Abstract
Stress-activated protein kinases are MAP kinase homologues that are activated by cellular stresses, bacterial endotoxin and inflammatory cytokines. They are activated by a dual threonine/tyrosine phosphorylation within a TPY sequence in the case of stress-activated protein kinase-1 and its isoforms (also called JNKs) or a TGY sequence in the case of stress-activated protein kinase-2 and its isoforms (also called p38, p40, RK, CSBPs, XMpk2 and Mxi2). Here we report the cloning and sequencing of a new protein kinase from rat with a TGY sequence in the activation domain. This stress-activated protein kinase-3 is 60% identical to mouse stress-activated protein kinase-2 and 45% identical to HOG1 from Saccharomyces cerevisiae. Transcripts encoding stress-activated protein kinase-3 are widely expressed, with high levels in skeletal muscle.
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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Amino Acid Sequence
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Animals
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Base Sequence
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Brain / enzymology*
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Calcium-Calmodulin-Dependent Protein Kinases / biosynthesis
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Calcium-Calmodulin-Dependent Protein Kinases / chemistry
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Cloning, Molecular
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Conserved Sequence
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DNA Primers
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DNA, Complementary
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Enzyme Activation
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Gene Library
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Isoenzymes / biosynthesis
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Isoenzymes / chemistry*
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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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Organ Specificity
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Polymerase Chain Reaction
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Protein Kinases / biosynthesis*
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Protein Kinases / chemistry*
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Rats
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Saccharomyces cerevisiae / enzymology
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Sequence Homology, Amino Acid
Substances
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DNA Primers
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DNA, Complementary
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Isoenzymes
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Protein Kinases
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Mitogen-Activated Protein Kinase 12
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Calcium-Calmodulin-Dependent Protein Kinases
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Mitogen-Activated Protein Kinases