| DOI | Resolve DOI: https://doi.org/10.1074/jbc.272.49.30623 |
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| Author | Search for: Wu, Cunle1 ; Search for: Lytvyn, Viktoria1 ; Search for: Thomas, David Y.1 ; Search for: Leberer, Ekkehard1 |
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| Name affiliation | - National Research Council Canada. NRC Biotechnology Research Institute
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| Format | Text |
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| Type | Article |
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| Journal title | The Journal of Biological Chemistry |
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| Volume | 272 |
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| Issue | 49 |
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| Pages | 30623–30626; # of pages: 4 |
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| Subject | pharmaceutical |
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| 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. |
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| Publication date | 1997-12-05 |
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| Language | English |
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| NRC number | 39978 |
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| NPARC number | 3539420 |
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| Export citation | Export as RIS |
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| Report a correction | Report a correction |
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Record identifier | 57390ace-6a05-491b-89e6-b1eec0af2fb5 | | Record created | 2009-03-01 |
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| Record modified | 2019-08-15 |
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