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MBC in Press, published online ahead of print October 19, 2005
Mol. Biol. Cell 10.1091/mbc.E05-06-0565

A more recent version of this article appeared on January 1, 2006
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Submitted on June 27, 2005
Revised on October 5, 2005
Accepted on October 12, 2005

The CLIP170 Homologue Bik1p Promotes the Phosphorylation and Asymmetric Localization of Kar9p

Jeffrey K. Moore, Sonia D’Silva, and Rita K. Miller

Department of Biology, University of Rochester, Rochester, NY 14627

Monitoring Editor: Tim Stearns

Accurate positioning of the mitotic spindle in S. cerevisiae is coordinated with the asymmetry of the two poles and requires the microtubule-to-actin linker, Kar9p. The asymmetric localization of Kar9p to one SPB and microtubule (MT) plus ends requires Cdc28p. Here, we show that the CLIP170 homologue, Bik1p, binds directly to Kar9p. In the absence of Bik1p, Kar9p localization is not restricted to the daughter-bound SPB, but is instead found on both SPBs. Kar9p is hypo-phosphorylated in bik1{Delta} mutants and Bik1p binds to both phosphorylated and unphosphorylated isoforms of Kar9p. Furthermore, the two-hybrid interaction between full length KAR9 and the cyclin CLB5 requires BIK1. The binding site of Clb5p on Kar9p maps to a short region within the basic domain of Kar9p that contains a conserved phosphorylation site, serine 496. Consistent with this, Kar9p is found on both SPBs in clb5{Delta} mutants at a frequency comparable to that seen in kar9-S496A strains. Together, these data suggest that Bik1p promotes the phosphorylation of Kar9p on serine 496, which affects its asymmetric localization to one SPB and associated cytoplasmic microtubules (cMTs). These findings provide further insight into a mechanism for directing centrosomal inheritance.

Address correspondence to: Rita K. Miller (rmlr{at}mail.rochester.edu)




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