Evidence map›Paper›PMID 25418170›Full record

ArticleBiophysical journal2014

Transport by populations of fast and slow kinesins uncovers novel family-dependent motor characteristics important for in vivo function.

Göker Arpağ, Shankar Shastry, William O Hancock, Erkan Tüzel

Erratum issuedAbstract read
In one paragraph

Article in Biophysical journal, 2014. 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 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing 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

52 citing papers in PubMed.

  1. Article
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  6. Review
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  8. Fluorogenic RNA-based biomaterials for imaging and tracking the cargo of extracellular vesicles.Journal of controlled release : official journal of the Controlled Release Society · 2024
    Article
  9. Article
  10. KIF1A is kinetically tuned to be a superengaging motor under hindering loads.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors.

Göker ArpağDepartment of Physics, Worcester Polytechnic Institute, Worcester, Massachusetts.
Shankar ShastryDepartment of Biomedical Engineering, The Pennsylvania State University, University Park, Pennsylvania.
William O HancockDepartment of Biomedical Engineering, The Pennsylvania State University, University Park, Pennsylvania. Electronic address: wohbio@engr.psu.edu.
Erkan TüzelDepartment of Physics, Worcester Polytechnic Institute, Worcester, Massachusetts. Electronic address: tuzel@mailaps.org.

Funding

Molecular mechanism of kinesin motilityR01GM076476 · NIGMS · PENNSYLVANIA STATE UNIVERSITY, THE · PI HANCOCK, WILLIAM OLAF · 2006 to 2019
$3.5M
Kinesin and +TIP-based microtubule steeringR01GM100076 · NIGMS · PENNSYLVANIA STATE UNIVERSITY, THE · PI HANCOCK, WILLIAM OLAF · 2012 to 2015
$1.7M
NIGMS NIH HHS R01 GM076476NIGMS NIH HHS R01GM076476NIGMS NIH HHS R01 GM100076NIGMS NIH HHS R01GM100076
6 · The paper itself

Abstract

Intracellular cargo transport frequently involves multiple motor types, either having opposite directionality or having the same directionality but different speeds. Although significant progress has been made in characterizing kinesin motors at the single-molecule level, predicting their ensemble behavior is challenging and requires tight coupling between experiments and modeling to uncover the underlying motor behavior. To understand how diverse kinesins attached to the same cargo coordinate their movement, we carried out microtubule gliding assays using pairwise mixtures of motors from the kinesin-1, -2, -3, -5, and -7 families engineered to have identical run lengths and surface attachments. Uniform motor densities were used and microtubule gliding speeds were measured for varying proportions of fast and slow motors. A coarse-grained computational model of gliding assays was developed and found to recapitulate the experiments. Simulations incorporated published force-dependent velocities and run lengths, along with mechanical interactions between motors bound to the same microtubule. The simulations show that the force-dependence of detachment is the key parameter that determines gliding speed in multimotor assays, while motor compliance, surface density, and stall force all play minimal roles. Simulations also provide estimates for force-dependent dissociation rates, suggesting that kinesin-1 and the mitotic motors kinesin-5 and -7 maintain microtubule association against loads, whereas kinesin-2 and -3 readily detach. This work uncovers unexpected motor behavior in multimotor ensembles and clarifies functional differences between kinesins that carry out distinct mechanical tasks in cells.

Indexed as

AnimalsDrosophilaKinesinsKineticsMiceMicrotubulesMolecular Dynamics SimulationXenopusKinesins

Identifiers

PMID25418170
PMCPMC4213720

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.