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Published 8 December 2003. doi:10.1083/jcb.200304034
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© The Rockefeller University Press, 0021-9525/2003/12/963 $8.00
The Journal of Cell Biology, Volume 163, Number 5, 963-971

Article

 Regulation of KinI kinesin ATPase activity by binding to the microtubule lattice

Carolyn A. Moores1, Mohammad Hekmat-Nejad2, Roman Sakowicz2 and Ronald A. Milligan1

1 Department of Cell Biology, The Scripps Research Institute, La Jolla, CA 92037
2 Cytokinetics Inc., South San Francisco, CA 94080

Address correspondence to Ronald A. Milligan, Department of Cell Biology, CB227, The Scripps Research Institute, 10550 N. Torrey Pines Road, La Jolla, CA 92037. Tel.: (858) 784-9827. Fax: (858) 784-2749. email: milligan{at}scripps.edu

KinI kinesins are important in regulating the complex dynamics of the microtubule cytoskeleton. They are unusual in that they depolymerize, rather than move along microtubules. To determine the attributes of KinIs that distinguish them from translocating kinesins, we examined the ATPase activity, microtubule affinity, and three-dimensional microtubule-bound structure of a minimal KinI motor domain. Together, the kinetic, affinity, and structural data lead to the conclusion that on binding to the microtubule lattice, KinIs release ADP and enter a stable, low-affinity, regulated state, from which they do not readily progress through the ATPase cycle. This state may favor detachment, or diffusion of the KinI to its site of action, the microtubule ends. Unlike conventional translocating kinesins, which are microtubule lattice–stimulated ATPases, it seems that with KinIs, nucleotide-mediated modulation of tubulin affinity is only possible when it is coupled to protofilament deformation. This provides an elegant mechanistic basis for their unique depolymerizing activity.

Key Words: kinesin; microtubules; cryoelectron microscopy; protein structure; mitosis

The online version of this article includes supplemental material.


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