New Activation Modus of STAT3 A TYROSINE-LESS REGION OF THE INTERLEUKIN-22 RECEPTOR RECRUITS STAT3 BY INTERACTING WITH ITS COILED-COIL DOMAIN
(2009) Journal of Biological Chemistry — Vol. 284, n° 39, p. 26377-26384 (2009)
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- 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-transferase pulldown experiments showed that the coiled-coil domain of STAT3 is constitutively associated with the C-terminal part of IL-22R, and a chimeric STAT3-STAT5 protein containing the coiled-coil domain of STAT3 could be activated by this tyrosine-independent mechanism. Deletion of the C-terminal part of IL-22R dramatically decreased its ability to activate STAT3 and to mediate IL-22 activity in cell lines, demonstrating that preassociation of STAT3 with this cytokine receptor, independent from the interaction between the Src homology 2 domain and phosphotyrosines, is required for its full activity.
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Dumoutier, L., de Meester, C., Tavernier, J., & Renauld, J.-C. (2009). New Activation Modus of STAT3 A TYROSINE-LESS REGION OF THE INTERLEUKIN-22 RECEPTOR RECRUITS STAT3 BY INTERACTING WITH ITS COILED-COIL DOMAIN. Journal of Biological Chemistry, 284(39), 26377-26384. https://doi.org/10.1074/jbc.M109.007955 (Original work published 2009)