Abstract
The osmotic balance between the cytoplasmic and extracellular compartments of cells is critical for the control of cell volume. A mammalian protein kinase, Jnk, which is a distant relative of the mitogen-activated protein kinase group, was activated by phosphorylation on threonine and tyrosine in osmotically shocked cells. The activation of Jnk may be relevant to the biological response to osmotic shock because the expression of human Jnk in the yeast Saccharomyces cerevisiae rescued a defect in growth on hyper-osmolar media. These data indicate that related protein kinases may mediate osmosensing signal transduction in yeast and mammalian cells.
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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Animals
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CHO Cells
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Calcium-Calmodulin-Dependent Protein Kinases / genetics
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Cricetinae
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Cricetulus
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Enzyme Activation
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Genetic Complementation Test
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JNK Mitogen-Activated Protein Kinases
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Mitogen-Activated Protein Kinases*
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Molecular Sequence Data
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Osmotic Pressure
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Protein Serine-Threonine Kinases / physiology*
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Saccharomyces cerevisiae / genetics
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Saccharomyces cerevisiae Proteins*
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Sequence Homology, Amino Acid
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Signal Transduction / physiology*
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Water-Electrolyte Balance / physiology*
Substances
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Saccharomyces cerevisiae Proteins
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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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JNK Mitogen-Activated Protein Kinases
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Mitogen-Activated Protein Kinases
Associated data
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GENBANK/L06279
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GENBANK/L26318