Evidence map›Paper›PMID 34083810›Full record

ArticleNature chemical biology2021

Differential regulation of single microtubules and bundles by a three-protein module.

Nandini Mani, Shuo Jiang, Alex E Neary, Sithara S Wijeratne, Radhika Subramanian

Open access · greenAbstract read
In one paragraph

Article in Nature chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.2field-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

10 citing papers in PubMed, 16 citations in OpenAlex.

  1. Review
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  7. Coupling of microtubule bundles isolates them from local disruptions to set the structural stability of the anaphase spindle.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
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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

5 authors at 2 institutions in 1 country.

Nandini Mani *Department of Molecular Biology, Massachusetts General Hospital, Boston, MA, USA.ORCID http://orcid.org/0000-0002-2025-9103
Shuo Jiang *Department of Molecular Biology, Massachusetts General Hospital, Boston, MA, USA.
Alex E NearyDepartment of Molecular Biology, Massachusetts General Hospital, Boston, MA, USA.
Sithara S WijeratneDepartment of Molecular Biology, Massachusetts General Hospital, Boston, MA, USA.
Radhika SubramanianDepartment of Molecular Biology, Massachusetts General Hospital, Boston, MA, USA. radhika@molbio.mgh.harvard.edu.ORCID http://orcid.org/0000-0002-3011-9403
Harvard University · USMassachusetts General Hospital · US

Funding

A versatile platform for reconstructing the spatial organization of intracellular signaling during cell-divisionDP2GM126894 · NIGMS · MASSACHUSETTS GENERAL HOSPITAL · PI SUBRAMANIAN, RADHIKA · 2017 to 2017
$2.6M
Asymmetric flow FFF and Composition Gradient/Light Scattering SystemS10RR023748 · NCRR · YALE UNIVERSITY · PI FOLTA-STOGNIEW, EWA JOANNA · 2007 to 2007
$271k
NCRR NIH HHS S10 RR023748NIGMS NIH HHS DP2 GM126894
6 · The paper itself

Abstract

A remarkable feature of the microtubule cytoskeleton is the coexistence of subpopulations having different dynamic properties. A prominent example is the anaphase spindle, where stable antiparallel bundles exist alongside dynamic microtubules and provide spatial cues for cytokinesis. How are the dynamics of spatially proximal arrays differentially regulated? We reconstitute a minimal system of three midzone proteins: microtubule-crosslinker PRC1 and its interactors CLASP1 and Kif4A, proteins that promote and suppress microtubule elongation, respectively. We find that their collective activity promotes elongation of single microtubules while simultaneously stalling polymerization of crosslinked bundles. This differentiation arises from (1) strong rescue activity of CLASP1, which overcomes the weaker effects of Kif4A on single microtubules, and (2) lower microtubule- and PRC1-binding affinity of CLASP1, which permits the dominance of Kif4A at overlaps. In addition to canonical mechanisms where antagonistic regulators set microtubule length, our findings illuminate design principles by which collective regulator activity creates microenvironments of arrays with distinct dynamic properties.

Indexed as

Cell Cycle ProteinsHumansKinesinsMicrotubule-Associated ProteinsMicrotubulesCell Cycle ProteinsCLASP1 protein, humanKIF4A protein, humanKinesinsMicrotubule-Associated ProteinsPRC1 protein, human

Identifiers

PMID34083810
PMCPMC8387365
OpenAlexW3164049161

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.