Evidence map›Paper›PMID 10613896›Full record

ArticleThe Journal of cell biology1999

The eps15 homology (EH) domain-based interaction between eps15 and hrb connects the molecular machinery of endocytosis to that of nucleocytosolic transport.

M Doria, A E Salcini, E Colombo, T G Parslow, P G Pelicci, P P Di Fiore

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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 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

25 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Functional characterization of 67 endocytic accessory proteins using multiparametric quantitative analysis of CCP dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  5. Review
  6. Article
  7. An Overview of The Globozoospermia as A Multigenic Identified Syndrome.International journal of fertility & sterility · 2019
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Role of HRB in clathrin-dependent endocytosis.The Journal of biological chemistry · 2008
    Article
  17. Article
  18. Article
  19. Article
  20. Article
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 2 countries.

M DoriaDepartment of Experimental Oncology, European Institute of Oncology, 20141 Milan, Italy.
A E Salcini
E Colombo
T G Parslow
P G Pelicci
P P Di Fiore
European Institute of Oncology · ITUniversity of Bari Aldo Moro · ITUniversity of California, San Francisco · US

Funding

GAG PROTEIN/RNA INTERACTIONS IN THE HIV LIFECYCLER01AI040317 · NIAID · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI PARSLOW, TRISTRAM G. · 1996 to 2005
$1.9M
NIAID NIH HHS AI40317NIAID NIH HHS R01 AI040317Telethon D.090
6 · The paper itself

Abstract

The Eps15 homology (EH) module is a protein-protein interaction domain that establishes a network of connections involved in various aspects of endocytosis and sorting. The finding that EH-containing proteins bind to Hrb (a cellular cofactor of the Rev protein) and to the related protein Hrbl raised the possibility that the EH network might also influence the so-called Rev export pathway, which mediates nucleocytoplasmic transfer of proteins and RNAs. In this study, we demonstrate that Eps15 and Eps15R, two EH-containing proteins, synergize with Hrb and Hrbl to enhance the function of Rev in the export pathway. In addition, the EH-mediated association between Eps15 and Hrb is required for the synergistic effect. The interaction between Eps15 and Hrb occurs in the cytoplasm, thus pointing to an unexpected site of action of Hrb, and to a possible role of the Eps15-Hrb complex in regulating the stability of Rev.

Indexed as

EndocytosisNuclear Pore Complex ProteinsRNA-Binding ProteinsAdaptor Proteins, Signal TransducingAnimalsBiological TransportCalcium-Binding ProteinsCell CompartmentationCell LineCell NucleusCytosolDrug SynergismGene Products, revNuclear ProteinsPhosphoproteinsSequence Homology, Amino AcidAdaptor Proteins, Signal TransducingAGFG1 protein, humanCalcium-Binding ProteinsEps15-rs protein, mouseGene Products, revNuclear Pore Complex ProteinsNuclear ProteinsPhosphoproteinsRNA-Binding Proteins

Identifiers

PMID10613896
PMCPMC2174238
OpenAlexW2072742255

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.