Evidence map›Paper›PMID 10228163›Full record

ArticleThe EMBO journal1999

Inhibition of the receptor-binding function of clathrin adaptor protein AP-2 by dominant-negative mutant mu2 subunit and its effects on endocytosis.

A Nesterov, R E Carter, T Sorkina, G N Gill, A Sorkin

Abstract readComparative Study
In one paragraph

Article in The EMBO journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.

0numbers the graph read from it
0cells of the map it votes in
87citing papers in PubMed
–field-weighted citation impact
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

87 citing papers in PubMed.

  1. Article
  2. A cytoplasmic motif in HLA-E that drives clathrin-mediated endocytosis and VCP-associated postendocytic trafficking.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  3. Review
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  5. Article
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  7. Article
  8. The motif EThe Journal of biological chemistry · 2020
    Article
  9. Article
  10. Article
  11. Article
  12. Article
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  14. Article
  15. Alternative Splicing in Ca(V)2.2 Regulates Neuronal Trafficking via Adaptor Protein Complex-1 Adaptor Protein Motifs.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

27 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.

A NesterovDepartment of Medicine, University of California at San Diego, La Jolla, CA 92093, USA.
R E Carter
T Sorkina
G N Gill
A Sorkin

Funding

University of Colorado Cancer Center Support Grant - Lung Cancer Patient-Derived Xenografts with Autologous Human Immune SystemsP30CA046934 · NCI · UNIVERSITY OF COLORADO DENVER · PI James V Degregori · 1988 to 2026
$117.0M
VESICULAR TRAFFICKING OF THE EGF RECEPTORP01CA058689 · NCI · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI BALCH, WILLIAM E · 1993 to 2002
$5.0M
MECHANISM OF GROWTH FACTOR RECEPTOR ENDOCYTOSISR29DK046817 · NIDDK · VANDERBILT UNIVERSITY · PI SORKIN, ALEXANDER D · 1994 to 1999
–
NCI NIH HHS CA46934NCI NIH HHS CA 58689NIDDK NIH HHS DK46817
6 · The paper itself

Abstract

Although interactions between the mu2 subunit of the clathrin adaptor protein complex AP-2 and tyrosine-based internalization motifs have been implicated in the selective recruitment of cargo molecules into coated pits, the functional significance of this interaction for endocytosis of many types of membrane proteins remains unclear. To analyze the function of mu2-receptor interactions, we constructed an epitope-tagged mu2 that incorporates into AP-2 and is targeted to coated pits. Mutational analysis revealed that Asp176 and Trp421 of mu2 are involved in the interaction with internalization motifs of TGN38 and epidermal growth factor (EGF) receptor. Inducible overexpression of mutant mu2, in which these two residues were changed to alanines, resulted in metabolic replacement of endogenous mu2 in AP-2 complexes and complete abrogation of AP-2 interaction with the tyrosine-based internalization motifs. As a consequence, endocytosis of the transferrin receptor was severely impaired. In contrast, internalization of the EGF receptor was not affected. These results demonstrate the potential usefulness of the dominant-interfering approach for functional analysis of the adaptor protein family, and indicate that clathrin-mediated endocytosis may proceed in both a mu2-dependent and -independent manner.

Indexed as

Adaptor Protein Complex 1Adaptor Protein Complex 2Adaptor Protein Complex 3Adaptor Protein Complex mu SubunitsEndocytosisAdaptor Protein Complex alpha SubunitsAdaptor Proteins, Vesicular TransportAnimalsBinding SitesBiological TransportCell CompartmentationCoated Pits, Cell-MembraneErbB ReceptorsHumansMembrane ProteinsPoint MutationAdaptor Protein Complex 1adaptor protein complex 1, mu 2 subunitAdaptor Protein Complex 2adaptor protein complex 2, mu 2 subunitAdaptor Protein Complex 3Adaptor Protein Complex alpha SubunitsAdaptor Protein Complex mu SubunitsAdaptor Proteins, Vesicular TransportAP1M2 protein, humanAP3M2 protein, humanErbB ReceptorsMembrane ProteinsReceptors, Cell SurfaceReceptors, Transferrin

Identifiers

PMID10228163
PMCPMC1171331

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.