Evidence map›Paper›PMID 18200045›Full record

ArticleThe EMBO journal2008

Structure of the Eps15-stonin2 complex provides a molecular explanation for EH-domain ligand specificity.

Julia Rumpf, Bernd Simon, Nadja Jung, Tanja Maritzen, Volker Haucke, Michael Sattler, Yvonne Groemping

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

18 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Intersectin scaffold proteins and their role in cell signaling and endocytosis.Biochimica et biophysica acta. Molecular cell research · 2017
    Review
  8. Article
  9. Article
  10. Predicting physical interactions between protein complexes.Molecular & cellular proteomics : MCP · 2013
    Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Article
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  18. Review
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

7 authors at 4 institutions in 1 country.

Julia RumpfDepartment of Biomolecular Mechanisms, Max-Planck-Institute for Medical Research, Heidelberg, Germany.
Bernd Simon
Nadja Jung
Tanja Maritzen
Volker Haucke
Michael Sattler
Yvonne Groemping
Freie Universität Berlin · DEMax Planck Institute for Medical Research · DEEuropean Molecular Biology Laboratory · DETechnical University of Munich · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Eps15 homology (EH) domain-containing proteins play a key regulatory role in intracellular membrane trafficking and cell signalling. EH domains serve as interaction platforms for short peptide motifs comprising the residues NPF within natively unstructured regions of accessory proteins. The EH-NPF interactions described thus far are of very low affinity and specificity. Here, we identify the presynaptic endocytic sorting adaptor stonin2 as a high-affinity ligand for the second EH domain (EH2) of the clathrin accessory protein Eps15. Calorimetric data indicate that both NPF motifs within stonin2 interact with EH2 simultaneously and with sub-micromolar affinity. The solution structure of this complex reveals that the first NPF motif binds to the conserved site on the EH domain, whereas the second motif inserts into a novel hydrophobic pocket. Our data show how combination of two EH-attachment sites provides a means for modulating specificity and allows discrimination from a large pool of potential binding partners containing NPF motifs.

Indexed as

Amino Acid MotifsAmino Acid SequenceAnimalsAnimals, NewbornCalcium-Binding ProteinsCells, CulturedChlorocebus aethiopsClathrinCOS CellsEndocytosisIntracellular Signaling Peptides and ProteinsLigandsMembrane ProteinsMolecular Sequence DataPhosphoproteinsProtein BindingCalcium-Binding ProteinsClathrinEps15 protein, ratIntracellular Signaling Peptides and ProteinsLigandsMembrane ProteinsPhosphoproteinsVesicular Transport Proteins

Identifiers

PMID18200045
PMCPMC2241652
OpenAlexW2170941672

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.