Abstract
It is demonstrated here that p42 MAPKinase (p42 MAPK) phosphorylates the Myristoylated Alanine-Rich C-Kinase Substrate (MARCKS) at Ser-113. In permeabilised Swiss 3T3 cells activation of protein kinase C (PKC) leads to p42 MAPK activation, but only the protein kinase C sites in MARCKS become phosphorylated and not Ser-113. The mitogen platelet-derived growth factor (PDGF) elicits the same response. These results demonstrate that while Ser-113 is a substrate for p42 MAPK in vitro and can be phosphorylated in vivo as shown by Taniguchi et al. [(1994) J. Biol. Chem. 269, 18299-18302], its phosphorylation is not subject to acute regulation by p42 MAPK in Swiss 3T3 cells.
MeSH terms
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3T3 Cells
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Amino Acid Sequence
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Animals
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Calcium-Calmodulin-Dependent Protein Kinases / metabolism*
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Cells, Cultured
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Enzyme Activation
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Intracellular Signaling Peptides and Proteins*
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Membrane Proteins*
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Mice
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Mitogen-Activated Protein Kinase 1
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Mitogens / pharmacology
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Molecular Sequence Data
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Molecular Weight
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Mutagenesis, Site-Directed
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Myristoylated Alanine-Rich C Kinase Substrate
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Peptide Fragments / chemistry
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Phosphorylation
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Platelet-Derived Growth Factor / pharmacology
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Protein Kinase C / metabolism*
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Protein-Tyrosine Kinases / metabolism*
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Proteins / metabolism*
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Recombinant Fusion Proteins / metabolism
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Serine / metabolism*
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Substrate Specificity
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Tetradecanoylphorbol Acetate / pharmacology
Substances
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Intracellular Signaling Peptides and Proteins
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Marcks protein, mouse
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Membrane Proteins
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Mitogens
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Peptide Fragments
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Platelet-Derived Growth Factor
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Proteins
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Recombinant Fusion Proteins
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Myristoylated Alanine-Rich C Kinase Substrate
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Serine
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Protein-Tyrosine Kinases
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Protein Kinase C
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Calcium-Calmodulin-Dependent Protein Kinases
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Mitogen-Activated Protein Kinase 1
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Tetradecanoylphorbol Acetate