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J Biol Chem, Vol. 274, Issue 47, 33654-33660, November 19, 1999

The Kinesin-like Motor Protein KIF1C Occurs in Intact Cells as a Dimer and Associates with Proteins of the 14-3-3 Family

From the Medical Clinic IV, University of Tübingen, Tübingen, 72076 Germany and the ^§ Max-Planck-Institut für Biochemie, Martinsried, 82152 Germany

Proteins of the kinesin superfamily are regulated in their motor activity as well as in their ability to bind to their cargo by carboxyl-terminal associating proteins and phosphorylation. KIF1C, a recently identified member of the KIF1/Unc104 family, was shown to be involved in the retrograde vesicle transport from the Golgi-apparatus to the endoplasmic reticulum. In a yeast two-hybrid screen using the carboxyl-terminal 350 amino acids of KIF1C as a bait, we identified as binding proteins 14-3-3 , , , and . In addition, a clone encoding the carboxyl-terminal 290 amino acids of KIF1C was found, indicating a potential for KIF1C to dimerize. Subsequent transient overexpression experiments showed that KIF1C can dimerize efficiently. However, in untransfected cells, only a small portion of KIF1C was detected as a dimer. The association of 14-3-3 proteins with KIF1C could be confirmed in transient expression systems and in untransfected cells and was dependent on the phosphorylation of serine 1092 located in a consensus binding sequence for 14-3-3 ligands. Serine 1092 was a substrate for the protein kinase casein kinase II in vitro, and inhibition of casein kinase II in cells diminished the association of KIF1C with 14-3-3. Our data thus suggest that KIF1C can form dimers and is associated with proteins of the 14-3-3 family.

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