title: Kinesin-2: a family of heterotrimeric and homodimeric motors with diverse intracellular transport functions.
abstract: Kinesin-2 was first purified as a heterotrimeric, anterograde, microtubule-based motor consisting of two distinct kinesin-related subunits and a novel associated protein (KAP) that is currently best known for its role in intraflagellar transport and ciliogenesis. Subsequent work, however, has revealed diversity in the oligomeric state of different kinesin-2 motors owing to the combinatorial heterodimerization of its subunits and the coexistence of both heterotrimeric and homodimeric kinesin-2 motors in some cells. Although the functional significance of the homo- versus heteromeric organization of kinesin-2 motor subunits and the role of KAP remain uncertain, functional studies suggest that cooperation between different types of kinesin-2 motors or between kinesin-2 and a member of a different motor family can generate diverse patterns of anterograde intracellular transport. Moreover, despite being restricted to ciliated eukaryotes, kinesin-2 motors are now known to drive diverse transport events outside cilia. Here, I review the organization, assembly, phylogeny, biological functions, and motility mechanism of this diverse family of intracellular transport motors.
authors.affiliation: Department of Molecular and Cell Biology, University of California, Davis, California 95616; email: jmscholey@ucdavis.edu.
authors.forename: Jonathan M
authors.initials: JM
authors.lastname: Scholey
mesh_terms: D000818:Animals; D001692:Biological Transport; D019143:Evolution, Molecular; D006801:Humans; D016547:Kinesins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D020409:Molecular Motor Proteins / Q000378:metabolism
chemical_list: D020409:Molecular Motor Proteins; D016547:Kinesins