A Kinesin-like Motor Inhibits Microtubule Dynamic Instability

Adenosine Triphosphatases Centrosome 0301 basic medicine Paclitaxel Molecular Motor Proteins Recombinant Fusion Proteins Adenylyl Imidodiphosphate Cryoelectron Microscopy Xenopus Proteins Microtubules Chromosomes Protein Structure, Tertiary Kinetics Xenopus laevis 03 medical and health sciences Adenosine Triphosphate Tubulin Animals Dimerization Microtubule-Associated Proteins Protein Binding
DOI: 10.1126/science.1094838 Publication Date: 2004-03-04T21:23:36Z
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.
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