Evidence map›Paper›PMID 28978447›Full record

ArticleBiophysical journal2017

Acetylated Microtubules Are Preferentially Bundled Leading to Enhanced Kinesin-1 Motility.

Linda Balabanian, Christopher L Berger, Adam G Hendricks

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
4.0field-weighted citation impact, top 5% 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

67 citing papers in PubMed, 108 citations in OpenAlex.

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  13. Luminal acetylation of microtubules is not essential forMicrobial cell (Graz, Austria) · 2025
    Article
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7 more citing papers are in PubMed but not listed here.

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

3 authors at 2 institutions in 2 countries.

Linda BalabanianDepartment of Bioengineering, McGill University, Montreal, Québec, Canada.
Christopher L BergerDepartment of Molecular Physiology and Biophysics, University of Vermont, Burlington, Vermont.
Adam G HendricksDepartment of Bioengineering, McGill University, Montreal, Québec, Canada. Electronic address: adam.hendricks@mcgill.ca.
McGill University · CAUniversity of Vermont · US

Funding

Tau-mediated regulation of axonal transportR01GM101066 · NIGMS · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI BERGER, CHRISTOPHER L. · 2013 to 2016
$1.6M
NIGMS NIH HHS R01 GM101066
6 · The paper itself

Abstract

The motor proteins kinesin and dynein transport organelles, mRNA, proteins, and signaling molecules along the microtubule cytoskeleton. In addition to serving as tracks for transport, the microtubule cytoskeleton directs intracellular trafficking by regulating the activity of motor proteins through the organization of the filament network, microtubule-associated proteins, and tubulin posttranslational modifications. However, it is not well understood how these factors influence motor motility, and in vitro assays and live cell observations often produce disparate results. To systematically examine the factors that contribute to cytoskeleton-based regulation of motor protein motility, we extracted intact microtubule networks from cells and tracked the motility of single fluorescently labeled motor proteins on these cytoskeletons. We find that tubulin acetylation alone does not directly affect kinesin-1 motility. However, acetylated microtubules are predominantly bundled, and bundling enhances kinesin run lengths and provides a greater number of available kinesin binding sites. The neuronal MAP tau is also not sensitive to tubulin acetylation, but enriches preferentially on highly curved regions of microtubules where it strongly inhibits kinesin motility. Taken together, these results suggest that the organization of the microtubule network is a key contributor to the regulation of motor-based transport.

Indexed as

AcetylationAnimalsChlorocebus aethiopsCOS CellsEscherichia coliKinesinsMicrotubulesProtein TransportRatsRecombinant Proteinstau ProteinsTubulinKinesinsRecombinant Proteinstau ProteinsTubulin

Identifiers

PMID28978447
PMCPMC5627185
OpenAlexW2762659278

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.