The family-specific α4-helix of the kinesin-13, MCAK, is critical to microtubule end recognition

Patel, Jennifer T. and Belsham, Hannah R. and Rathbone, Alexandra J. and Wickstead, Bill and Gell, Christopher and Friel, Claire T. (2016) The family-specific α4-helix of the kinesin-13, MCAK, is critical to microtubule end recognition. Open Biology, 6 (10). p. 160223. ISSN 2046-2441

PDF - Requires a PDF viewer such as GSview, Xpdf or Adobe Acrobat Reader
Available under Licence Creative Commons Attribution.
Download (852kB) | Preview


Kinesins that influence the dynamics of microtubule growth and shrinkage require the ability to distinguish between the microtubule end and the microtubule lattice. The microtubule depolymerizing kinesin MCAK has been shown to specifically recognize the microtubule end. This ability is key to the action of MCAK in regulating microtubule dynamics. We show that the a4-helix of the motor domain is crucial to microtubule end recognition. Mutation of the residues K524, E525 and R528, which are located in the C-terminal half of the a4-helix, specifically disrupts the ability of MCAK to recognize the microtubule end. Mutation of these residues, which are conserved in the kinesin-13 family and discriminate members of this family from translocating kinesins, impairs the ability of MCAK to discriminate between the microtubule lattice and the microtubule end.

Item Type: Article
Keywords: MCAK; kinesin-13; microtubule; depolymerization; ATP turnover; microtubule end recognition
Schools/Departments: University of Nottingham, UK > Faculty of Medicine and Health Sciences > School of Life Sciences
Identification Number:
Depositing User: Eprints, Support
Date Deposited: 17 Oct 2016 12:55
Last Modified: 14 Oct 2017 19:52

Actions (Archive Staff Only)

Edit View Edit View