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The kinesin-related protein MCAK is a microtubule depolymerase that forms an ATP-hydrolyzing complex at microtubule ends

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Hunter,  A. W.
Max Planck Society;

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Diez,  S.
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Howard,  J.
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Citation

Hunter, A. W., Caplow, M., Coy, D. L., Hancock, W. O., Diez, S., Wordeman, L., et al. (2003). The kinesin-related protein MCAK is a microtubule depolymerase that forms an ATP-hydrolyzing complex at microtubule ends. Molecular Cell, 11(2), 445-457.


Cite as: https://hdl.handle.net/21.11116/0000-0001-12A5-0
Abstract
MCAK belongs to the Kin I subfamily of kinesin-related proteins, a unique group of motor proteins that are not motile but instead destabilize microtubules. We show that MCAK is an ATPase that catalytically depolymerizes microtubules by accelerating, 100-fold, the rate of dissociation of tubulin from microtubule ends. MCAK has one high-affinity binding site per protofilament end, which, when occupied, has both the depolymerase and ATPase activities. MCAK targets protofilament ends very rapidly (on-rate 54 muM(-1).s(-1)), perhaps by diffusion along the microtubule lattice and, once there, removes similar to20 tubulin dimers at a rate of 1 s(-1). We propose that up to 14 MCAK dimers assemble at the end of a microtubule to form an ATP-hydrolyzing complex that processively depolymerizes the microtubule.