The mechanisms of kinesin motor motility: lessons from the monomeric motor KIF1A.
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.
Hirokawa
Nobutaka
N
Department of Cell Biology and Anatomy, University of Tokyo, Graduate School of Medicine, Bunkyo-ku, Tokyo, Japan. hirokawa@m.u-tokyo.ac.jp
Nitta
Ryo
R
Okada
Yasushi
Y
D000818:Animals; D006801:Humans; D016547:Kinesins / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D009711:Nucleotides / Q000378:metabolism; D017434:Protein Structure, Tertiary; D021381:Protein Transport
D009711:Nucleotides; D016547:Kinesins