Evidence map›Paper›PMID 26854759›Full record

ArticleJournal of molecular biology2016

Interactions between the Microtubule Binding Protein EB1 and F-Actin.

Emily O Alberico, Zhiqing C Zhu, Yueh-Fu O Wu, Melissa K Gardner, Dave R Kovar, Holly V Goodson

Abstract read
In one paragraph

Article in Journal of molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.9field-weighted citation impact, top 17% 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

15 citing papers in PubMed, 33 citations in OpenAlex.

  1. Review
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  10. Article
  11. Microtubules in cell migration.Essays in biochemistry · 2019
    Review
  12. Article
  13. Article
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  15. 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

6 authors at 3 institutions in 1 country.

Emily O AlbericoDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN, 46556, USA.
Zhiqing C ZhuDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN, 46556, USA.
Yueh-Fu O WuDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN, 46556, USA.
Melissa K GardnerDepartment of Genetics, Cell Biology, and Development, University of Minnesota, Minneapolis, MN, 55455, USA.
Dave R KovarDepartment of Molecular Genetics and Cell Biology, The University of Chicago, Chicago, IL, 60637, USA.
Holly V GoodsonDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN, 46556, USA. Electronic address: hgoodson@nd.edu.
University of Notre Dame · USUniversity of Chicago · USUniversity of Minnesota · US

Funding

Quantitative Analysis and Modeling of Microtubule Structure and RegulationR01GM103833 · NIGMS · UNIVERSITY OF MINNESOTA · PI GARDNER, MELISSA · 2013 to 2017
$1.4M
NIGMS NIH HHS R01 GM103833
6 · The paper itself

Abstract

Many cellular processes including cell division and cell migration require coordination between the actin and microtubule (MT) cytoskeletons. This coordination is as-yet poorly understood, but proteins such as formins and IQGAP1 are known to be involved. We show that the MT binding protein EB1 (end-binding protein 1), a key regulator of MT dynamics, can bind directly to filamentous actin (F-actin) F-actin. We determined that the EB1:F-actin interaction is salt sensitive and weak under physiological salt concentrations but might be relevant in contexts where the local concentration of actin is high. Using bioinformatics and mutagenesis, we found that the EB1:F-actin binding site partially overlaps the well-characterized EB1:MT binding interface. Congruently, competition experiments indicate that EB1 can bind to F-actin or MTs but not both simultaneously. These observations suggest that EB1:F-actin interactions may negatively regulate EB1:MT interactions, and we speculate that this interaction may assist cells in differentially regulating MT stability in the actin-rich cortex as opposed to the cell interior.

Indexed as

ActinsAmino Acid SequenceAnimalsBinding SitesComputational BiologyDNA Mutational AnalysisHumansMicrotubule-Associated ProteinsModels, MolecularMolecular Sequence DataProtein BindingProtein Interaction MappingSequence AlignmentActinsMAPRE1 protein, humanMicrotubule-Associated ProteinsactincytoskeletonEB1microtubulesplus-end tracking protein

Identifiers

PMID26854759
PMCPMC4834876
OpenAlexW2255956841

What OpenQuestion holds

Textmetadata
LicenceTDM
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.