Evidence map›Paper›PMID 27653487›Full record

ArticleBiophysical journal2016

The Effect of Temperature on Microtubule-Based Transport by Cytoplasmic Dynein and Kinesin-1 Motors.

Weili Hong, Anjneya Takshak, Olaolu Osunbayo, Ambarish Kunwar, Michael Vershinin

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2016. 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 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.1field-weighted citation impact, top 15% 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

17 citing papers in PubMed, 36 citations in OpenAlex.

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  12. Temperature-dependent activity of kinesins is regulable.Biochemical and biophysical research communications · 2020
    Article
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  14. Article
  15. Review
  16. Effect of fuel concentration and force on collective transport by a team of dynein motors.Protein science : a publication of the Protein Society · 2017
    Article
  17. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 2 countries.

Weili HongDepartment of Physics & Astronomy, University of Utah, Salt Lake City, Utah.
Anjneya TakshakDepartment of Biosciences and Bioengineering, Indian Institute of Technology Bombay, Powai, Mumbai, Maharashtra, India.
Olaolu OsunbayoDepartment of Biology, University of Utah, Salt Lake City, Utah.
Ambarish KunwarDepartment of Biosciences and Bioengineering, Indian Institute of Technology Bombay, Powai, Mumbai, Maharashtra, India.
Michael VershininDepartment of Physics & Astronomy, University of Utah, Salt Lake City, Utah; Department of Biology, University of Utah, Salt Lake City, Utah. Electronic address: vershinin@physics.utah.edu.
University of Utah · USIndian Institute of Technology Bombay · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cytoplasmic dynein and kinesin are both microtubule-based molecular motors but are structurally and evolutionarily unrelated. Under standard conditions, both move with comparable unloaded velocities toward either the microtubule minus (dynein) or plus (most kinesins) end. This similarity is important because it is often implicitly incorporated into models that examine the balance of cargo fluxes in cells and into models of the bidirectional motility of individual cargos. We examined whether this similarity is a robust feature, and specifically whether it persists across the biologically relevant temperature range. The velocity of mammalian cytoplasmic dynein, but not of mammalian kinesin-1, exhibited a break from simple Arrhenius behavior below 15°C-just above the restrictive temperature of mammalian fast axonal transport. In contrast, the velocity of yeast cytoplasmic dynein showed a break from Arrhenius behavior at a lower temperature (∼8°C). Our studies implicate cytoplasmic dynein as a more thermally tunable motor and therefore a potential thermal regulator of microtubule-based transport. Our theoretical analysis further suggests that motor velocity changes can lead to qualitative changes in individual cargo motion and hence net intracellular cargo fluxes. We propose that temperature can potentially be used as a noninvasive probe of intracellular transport.

Indexed as

Biological TransportTemperatureAnimalsComputer SimulationCytoplasmic DyneinsKinesinsModels, MolecularOptical TweezersRatsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsStochastic ProcessesCytoplasmic DyneinsKinesinsSaccharomyces cerevisiae Proteins

Identifiers

PMID27653487
PMCPMC5034348
OpenAlexW2522580113

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.