2. Academic Validation
  3. The family-specific α4-helix of the kinesin-13, MCAK, is critical to microtubule end recognition

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

  • Open Biol. 2016 Oct;6(10):160223. doi: 10.1098/rsob.160223.
Jennifer T Patel 1,  Hannah R Belsham 1,  Alexandra J Rathbone 1,  Bill Wickstead 1,  Christopher Gell 1,  Claire T Friel 2
Affiliations

Affiliations

  • 1 School of Life Sciences, University of Nottingham, Medical School, QMC, Nottingham NG7 2UH, UK.
  • 2 School of Life Sciences, University of Nottingham, Medical School, QMC, Nottingham NG7 2UH, UK [email protected].
PMID: 27733589 DOI: 10.1098/rsob.160223
Abstract

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 α4-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 α4-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.

Keywords

ATP turnover; MCAK; depolymerization; kinesin-13; microtubule; microtubule end recognition.

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