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.
Regulation of KinI kinesin ATPase activity by binding to the microtubule lattice
C. Moores,Mohammad Hekmat-Nejad,R. Sakowicz,R. Milligan
Published 2003 in Journal of Cell Biology
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- Publication year
2003
- Venue
Journal of Cell Biology
- Publication date
2003-12-08
- Fields of study
Biology, Medicine
- Identifiers
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- Source metadata
Semantic Scholar, PubMed
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