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J Biol Chem, Vol. 273, Issue 32, 20267-20275, August 7, 1998
From the Department of Molecular Biology, Max-Planck Institut
für Biochemie, Am Klopferspitz 18a,
82152 Martinsried, Germany
Kinesins comprise a large family of
microtubule-based motor proteins, of which individual members mediate
specific types of motile processes. Using the ezrin domain of the
protein-tyrosine phosphatase PTPD1 as a bait in a yeast two-hybrid
screen, we identified a new kinesin-like protein, KIF1C. KIF1C
represents a member of the Unc104 subfamily of kinesin-like proteins
that are involved in the transport of mitochondria or synaptic vesicles
in axons. Like its homologues, the 1103-amino acid protein KIF1C
consists of an amino-terminal motor domain followed by a U104 domain
and probably binds to target membranes through carboxyl-terminal
sequences. Interestingly, KIF1C was tyrosine-phosphorylated after
peroxovanadate stimulation when overexpressed in 293 or NIH3T3
fibroblasts or in native C2C12 cells.
Using immunofluorescence, we found that KIF1C is localized primarily at
the Golgi apparatus. In brefeldin A-treated cells, the Golgi membranes
and KIF1C redistributed to the endoplasmic reticulum (ER). This
brefeldin A-induced flow of Golgi membranes into the ER was inhibited
in cells transiently overexpressing catalytically inactive KIF1C. In
conclusion, our data suggest an involvement of tyrosine phosphorylation
in the regulation of the Golgi to ER membrane flow and describe a new kinesin-like motor protein responsible for this transport.
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