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
(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]