Skip to content Skip to navigation
University of Warwick
  • Study
  • |
  • Research
  • |
  • Business
  • |
  • Alumni
  • |
  • News
  • |
  • About

University of Warwick
Publications service & WRAP

Highlight your research

  • WRAP
    • Home
    • Search WRAP
    • Browse by Warwick Author
    • Browse WRAP by Year
    • Browse WRAP by Subject
    • Browse WRAP by Department
    • Browse WRAP by Funder
    • Browse Theses by Department
  • Publications Service
    • Home
    • Search Publications Service
    • Browse by Warwick Author
    • Browse Publications service by Year
    • Browse Publications service by Subject
    • Browse Publications service by Department
    • Browse Publications service by Funder
  • Help & Advice
University of Warwick

The Library

  • Login
  • Admin

Electrostatically biased binding of kinesin to microtubules

Tools
- Tools
+ Tools

Grant, Barry J., Gheorghe, Dana M., Zheng, Wenjun, Alonso, M. (Maria), Huber, Gary, Dlugosz, Maciej, McCammon, J. Andrew and Cross, R. A. (2011) Electrostatically biased binding of kinesin to microtubules. PLoS Biology, Vol.9 (No.11). e1001207. doi:10.1371/journal.pbio.1001207 ISSN 1545-7885.

[img]
Preview
PDF
WRAP_Georghe_ournal.pbio.1001207.pdf - Published Version - Requires a PDF viewer.

Download (714Kb)
Official URL: http://dx.doi.org/10.1371/journal.pbio.1001207

Request Changes to record.

Abstract

The minimum motor domain of kinesin-1 is a single head. Recent evidence suggests that such minimal motor domains generate force by a biased binding mechanism, in which they preferentially select binding sites on the microtubule that lie ahead in the progress direction of the motor. A specific molecular mechanism for biased binding has, however, so far been lacking. Here we use atomistic Brownian dynamics simulations combined with experimental mutagenesis to show that incoming kinesin heads undergo electrostatically guided diffusion-to-capture by microtubules, and that this produces directionally biased binding. Kinesin-1 heads are initially rotated by the electrostatic field so that their tubulin-binding sites face inwards, and then steered towards a plus-endwards binding site. In tethered kinesin dimers, this bias is amplified. A 3-residue sequence (RAK) in kinesin helix alpha-6 is predicted to be important for electrostatic guidance. Real-world mutagenesis of this sequence powerfully influences kinesin-driven microtubule sliding, with one mutant producing a 5-fold acceleration over wild type. We conclude that electrostatic interactions play an important role in the kinesin stepping mechanism, by biasing the diffusional association of kinesin with microtubules.

Item Type: Journal Article
Subjects: Q Science > QP Physiology
Divisions: Faculty of Science, Engineering and Medicine > Medicine > Warwick Medical School
Library of Congress Subject Headings (LCSH): Kinesin -- Movements
Journal or Publication Title: PLoS Biology
Publisher: Public Library of Science
ISSN: 1545-7885
Official Date: November 2011
Dates:
DateEvent
November 2011Published
Volume: Vol.9
Number: No.11
Page Range: e1001207
DOI: 10.1371/journal.pbio.1001207
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Open Access (Creative Commons)
Date of first compliant deposit: 18 December 2015
Date of first compliant Open Access: 18 December 2015

Request changes or add full text files to a record

Repository staff actions (login required)

View Item View Item

Downloads

Downloads per month over past year

View more statistics

twitter

Email us: wrap@warwick.ac.uk
Contact Details
About Us