Evidence map›Paper›PMID 28287156›Full record

ArticleScientific reports2017

Single Molecule Investigation of Kinesin-1 Motility Using Engineered Microtubule Defects.

Michael W Gramlich, Leslie Conway, Winnie H Liang, Joelle A Labastide, Stephen J King, Jing Xu, Jennifer L Ross

Abstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
–field-weighted citation impact
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

14 citing papers in PubMed.

  1. Review
  2. Cholesterol in the cargo membrane amplifies tau inhibition of kinesin-1-based transport.Proceedings of the National Academy of Sciences of the United States of America · 2023
    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

7 authors.

Michael W GramlichDepartment of Physics, University of Massachusetts Amherst, Amherst, MA 01003, USA.
Leslie ConwayMolecular and Cellular Biology Graduate Program, University of Massachusetts Amherst, Amherst, MA 01003, USA.
Winnie H LiangDepartment of Physics, University of California Merced, Merced, CA 95343, USA.
Joelle A LabastideDepartment of Physics, University of Massachusetts Amherst, Amherst, MA 01003, USA.
Stephen J KingBurnett School of Biomedical Sciences, University of Central Florida, Orlando, FL 32827, USA.
Jing XuDepartment of Physics, University of California Merced, Merced, CA 95343, USA.
Jennifer L RossDepartment of Physics, University of Massachusetts Amherst, Amherst, MA 01003, USA.

Funding

Dynactin/microtubule interactions in dynein motilityR01NS048501 · NINDS · UNIVERSITY OF MISSOURI KANSAS CITY · PI KING, STEPHEN J · 2004 to 2014
$2.9M
Do Cargo Membrane Fluidity and Microdomain Formation Impact Motor Protein-Based Motility?R15GM120682 · NIGMS · UNIVERSITY OF CALIFORNIA, MERCED · PI XU, JING · 2016 to 2024
$1.4M
Cellular Remodeling by Microtubule SeveringR01GM109909 · NIGMS · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI ROSS, JENNIFER L, SHARP, DAVID JAMES · 2014 to 2017
$1.2M
NIGMS NIH HHS R01 GM109909NIGMS NIH HHS R15 GM120682NINDS NIH HHS R01 NS048501
6 · The paper itself

Abstract

The structure of the microtubule is tightly regulated in cells via a number of microtubule associated proteins and enzymes. Microtubules accumulate structural defects during polymerization, and defect size can further increase under mechanical stresses. Intriguingly, microtubule defects have been shown to be targeted for removal via severing enzymes or self-repair. The cell's control in defect removal suggests that defects can impact microtubule-based processes, including molecular motor-based intracellular transport. We previously demonstrated that microtubule defects influence cargo transport by multiple kinesin motors. However, mechanistic investigations of the observed effects remained challenging, since defects occur randomly during polymerization and are not directly observable in current motility assays. To overcome this challenge, we used end-to-end annealing to generate defects that are directly observable using standard epi-fluorescence microscopy. We demonstrate that the annealed sites recapitulate the effects of polymerization-derived defects on multiple-motor transport, and thus represent a simple and appropriate model for naturally-occurring defects. We found that single kinesins undergo premature dissociation, but not preferential pausing, at the annealed sites. Our findings provide the first mechanistic insight to how defects impact kinesin-based transport. Preferential dissociation on the single-molecule level has the potential to impair cargo delivery at locations of microtubule defect sites in vivo.

Indexed as

Computer SimulationModels, TheoreticalAnimalsBiological TransportBrainCattleKinesinsMicroscopy, FluorescenceMicrotubulesPolymerizationSwineTubulinKinesinsTubulin

Identifiers

PMID28287156
PMCPMC5347089

What OpenQuestion holds

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LicenceCC BY
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.