156139
OpenAlexW2019196882

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.