Abstract
A MAP kinase homologue, termed the reactivating kinase (RK), lies in a signalling pathway which mediates cellular responses to stress. Here we demonstrate that the stress-induced activation of the RK in human KB cells is accompanied by the phosphorylation of Thr-180 and Tyr-182, and that the phosphorylation of both residues is required for the activation of this enzyme.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Binding Sites
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Cell Line
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DNA, Complementary / genetics
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Enzyme Activation
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Humans
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Intracellular Signaling Peptides and Proteins
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Molecular Sequence Data
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Mutation
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Peptide Fragments / chemistry
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Peptide Fragments / genetics
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Phosphorylation
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Protein Kinases*
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Protein Serine-Threonine Kinases / chemistry
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Protein Serine-Threonine Kinases / genetics
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Protein Serine-Threonine Kinases / metabolism*
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Protein-Tyrosine Kinases / chemistry
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Protein-Tyrosine Kinases / genetics
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Protein-Tyrosine Kinases / metabolism*
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Xenopus
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Xenopus Proteins*
Substances
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DNA, Complementary
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Intracellular Signaling Peptides and Proteins
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Peptide Fragments
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Xenopus Proteins
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Protein Kinases
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MAP-kinase-activated kinase 2
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Mpk2 protein, Xenopus
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Protein-Tyrosine Kinases
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Protein Serine-Threonine Kinases