Abstract
ERK6, a mitogen-activated protein (MAP) kinase-related serine/threonine kinase, is highly expressed in human skeletal muscle and appears to function as a signal transducer during differentiation of myoblasts to myotubes. In transfected 293 cells, activation of the 45-kDa enzyme results in tyrosine-phosphorylated 46- and 56-kDa forms, which phosphorylate myelin basic protein. Overexpression of wild-type ERK6 or the inactive mutant Y185F has no effect on fibroblast and myoblast proliferation, but it enhances or inhibits C2C12 cell differentiation to myotubes, respectively. Our findings suggest ERK6 to be a tissue-specific, differentiation signal-transducing factor that is connected to phosphotyrosine-mediated signaling pathways distinct from those activating other members of the MAP kinase family such as LRK1 and ERK2.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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3T3 Cells
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Amino Acid Sequence
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Animals
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Base Sequence
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Cell Differentiation
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Cloning, Molecular
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Enzyme Activation
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Gene Library
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Genetic Vectors
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Humans
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Insulin / pharmacology
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Kidney
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Mice
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Mitogen-Activated Protein Kinase 12
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Mitogen-Activated Protein Kinases*
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Molecular Sequence Data
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Muscle, Skeletal / enzymology
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Mutagenesis, Site-Directed
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Myelin Basic Protein / metabolism
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Oligodeoxyribonucleotides
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Phosphotyrosine / analysis
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Point Mutation
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Protein Kinases / biosynthesis
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Protein Kinases / metabolism*
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / metabolism
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Retroviridae
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Sequence Homology, Amino Acid
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Signal Transduction
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Transfection
Substances
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Insulin
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Myelin Basic Protein
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Oligodeoxyribonucleotides
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Recombinant Proteins
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Phosphotyrosine
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Protein Kinases
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Mitogen-Activated Protein Kinase 12
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Mitogen-Activated Protein Kinases