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(Received for publication, September 8, 1997, and in revised form, October 2, 1997)
From the Eukaryotic Genetics Group, Biotechnology Research
Institute, National Research Council of Canada, Montreal,
Quebec H4P 2R2, Canada
The budding yeast Saccharomyces
cerevisiae has two functionally redundant myosin-I isoforms
encoded by the MYO3 and MYO5 genes. The
function shared by these myosin proteins is required for proper yeast
budding. Serine residue 357 in the head domain of Myo3p, conserved
among myosin-I proteins including yeast Myo5p, was identified as a
unique phosphorylation site for the serine/threonine protein kinase
Ste20p and its closely related isoform Cla4p. These protein kinases
share a function that is also essential for budding. Replacement of
serine 357 with alanine disrupted the in vivo function of
Myo3p, whereas this function was maintained by changing the serine
residue to aspartate. This mutant version failed to compensate the
growth defect of cells which lack both Ste20p and Cla4p, suggesting
that myosin-I is not the only essential target of these protein
kinases. Our results suggest that phosphorylation of the head domain by Ste20p-like protein kinases plays an essential role in the function of
myosin-I in yeast cells.
Volume 272, Number 49,
Issue of December 5, 1997
pp. 30623-30626
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
COMMUNICATION:
The Phosphorylation Site for Ste20p-like Protein Kinases Is
Essential for the Function of Myosin-I in Yeast
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