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Vol. 11, Issue 2, 691-702, February 2000
Department of Anatomy and Cell Biology, University of Michigan
Medical School, Ann Arbor, Michigan 48109-0616
We have discovered evidence for a physical interaction between a
class V myosin, Myo2p, and a kinesin-related protein, Smy1p, in budding
yeast. These proteins had previously been linked by genetic and
colocalization studies, but we had been unable to determine the nature
of their association. We now show by two-hybrid analysis that a
69-amino acid region of the Smy1p tail interacts with the globular
portion of the Myo2p tail. Deletion of this myosin-binding region of
Smy1p eliminates its ability to colocalize with Myo2p and to overcome
the myo2-66 mutant defects, suggesting that the
interaction is necessary for these functions. Further insights about
the Smy1p-Myo2p interaction have come from studies of a new mutant
allele, myo2-2, which causes a loss of Myo2p
localization. We report that Smy1p localization is also lost in the
myo2-2 mutant, demonstrating that Smy1p localization is
dependent on Myo2p. We also found that overexpression of Smy1p
partially restores myo2-2p localization in a myosin-binding
region-dependent manner. Thus, overexpression of Smy1p can overcome
defects in both the head and tail domains of Myo2p (caused by the
myo2-66 and myo2-2 alleles, respectively). We propose that Smy1p enhances some aspect of Myo2p function, perhaps delivery or docking of vesicles at the bud tip.
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