Evidence map›Paper›PMID 28636917›Full record

ArticleBiophysical journal2017

Kinesin Processivity Is Determined by a Kinetic Race from a Vulnerable One-Head-Bound State.

Keith J Mickolajczyk, William O Hancock

Abstract 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 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing 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

30 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Volumetric Single-Molecule Tracking Inside Subcellular Structures.Small (Weinheim an der Bergstrasse, Germany) · 2026
    Article
  5. Review
  6. Article
  7. Dissecting the pH Sensitivity of Kinesin-Driven Transport.The journal of physical chemistry. B · 2024
    Article
  8. Article
  9. Article
  10. Motor guidance by long-range communication on the microtubule highway.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Backstepping Mechanism of Kinesin-1.Biophysical journal · 2020
    Article
  16. Article
  17. The mechanochemistry of the kinesin-2 KIF3AC heterodimer is related to strain-dependent kinetic properties of KIF3A and KIF3C.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors.

Keith J MickolajczykDepartment of Biomedical Engineering, Penn State University, University Park, Pennsylvania; Intercollege Graduate Degree Program in Bioengineering, Penn State University, University Park, Pennsylvania.
William O HancockDepartment of Biomedical Engineering, Penn State University, University Park, Pennsylvania; Intercollege Graduate Degree Program in Bioengineering, Penn State University, University Park, Pennsylvania. Electronic address: wohbio@engr.psu.edu.

Funding

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

Abstract

Kinesin processivity, defined as the average number of steps that occur per interaction with a microtubule, is an important biophysical determinant of the motor's intracellular capabilities. Despite its fundamental importance to the diversity of tasks that kinesins carry out in cells, no existing quantitative model fully explains how structural differences between kinesins alter kinetic rates in the ATPase cycle to produce functional changes in processivity. Here we use high-resolution single-molecule microscopy to directly observe the stepping behavior of kinesin-1 and -2 family motors with different length neck-linker domains. We characterize a one-head-bound posthydrolysis vulnerable state where a kinetic race occurs between attachment of the tethered head to its next binding site and detachment of the bound head from the microtubule. We find that greater processivity is correlated with faster attachment of the tethered head from this vulnerable state. In compliment, we show that slowing detachment from this vulnerable state by strengthening motor-microtubule electrostatic interactions also increases processivity. Furthermore, we provide evidence that attachment of the tethered head is irreversible, suggesting a first passage model for exit from the vulnerable state. Overall, our results provide a kinetic framework for explaining kinesin processivity and for mapping structural differences to functional differences in diverse kinesin isoforms.

Indexed as

Adenosine DiphosphateAdenosine TriphosphatasesAdenosine TriphosphateAnimalsBinding SitesDrosophilaDrosophila ProteinsEscherichia coliHumansHydrolysisKinesinsKineticsMicrotubulesModels, MolecularProtein BindingSingle Molecule ImagingAdenosine DiphosphateAdenosine TriphosphatasesAdenosine TriphosphateDrosophila ProteinsKhc protein, DrosophilaKIF2A protein, humanKinesinsSolvents

Identifiers

PMID28636917
PMCPMC5479115

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.