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J. Cell Biol.,
Volume 144, Number 6, March 22, 1999 1219-1233
Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, Connecticut 06520-8103
The mechanisms by which kinesin-related
proteins interact with other proteins to carry out specific cellular processes is poorly understood. The kinesin-related protein, Kar3p, has been implicated in many
microtubule functions in yeast. Some of these functions
require interaction with the Cik1 protein (Page, B.D., L.L. Satterwhite, M.D. Rose, and M. Snyder. 1994. J.
Cell Biol. 124:507-519). We have identified a Saccharomyces cerevisiae gene, named VIK1, encoding a protein
with sequence and structural similarity to Cik1p. The
Vik1 protein is detected in vegetatively growing cells
but not in mating pheromone-treated cells. Vik1p physically associates with Kar3p in a complex separate from
that of the Kar3p-Cik1p complex. Vik1p localizes to the
spindle-pole body region in a Kar3p-dependent manner. Reciprocally, concentration of Kar3p at the spindle
poles during vegetative growth requires the presence of
Vik1p, but not Cik1p. Phenotypic analysis suggests that
Cik1p and Vik1p are involved in different Kar3p functions. Disruption of VIK1 causes increased resistance to
the microtubule depolymerizing drug benomyl and partially suppresses growth defects of cik1
mutants. The
vik1 and kar3 mutations, but not cik1, partially suppresses the temperature-sensitive growth defect of
strains lacking the function of two other yeast kinesin-related proteins, Cin8p and Kip1p. Our results indicate
that Kar3p forms functionally distinct complexes with
Cik1p and Vik1p to participate in different microtubule-mediated events within the same cell.
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