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

The kinesin-12 Kif15 is a processive track-switching tetramer

Tools
- Tools
+ Tools

Drechsler, Hauke, McHugh, Toni, Singleton, Martin R., Carter, Nicholas J. and McAinsh, Andrew D. (2014) The kinesin-12 Kif15 is a processive track-switching tetramer. eLife, Volume 3 . Article number e01724. doi:10.7554/eLife.01724 ISSN 2050-084X.

[img]
Preview
PDF
WRAP_Drechsler_elife01724.pdf - Published Version - Requires a PDF viewer.
Available under License Creative Commons Attribution.

Download (5Mb) | Preview
Official URL: http://dx.doi.org/10.7554/eLife.01724

Request Changes to record.

Abstract

Kinesin-12 motors are a little studied branch of the kinesin superfamily with the human protein (Kif15) implicated in spindle mechanics and chromosome movement. In this study, we reconstitute full-length hKif15 and its microtubule-targeting factor hTpx2 in vitro to gain insight into the motors mode of operation. We reveal that hKif15 is a plus-end-directed processive homotetramer that can step against loads of up to 3.5 pN. We further show that hKif15 is the first kinesin that effectively switches microtubule tracks at intersections, enabling it to navigate microtubule networks, such as the spindle. hKif15 tetramers are also capable of cross-linking microtubules, but unexpectedly, this does not depend on hTpx2. Instead, we find that hTpx2 inhibits hKif15 stepping when microtubule-bound. Our data reveal that hKif15 is a second tetrameric spindle motor in addition to the kinesin-5 Eg5 and provides insight into the mechanisms by which hKif15 and its inhibitor hTpx2 modulate spindle microtubule architecture.

Item Type: Journal Article
Subjects: Q Science > QP Physiology
Divisions: Faculty of Science, Engineering and Medicine > Medicine > Warwick Medical School > Biomedical Sciences > Cell & Developmental Biology
Faculty of Science, Engineering and Medicine > Medicine > Warwick Medical School
Library of Congress Subject Headings (LCSH): Kinesin, Spindle (Cell division)
Journal or Publication Title: eLife
Publisher: eLife Sciences Publications Ltd.
ISSN: 2050-084X
Official Date: 25 March 2014
Dates:
DateEvent
25 March 2014Published
20 February 2014Accepted
16 October 2013Submitted
Volume: Volume 3
Article Number: Article number e01724
DOI: 10.7554/eLife.01724
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Open Access (Creative Commons)
Date of first compliant deposit: 28 December 2015
Date of first compliant Open Access: 28 December 2015
Funder: Marie Curie Cancer Care, Warwick Medical School
Adapted As:

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