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© The Rockefeller University Press, 0021-9525/1999//1219 $5.00
The Journal of Cell Biology, Volume 144, Number 6, , 1999 1219-1233

Regular Articles

Differential Regulation of the Kar3p Kinesin-related Protein by Two Associated Proteins, Cik1p and Vik1p



Brendan D. Manning, Jennifer G. Barrett, Julie A. Wallace, Howard Granok, and Michael Snyder

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{Delta} mutants. The vik1{Delta} and kar3{Delta} mutations, but not cik1{Delta}, 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.

Key Words: kinesin • microtubules • molecular motors • cytoskeleton • Saccharomyces cerevisiae

Abbreviations used in this paper: HA, hemagglutinin; HAT, HA/transposon tag; KAP, kinesin-associated protein; KHC, kinesin-heavy chain; KLC, kinesin light chain; KRP, kinesin-related protein; ORF, open reading frame; SPB, spindle-pole bodies.

B.D. Manning and J.G. Barrett were supported by National Institutes of Health (NIH) training grants and NIH grants GM3649 and GM52197, and this research was funded by NIH grant GM52197.


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