Processivity of the single-headed kinesin KIF1A through biased binding to tubulin

Yasushi Okada, Hideo Higuchi and Nobutaka Hirokawa ()
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Yasushi Okada: University of Tokyo, Graduate School of Medicine
Hideo Higuchi: Tohoku University
Nobutaka Hirokawa: University of Tokyo, Graduate School of Medicine

Nature, 2003, vol. 424, issue 6948, 574-577

Abstract: Abstract Conventional isoforms of the motor protein kinesin behave functionally not as ‘single molecules’ but as ‘two molecules’ paired. This dimeric structure poses a barrier to solving its mechanism1,2,3,4. To overcome this problem, we used an unconventional kinesin KIF1A (refs 5, 6) as a model molecule. KIF1A moves processively as an independent monomer7,8, and can also work synergistically as a functional dimer9. Here we show, by measuring its movement with an optical trapping system10, that a single ATP hydrolysis triggers a single stepping movement of a single KIF1A monomer. The step size is distributed stochastically around multiples of 8 nm with a gaussian-like envelope and a standard deviation of 15 nm. On average, the step is directional to the microtubule's plus-end against a load force of up to 0.15 pN. As the source for this directional movement, we show that KIF1A moves to the microtubule's plus-end by ∼3 nm on average on binding to the microtubule, presumably by preferential binding to tubulin on the plus-end side. We propose a simple physical formulation to explain the movement of KIF1A.

Date: 2003
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DOI: 10.1038/nature01804

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