Glutathione peroxidase 1 is regulated by the c-Abl and Arg tyrosine kinases.
The c-Abl and Arg tyrosine kinases are activated in the cellular response to oxidative stress. The present studies demonstrate that c-Abl and Arg associate with glutathione peroxidase 1 (GPx1) and that this interaction is regulated by intracellular oxidant levels. The c-Abl and Arg SH3 domains bind directly to a proline-rich ... site in GPx1 at amino acids 132-145. GPx1 also functions as a substrate for c-Abl- and Arg-mediated phosphorylation on Tyr-96. The results further show that c-Abl and Arg stimulate GPx activity and that these kinases contribute to GPx-mediated protection of cells against oxidative stress. Our findings provide the first evidence that GPx1 is regulated by a signaling pathway that is activated in the oxidative stress response.
Mesh Terms:
Animals, Catalytic Domain, Enzyme Activation, Glutathione, Glutathione Peroxidase, Humans, Mice, Mice, Knockout, Mutation, Oxidative Stress, Protein-Tyrosine Kinases, Proto-Oncogene Proteins c-abl, Recombinant Proteins, Signal Transduction, src Homology Domains
Animals, Catalytic Domain, Enzyme Activation, Glutathione, Glutathione Peroxidase, Humans, Mice, Mice, Knockout, Mutation, Oxidative Stress, Protein-Tyrosine Kinases, Proto-Oncogene Proteins c-abl, Recombinant Proteins, Signal Transduction, src Homology Domains
J. Biol. Chem.
Date: Oct. 10, 2003
PubMed ID: 12893824
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