PubMed Journals: J Biol Chem

  Source:		PMID: 10559254

    		J Biol Chem. 1999 Nov 19;274(47):33654-60.
			The kinesin-like motor protein KIF1C occurs
			in intact cells as a dimer and associates
			with proteins of the 14-3-3 family.

			Dorner C(1), Ullrich A, Häring HU, Lammers

			Author Information
			(1) Medical Clinic IV, University of Tübingen,
			Tübingen, 72076 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 beta, gamma, epsilon, and zeta. 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 14-3-3gamma. Our data thus
			suggest that KIF1C can form dimers and is
			associated with proteins of the 14-3-3 family.

			PMID: 10559254 [Indexed for MEDLINE]

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