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.
MeSH Terms
3T3 Cells
Amino Acid Sequence
Animals
Base Sequence
Cell Differentiation
Cloning, Molecular
Enzyme Activation
Gene Library
Genetic Vectors
Humans
Insulin/pharmacology
Kidney
Mice
Mitogen-Activated Protein Kinase 12
Mitogen-Activated Protein Kinases
Molecular Sequence Data
Muscle, Skeletal/enzymology
Mutagenesis, Site-Directed
Myelin Basic Protein/metabolism
Oligodeoxyribonucleotides
Phosphotyrosine/analysis
Point Mutation
Protein Kinases/biosynthesis,metabolism
Recombinant Proteins/biosynthesis,metabolism
Retroviridae
Sequence Homology, Amino Acid
Signal Transduction
Transfection
Chemicals
Insulin
Myelin Basic Protein
Oligodeoxyribonucleotides
Recombinant Proteins
Phosphotyrosine
Protein Kinases
Mitogen-Activated Protein Kinase 12
Mitogen-Activated Protein Kinases
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Lechner C
Department of Molecular Biology, Max-Planck-Institut für Biochemie, Martinsried, Germany.
Zahalka M A
Giot J F
Møller N P
Ullrich A
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