Evidence map›Paper›PMID 15616574›Full record

ArticleThe EMBO journal2005

Structural insights into the EB1-APC interaction.

Srinivas Honnappa, Corinne M John, Dirk Kostrewa, Fritz K Winkler, Michel O Steinmetz

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 72 papers.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

72 citing papers in PubMed, 148 citations in OpenAlex.

  1. Review
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  7. MAPping tubulin mutations.Frontiers in cell and developmental biology · 2023
    Review
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12 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Srinivas HonnappaBiomolecular Research, Structural Biology, Paul Scherrer Institut, Villigen PSI, Switzerland.
Corinne M John
Dirk Kostrewa
Fritz K Winkler
Michel O Steinmetz
Paul Scherrer Institute · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

EB1 proteins bind to microtubule ends where they act in concert with other components, including the adenomatous polyposis coli (APC) tumor suppressor, to regulate the microtubule filament system. We find that EB1 is a stable dimer with a parallel coiled coil and show that dimerization is essential for the formation of its C-terminal domain (EB1-C). The crystal structure of EB1-C reveals a highly conserved surface patch with a deep hydrophobic cavity at its center. EB1-C binds two copies of an APC-derived C-terminal peptide (C-APCp1) with equal 5 microM affinity. The conserved APC Ile2805-Pro2806 sequence motif serves as an anchor for the interaction of C-APCp1 with the hydrophobic cavity of EB1-C. Phosphorylation of the conserved Cdc2 site Ser2789-Lys2792 in C-APCp1 reduces binding four-fold, indicating that the interaction APC-EB1 is post-translationally regulated in cells. Our findings provide a basis for understanding the dynamic crosstalk of EB1 proteins with their molecular targets in eukaryotic organisms.

Indexed as

Amino Acid SequenceCrystallographyEscherichia coli ProteinsModels, MolecularMolecular Sequence DataPhosphorylationPlasmidsProtein BindingProtein ConformationSequence Homology, Amino AcidEscherichia coli Proteins

Identifiers

PMID15616574
PMCPMC545816
OpenAlexW2155289420

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.