The phosphorylation site for Ste20p-like protein kinases is essential for the function of myosin-I in yeast

From National Research Council Canada

DOIResolve DOI: https://doi.org/10.1074/jbc.272.49.30623
AuthorSearch for: 1; Search for: 1; Search for: 1; Search for: 1
Name affiliation
  1. National Research Council of Canada. NRC Biotechnology Research Institute
FormatText, Article
Journal titleThe Journal of Biological Chemistry
ISSN0021-9258
1083-351X
Volume272
Issue49
Pages30623–30626
Subjectpharmaceutical
Abstract
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.
Publication date
PublisherAmerican Society for Biochemistry and Molecular Biology
LanguageEnglish
Peer reviewedYes
NRC numberNRC-BRI-39978
NPARC number3539420
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Record created2009-03-01
Record modified2020-03-20
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