Oxidative stress activates both Src-kinases and their negative regulator Csk and induces phosphorylation of two targeting proteins for Csk: caveolin-1 and paxillin.

@article{Cao2004OxidativeSA,
  title={Oxidative stress activates both Src-kinases and their negative regulator Csk and induces phosphorylation of two targeting proteins for Csk: caveolin-1 and paxillin.},
  author={Haiming Cao and Amy R. Sanguinetti and Cynthia Corley Mastick},
  journal={Experimental cell research},
  year={2004},
  volume={294 1},
  pages={159-71}
}
Csk negatively regulates Src family kinases (SFKs). In lymphocytes, Csk is constitutively active, and is transiently inactivated in response to extracellular stimuli, allowing activation of SFKs. In contrast, both SFKs and Csk were inactive in unstimulated mouse embryonic fibroblasts, and both were activated in response to oxidative stress. Csk modulated the oxidative stress-induced, but not the basal SFK activity in these cells. These data indicate that Csk may be more important for the return… CONTINUE READING

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