Stat3: a STAT family member activated by tyrosine phosphorylation in response to epidermal growth factor and interleukin-6
The STAT family of proteins carries out a dual function: signal transduction and activation of
transcription. A new family member, Stat3, becomes activated through phosphorylation on
tyrosine as a DNA binding protein in response to epidermal growth factor (EGF) and
interleukin-6 (IL-6) but not interferon γ (IFN-γ). It is likely that this phosphoprotein forms
homodimers as well as heterodimers with the first described member of the STAT family,
Stat91 (renamed Stat1 α), which is activated by the IFNs and EGF. Differential activation of …
transcription. A new family member, Stat3, becomes activated through phosphorylation on
tyrosine as a DNA binding protein in response to epidermal growth factor (EGF) and
interleukin-6 (IL-6) but not interferon γ (IFN-γ). It is likely that this phosphoprotein forms
homodimers as well as heterodimers with the first described member of the STAT family,
Stat91 (renamed Stat1 α), which is activated by the IFNs and EGF. Differential activation of …
The STAT family of proteins carries out a dual function: signal transduction and activation of transcription. A new family member, Stat3, becomes activated through phosphorylation on tyrosine as a DNA binding protein in response to epidermal growth factor (EGF) and interleukin-6 (IL-6) but not interferon γ (IFN-γ). It is likely that this phosphoprotein forms homodimers as well as heterodimers with the first described member of the STAT family, Stat91 (renamed Stat1 α), which is activated by the IFNs and EGF. Differential activation of different STAT proteins in response to different ligands should help to explain specificity in nuclear signaling from the cell surface.
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