Stats and Smads: Linking receptors to transcription. IFNg receptor activation induces protein-tyrosine kinases of the Jak family. These act on the cytoplasmic tail of the receptor, creating SH2 docking sites. STAT proteins are recruited to the membrane via their SH2 domain, and are themselves phosphorylated by the Jak kinases. Phosphorylated STATs dimerize and translocate to the nucleus where they activate transcription by binding directly to specific DNA sequences. In a somewhat anlogous manner, R-SMADs are recruited to activated TGFb receptors from their membrane anchor protein SARA. Following phosphoylation, the R-SMAD protein forms heterodimers with SMAD4 and translocates to the nucleus.
Copyright © 2001-2005 Daniele Focosi.
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