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J Biol Chem, Vol. 275, Issue 18, 13737-13745, May 5, 2000
From the Department of Biology and Program in Cell and Molecular
Biology, Colorado State University, Fort Collins, Colorado 80523
Kinesin-like calmodulin-binding protein (KCBP) is
a novel member of the kinesin superfamily that is involved in cell
division and trichome morphogenesis. KCBP is unique among all known
kinesins in having a myosin tail homology-4 region in the N-terminal
tail and a calmodulin-binding region following the motor domain.
Calcium, through calmodulin, has been shown to negatively regulate the interaction of KCBP with microtubules. Here we have used the yeast two-hybrid system to identify the proteins that interact with the tail
region of KCBP. A protein kinase (KCBP-interacting protein kinase
(KIPK)) was found to interact specifically with the tail region of
KCBP. KIPK is related to a group of protein kinases specific to plants
that has an additional sequence between subdomains VII and VIII of the
conserved C-terminal catalytic domain and an extensive N-terminal
region. The catalytic domain alone of KIPK interacted weakly with the
N-terminal KCBP protein but strongly with full-length KCBP, whereas the
noncatalytic region did not interact with either protein. The
interaction of KCBP with KIPK was confirmed using coprecipitation
assays. Using bacterially expressed full-length and truncated proteins,
we have shown that the catalytic domain is capable of phosphorylating
itself. The association of KIPK with KCBP suggests regulation of KCBP
or KCBP-associated proteins by phosphorylation and/or that KCBP is
involved in targeting KIPK to its proper cellular location.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF236104.
Interaction of a Kinesin-like Calmodulin-binding Protein with a
Protein Kinase*
*
This work was supported by National Science Foundation Grant
MCB-9630782 (to A. S. N. R.).The costs of publication of this article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.: 970-491-5773;
Fax: 970-491-0649; E-mail: reddy@lamar.colostate.edu.
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