New activation modus of STAT3: a tyrosine-less region of the interleukin-22 receptor recruits STAT3 by interacting with its coiled-coil domain.

@article{Dumoutier2009NewAM,
  title={New activation modus of STAT3: a tyrosine-less region of the interleukin-22 receptor recruits STAT3 by interacting with its coiled-coil domain.},
  author={Laure Dumoutier and Carole de Meester and Jan Tavernier and Jean-Christophe Renauld},
  journal={The Journal of biological chemistry},
  year={2009},
  volume={284 39},
  pages={26377-84}
}
Activation of STAT proteins by cytokines is initiated by their Src homology 2 domain-mediated association with phosphotyrosine residues from the cytoplasmic domain of a receptor. Here, we show that the C terminus of the interleukin-22 receptor (IL-22R) recruits in a tyrosine-independent manner the coiled-coil domain of STAT3. Mutation of all IL-22R cytoplasmic tyrosines did not abolish activation of STAT3, in contrast to that of STAT1 and STAT5. Coimmunoprecipitation and glutathione S… CONTINUE READING

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STAT3 Recruitment and Phosphorylation 26384 JOURNAL OF BIOLOGICAL CHEMISTRY VOLUME

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