Directional motility of kinesin motor proteins.
Kinesin motor proteins are molecules capable of moving along microtubules. They share homology in the so-called core motor domain which acts as a microtubule-dependent ATPase. The surprising finding that different members of the superfamily move in opposite directions along microtubules despite their close similarity has stimulated intensive research on the determinants of motor directionality. This article reviews recent biophysical, biochemical, structural and mutagenic studies that contributed to the elucidation of the mechanisms that cause directional motion of kinesin motor proteins.
Woehlke
G
G
Adolf-Butenandt-Institute of Cell Biology, Ludwig-Maximilians-University Munich, Schillerstr. 42, D-80 336, Munich, Germany. guenther.woehlke@lrz.uni-muenchen.de
Schliwa
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M
D000595:Amino Acid Sequence; D000818:Animals; D020285:Cryoelectron Microscopy; D018360:Crystallography, X-Ray; D029721:Drosophila Proteins; D006801:Humans; D016547:Kinesins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism* / Q000648:ultrastructure; D007700:Kinetics; D008870:Microtubules / Q000737:chemistry / Q000235:genetics / Q000378:metabolism / Q000648:ultrastructure; D008954:Models, Biological; D020409:Molecular Motor Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism* / Q000648:ultrastructure; D008969:Molecular Sequence Data; D009068:Movement; D009154:Mutation / Q000235:genetics; D013816:Thermodynamics
D029721:Drosophila Proteins; D020409:Molecular Motor Proteins; C066696:ncd protein, Drosophila; D016547:Kinesins