title: Kinesin assembly and movement in cells.
abstract: Long-distance transport in eukaryotic cells is driven by molecular motors that move along microtubule tracks. Molecular motors of the kinesin superfamily contain a kinesin motor domain attached to family-specific sequences for cargo binding, regulation, and oligomerization. The biochemical and biophysical properties of the kinesin motor domain have been widely studied, yet little is known about how kinesin motors work in the complex cellular environment. We discuss recent studies on the three major families involved in intracellular transport (kinesin-1, kinesin-2, and kinesin-3) that have begun to bridge the gap in knowledge between the in vitro and in vivo behaviors of kinesin motors. These studies have increased our understanding of how kinesin subunits assemble to produce a functional motor, how kinesin motors are affected by biochemical cues and obstacles present on cellular microtubules, and how multiple motors on a cargo surface can work collectively for increased force production and travel distance.
authors.affiliation: Department of Cell and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, USA. kjverhey@umich.edu
authors.forename: Kristen J
authors.initials: KJ
authors.lastname: Verhey
authors.forename: Neha
authors.initials: N
authors.lastname: Kaul
authors.forename: Virupakshi
authors.initials: V
authors.lastname: Soppina
mesh_terms: D001665:Binding Sites; D002465:Cell Movement / Q000502:physiology*; D003198:Computer Simulation; D016547:Kinesins / Q000737:chemistry* / Q000502:physiology*; D008954:Models, Biological; D008956:Models, Chemical; D020409:Molecular Motor Proteins / Q000737:chemistry* / Q000502:physiology*; D011485:Protein Binding
chemical_list: D020409:Molecular Motor Proteins; D016547:Kinesins