A kinesin-like motor inhibits microtubule dynamic instability
Research output: Contribution to journal › Research article › Contributed › peer-review
Contributors
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.
Details
| Original language | English |
|---|---|
| Pages (from-to) | 1519-1522 |
| Number of pages | 4 |
| Journal | Science |
| Volume | 303 |
| Issue number | 5663 |
| Publication status | Published - 5 Mar 2004 |
| Peer-reviewed | Yes |
| Externally published | Yes |
External IDs
| Scopus | 1542317579 |
|---|---|
| ORCID | /0000-0002-7689-8617/work/142237005 |
Keywords
Keywords
- Adenosine Triphosphatases/metabolism, Adenosine Triphosphate/metabolism, Adenylyl Imidodiphosphate/metabolism, Animals, Centrosome/metabolism, Chromosomes/metabolism, Cryoelectron Microscopy, Dimerization, Kinetics, Microtubule-Associated Proteins/chemistry, Microtubules/drug effects, Molecular Motor Proteins/metabolism, Paclitaxel/pharmacology, Protein Binding, Protein Structure, Tertiary, Recombinant Fusion Proteins/metabolism, Tubulin/metabolism, Xenopus Proteins/chemistry, Xenopus laevis