A Kinesin-like Motor Inhibits Microtubule Dynamic Instability

• DOI: 10.1126/science.1094838
• Publication Date: 2004-03-04T21:23:36Z
• Authors: Henrik Bringmann; Georgios Skiniotis; Annina Spilker; Stefanie Kandels-...; Isabelle Vernos; Thomas Surrey
• Keywords: 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

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.