Evidence map›Paper›PMID 27493215›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Near-atomic cryo-EM structure of PRC1 bound to the microtubule.

Elizabeth H Kellogg, Stuart Howes, Shih-Chieh Ti, Erney Ramírez-Aportela, Tarun M Kapoor, Pablo Chacón, Eva Nogales

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
6.8field-weighted citation impact, top 3% 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

47 citing papers in PubMed, 82 citations in OpenAlex.

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  20. Comprehensive Analysis of Binding Sites in Tubulin.Angewandte Chemie (International ed. in English) · 2021
    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

7 authors at 3 institutions in 2 countries.

Elizabeth H KelloggMolecular Biophysics and Integrative Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720; Howard Hughes Medical Institute, University of California, Berkeley, CA 94720;
Stuart HowesBiophysics Graduate Group, University of California, Berkeley, CA 94720;
Shih-Chieh TiLaboratory of Chemistry and Cell Biology, The Rockefeller University, New York, NY 10065;
Erney Ramírez-AportelaDepartment of Biological Physical Chemistry, Rocasolano Physical Chemistry Institute, Consejo Superior de Investigaciones Científicas, Madrid 28006, Spain;
Tarun M KapoorLaboratory of Chemistry and Cell Biology, The Rockefeller University, New York, NY 10065;
Pablo ChacónDepartment of Biological Physical Chemistry, Rocasolano Physical Chemistry Institute, Consejo Superior de Investigaciones Científicas, Madrid 28006, Spain;
Eva NogalesMolecular Biophysics and Integrative Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720; Howard Hughes Medical Institute, University of California, Berkeley, CA 94720; California Institute for Quantitative Biosciences, University of California, Berkeley, CA 94720; Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720 enogales@lbl.gov.
University of California, Berkeley · USInstituto de Química Física Blas Cabrera · ESRockefeller University · US

Funding

TUBULIN STRUCTURE BY ELECTRON CRYSTALLOGRAPHYP01GM051487 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI CATE, JAMIE H · 1994 to 2018
$27.6M
MOLECULAR BIOPHYSICS TRAINING GRANTT32GM008295 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI HURLEY, JAMES H, WEMMER, DAVID E · 1989 to 2022
$8.1M
Motor Protein Dynamics and Mitotic MechanismsR01GM065933 · NIGMS · ROCKEFELLER UNIVERSITY · PI KAPOOR, TARUN M. · 2002 to 2018
$6.7M
NIGMS NIH HHS P01 GM051487NIGMS NIH HHS R01 GM065933NIGMS NIH HHS T32 GM008295
6 · The paper itself

Abstract

Proteins that associate with microtubules (MTs) are crucial to generate MT arrays and establish different cellular architectures. One example is PRC1 (protein regulator of cytokinesis 1), which cross-links antiparallel MTs and is essential for the completion of mitosis and cytokinesis. Here we describe a 4-Å-resolution cryo-EM structure of monomeric PRC1 bound to MTs. Residues in the spectrin domain of PRC1 contacting the MT are highly conserved and interact with the same pocket recognized by kinesin. We additionally found that PRC1 promotes MT assembly even in the presence of the MT stabilizer taxol. Interestingly, the angle of the spectrin domain on the MT surface corresponds to the previously observed cross-bridge angle between MTs cross-linked by full-length, dimeric PRC1. This finding, together with molecular dynamic simulations describing the intrinsic flexibility of PRC1, suggests that the MT-spectrin domain interface determines the geometry of the MT arrays cross-linked by PRC1.

Indexed as

Amino Acid MotifsAnimalsBinding SitesCell Cycle ProteinsCryoelectron MicroscopyCrystallography, X-RayGene ExpressionHumansKinesinsMicrotubulesMolecular Dynamics SimulationPaclitaxelProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein Interaction Domains and MotifsCell Cycle ProteinsKinesinsPaclitaxelPRC1 protein, humanProtein SubunitsRecombinant ProteinsTubulinTubulin Modulatorscryo-EMcytoskeletonMAPsmicrotubulesPRC1

Identifiers

PMID27493215
PMCPMC5003279
OpenAlexW2495930560

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.