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Published 28 February 2005. doi:10.1083/jcb.200409035
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 168, Number 5, 691-696
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 Long-range cooperative binding of kinesin to a microtubule in the presence of ATP

Etsuko Muto1,2, Hiroyuki Sakai3, and Kuniyoshi Kaseda4

1 Form and Function Group, PRESTO, JST, Mino, Osaka 562-0035, Japan
2 Brain Developmental Research Group, RIKEN Brain Science Institute, Saitama 351-0198, Japan
3 Laboratory for Neuroinformatics, Advanced Technology Development Group, RIKEN Brain Science Institute, Saitama 351-0198, Japan
4 Gene Function Research Center, National Institute of Advanced Industrial Science and Technology, Ibaraki 305-8562, Japan

Correspondence to Etsuko Muto: emuto{at}brain.riken.go.jp


Abstract
Interaction of kinesin-coated latex beads with a single microtubule (MT) was directly observed by fluorescence microscopy. In the presence of ATP, binding of a kinesin bead to the MT facilitated the subsequent binding of other kinesin beads to an adjacent region on the MT that extended for micrometers in length. This cooperative binding was not observed in the presence of ADP or 5'-adenylylimidodiphosphate (AMP-PNP), where binding along the MT was random. Cooperative binding also was induced by an engineered, heterodimeric kinesin, WT/E236A, that could hydrolyze ATP, yet remained fixed on the MT in the presence of ATP. Relative to the stationary WT/E236A kinesin on a MT, wild-type kinesin bound preferentially in close proximity, but was biased to the plus-end direction. These results suggest that kinesin binding and ATP hydrolysis may cause a long-range state transition in the MT, increasing its affinity for kinesin toward its plus end. Thus, our study highlights the active involvement of MTs in kinesin motility.

K. Kaseda's present address is Molecular Motor Group, Marie Curie Research Institute, Surrey, RH8 0TL, UK.

Abbreviations used in this paper: AMP-PNP, 5'-adenylylimidodiphosphate; MT, microtubule; PDD, probability density distribution.


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