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KIF1B 2, Capable of Interacting with CHP, Is Localized to Synaptic Vesicles
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2002
Year
Synaptic TransmissionKif1b 2Molecular BiologyCytoskeletonCellular NeurobiologySynaptic SignalingCellular PhysiologySynaptic VesiclesKinesin Family ProteinsMolecular SignalingProtein FunctionMolecular PhysiologyMolecular NeuroscienceNovel Kinesin-related ProteinProtein TransportCell BiologyProtein PhosphorylationKinesin-related ProteinsSynaptic PlasticitySignal TransductionNatural SciencesMolecular NeurobiologyIntracellular TraffickingCellular BiochemistryMedicine
Kinesin family proteins are microtubule-dependent molecular motors involved in the intracellular motile process. Using a Ca2+ -binding protein, CHP (calcineurin B homologous protein), as a bait for yeast two hybrid screening, we identified a novel kinesin-related protein, KIF1Bbeta2. KIF1Bbeta2 is a member of the KIF1 subfamily of kinesin-related proteins, and consists of an amino terminal KIF1B-type motor domain followed by a tail region highly similar to that of KIF1A. CHP binds to regions adjacent to the motor domains of KIF1Bbeta2 and KIF1B, but not to those of the other KIF1 family members, KIF1A and KIF1C. Immunostaining of neuronal cells showed that a significant portion of KIF1Bbeta2 is co-localized with synaptophysin, a marker protein for synaptic vesicles, but not with a mitochondria-staining dye. Subcellular fractionation analysis indicated the co-localization of KIF1Bbeta2 with synaptophysin. These results suggest that KIF1Bbeta2, a novel CHP-interacting molecular motor, mediates the transport of synaptic vesicles in neuronal cells.