Abstract
The role of mitogen-activated protein (MAP) kinase cascades in integrating distinct upstream signals was studied in yeast. Mutants that were not able to activate PBS2 MAP kinase kinase (MAPKK; Pbs2p) at high osmolarity were characterized. Pbs2p was activated by two independent signals that emanated from distinct cell-surface osmosensors. Pbs2p was activated by MAP kinase kinase kinases (MAPKKKs) Ssk2p and Ssk22p that are under the control of the SLN1-SSK1 two-component osmosensor. Alternatively, Pbs2p was activated by a mechanism that involves the binding of its amino terminal proline-rich motif to the Src homology 3 (SH3) domain of a putative transmembrane osmosensor Sho1p.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Calcium-Calmodulin-Dependent Protein Kinases / metabolism
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Cloning, Molecular
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Enzyme Activation
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Fungal Proteins / metabolism
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Genes, Fungal
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Intracellular Signaling Peptides and Proteins
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MAP Kinase Kinase Kinases
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Mitogen-Activated Protein Kinase Kinases
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Mitogen-Activated Protein Kinases*
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Molecular Sequence Data
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Mutation
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Osmolar Concentration
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Phosphorylation
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Protein Kinases / metabolism*
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Protein Serine-Threonine Kinases / metabolism*
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Saccharomyces cerevisiae / enzymology*
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Saccharomyces cerevisiae / genetics
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Saccharomyces cerevisiae Proteins*
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Signal Transduction
Substances
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Fungal Proteins
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Intracellular Signaling Peptides and Proteins
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SSK1 protein, S cerevisiae
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Saccharomyces cerevisiae Proteins
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Protein Kinases
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Protein Serine-Threonine Kinases
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Calcium-Calmodulin-Dependent Protein Kinases
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HOG1 protein, S cerevisiae
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Mitogen-Activated Protein Kinases
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MAP Kinase Kinase Kinases
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Mitogen-Activated Protein Kinase Kinases
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SLN1 protein, S cerevisiae
Associated data
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GENBANK/L41926
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GENBANK/L41927