Journal
NATURE REVIEWS MOLECULAR CELL BIOLOGY
Volume 10, Issue 12, Pages 877-884Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nrm2807
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Most kinesins move processively along microtubules by using energy derived from ATP hydrolysis. Almost all of the intermediate structures of this ATPase reaction cycle have been solved for the monomeric kinesin 3 family motor KIF1A. Based on this structural information, we propose a common mechanism of kinesin motility, focusing on the regulation of kinesin motility through their interaction with microtubules and by their 'neck-linker' region, which connects their motor domain to cargo and kinesin partner heads.
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