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© The Rockefeller University Press, 0021-9525/1998//873 $5.00
The Journal of Cell Biology, Volume 140, Number 4, , 1998 873-883

Article

Smy1p, a Kinesin-related Protein That Does Not Require Microtubules



S.H. Lillie and S.S. Brown

Department of Anatomy and Cell Biology, University of Michigan Medical School, Ann Arbor, Michigan 48109-0616

Abstract. We have previously reported that a defect in Myo2p, a myosin in budding yeast (Saccharomyces cerevisiae), can be partially corrected by overexpression of Smy1p, which is by sequence a kinesin-related protein (Lillie, S.H., and S.S. Brown. 1992. Nature. 356:358– 361). Such a functional link between putative actin- and microtubule-based motors is surprising, so here we have tested the prediction that Smy1p indeed acts as a microtubule-based motor. Unexpectedly, we found that abolition of microtubules by nocodazole does not interfere with the ability of Smy1p to correct the mutant Myo2p defect, nor does it interfere with the ability of Smy1p to localize properly. In addition, other perturbations of microtubules, such as treatment with benomyl or introduction of tubulin mutations, do not exacerbate the Myo2p defect. Furthermore, a mutation in SMY1 strongly predicted to destroy motor activity does not destroy Smy1p function. We have also observed a genetic interaction between SMY1 and two of the late SEC mutations, sec2 and sec4. This indicates that Smy1p can play a role even when Myo2p is wild type, and that Smy1p acts at a specific step of the late secretory pathway. We conclude that Smy1p does not act as a microtubule-based motor to localize properly or to compensate for defective Myo2p, but that it must instead act in some novel way.

We thank C. Schmidt (University of Michigan, Ann Arbor, MI) for in vitro motility assays; T. Huffaker for the gifts of benomyl and tub2 mutants, and for advice on the use of benomyl; A. Hoyt for tub1 and tub3 mutants; A. Hoyt and T. Stearns for advice on nocodazole; and B. Fuller (University of Michigan) for critical reading of the manuscript.

This work was supported by a grant to S.S. Brown, (RO1GM46745) and partially by a grant to the General Clinical Research Center at the University of Michigan (M01RR00042), both from the National Institutes of Health.

Address all correspondence to Susan S. Brown, Department of Anatomy and Cell Biology, University of Michigan Medical School, Ann Arbor, MI 48109-0616. Tel.: (313) 764-2520. Fax: (313) 763-1166. E-mail: susanbb{at}umich.edu

1. Abbreviations used in this paper: YM-P, yeast medium-Pringle; YPD, yeast extract/peptone/dextrose medium.


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