Abstract
The motility of molecular motors and the dynamic instability of microtubules are key dynamic processes for mitotic spindle assembly and function. We report here that one of the mitotic kinesins that localizes to chromosomes, Xklp1 from Xenopus laevis, could inhibit microtubule growth and shrinkage. This effect appeared to be mediated by a structural change in the microtubule lattice. We also found that Xklp1 could act as a fast, nonprocessive, plus end-directed molecular motor. The integration of the two properties, motility and inhibition of microtubule dynamics, in one molecule emphasizes the versatile properties of kinesin family members.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine Triphosphatases / metabolism
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Adenosine Triphosphate / metabolism
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Adenylyl Imidodiphosphate / metabolism
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Adenylyl Imidodiphosphate / pharmacology
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Animals
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Centrosome / metabolism
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Chromosomes / metabolism
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Cryoelectron Microscopy
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Dimerization
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Kinetics
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Microtubule-Associated Proteins / chemistry
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Microtubule-Associated Proteins / genetics
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Microtubule-Associated Proteins / metabolism*
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Microtubules / drug effects
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Microtubules / metabolism
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Microtubules / physiology*
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Microtubules / ultrastructure
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Molecular Motor Proteins / metabolism*
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Paclitaxel / pharmacology
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Protein Binding
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Protein Structure, Tertiary
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Recombinant Fusion Proteins / metabolism
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Tubulin / metabolism
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Xenopus Proteins / chemistry
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Xenopus Proteins / genetics
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Xenopus Proteins / metabolism*
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Xenopus laevis
Substances
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Microtubule-Associated Proteins
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Molecular Motor Proteins
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NAT14 protein, Xenopus
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Recombinant Fusion Proteins
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Tubulin
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Xenopus Proteins
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Adenylyl Imidodiphosphate
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Adenosine Triphosphate
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Adenosine Triphosphatases
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Paclitaxel