Kinesin Family, Member 1C (KIF1C)

KIF1C contains an N-terminal motor domain followed by a U104 domain. KIF1C migrated as an approximately 135-kD protein. KIF1C was expressed as a 4.2-kb mRNA in all human tissues examined, with the most abundant expression in heart and skeletal muscle. KIF1C is tyrosine-phosphorylated and associates with PTPD1 in vivo. KIF1C is localized primarily at the Golgi apparatus. Disruption of the Golgi apparatus with brefeldin A induced the flow of Golgi membranes and KIF1C to the endoplasmic reticulum. This redistribution of membranes was inhibited in cells overexpressing a catalytically inactive mutant KIF1C protein. The authors concluded that KIF1C is required for the retrograde transport of Golgi vesicles to the endoplasmic reticulum and that tyrosine phosphorylation is a putative regulator of this transport.