Evidence map›Paper›PMID 21079666›Full record

ArticlePLoS computational biology2010

Monte Carlo analysis of neck linker extension in kinesin molecular motors.

Matthew L Kutys, John Fricks, William O Hancock

Open access · goldAbstract read
In one paragraph

Article in PLoS computational biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.3field-weighted citation impact, top 22% 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

18 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Article
  3. ADP release can explain spatially-dependent kinesin binding times.bioRxiv : the preprint server for biology · 2023
    Article
  4. Article
  5. Long-range intramolecular allostery and regulation in the dynein-like AAA protein Mdn1.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  6. Article
  7. Article
  8. Article
  9. Parsing the roles of neck-linker docking and tethered head diffusion in the stepping dynamics of kinesin.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Estimating Velocity for Processive Motor Proteins with Random Detachment.Journal of agricultural, biological, and environmental statistics · 2013
    Article
  15. Article
  16. Article
  17. Article
  18. Interhead tension determines processivity across diverse N-terminal kinesins.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
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 1 institution in 1 country.

Matthew L KutysDepartment of Bioengineering, The Pennsylvania State University, University Park, Pennsylvania, United States of America.
John Fricks
William O Hancock
Pennsylvania State University · US

Funding

Molecular mechanism of kinesin motilityR01GM076476 · NIGMS · PENNSYLVANIA STATE UNIVERSITY, THE · PI HANCOCK, WILLIAM OLAF · 2006 to 2019
$3.5M
NIGMS NIH HHS R01 GM076476NIGMS NIH HHS R01-GM076476
6 · The paper itself

Abstract

Kinesin stepping is thought to involve both concerted conformational changes and diffusive movement, but the relative roles played by these two processes are not clear. The neck linker docking model is widely accepted in the field, but the remainder of the step--diffusion of the tethered head to the next binding site--is often assumed to occur rapidly with little mechanical resistance. Here, we investigate the effect of tethering by the neck linker on the diffusive movement of the kinesin head, and focus on the predicted behavior of motors with naturally or artificially extended neck linker domains. The kinesin chemomechanical cycle was modeled using a discrete-state Markov chain to describe chemical transitions. Brownian dynamics were used to model the tethered diffusion of the free head, incorporating resistive forces from the neck linker and a position-dependent microtubule binding rate. The Brownian dynamics and chemomechanical cycle were coupled to model processive runs consisting of many 8 nm steps. Three mechanical models of the neck linker were investigated: Constant Stiffness (a simple spring), Increasing Stiffness (analogous to a Worm-Like Chain), and Reflecting (negligible stiffness up to a limiting contour length). Motor velocities and run lengths from simulated paths were compared to experimental results from Kinesin-1 and a mutant containing an extended neck linker domain. When tethered by an increasingly stiff spring, the head is predicted to spend an unrealistically short amount of time within the binding zone, and extending the neck is predicted to increase both the velocity and processivity, contrary to experiments. These results suggest that the Worm-Like Chain is not an adequate model for the flexible neck linker domain. The model can be reconciled with experimental data if the neck linker is either much more compliant or much stiffer than generally assumed, or if weak kinesin-microtubule interactions stabilize the diffusing head near its binding site.

Indexed as

Molecular Dynamics SimulationMonte Carlo MethodComputational BiologyElasticityFrictionKinesinsThermodynamicsTubulinKinesinsTubulin

Identifiers

PMID21079666
PMCPMC2973807
OpenAlexW2049954074

What OpenQuestion holds

Textmetadata
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.