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• W2094996941 abstract "Activation of the signal transducer and activator of transcription 3 (STAT3) in response to interleukin-6 (IL-6) type cytokines involves both phosphorylation of Tyr705, which enables dimerization, nuclear translocation and DNA binding, as well as ser727 phosphorylation. Here, we describe that the 65 C-terminal amino acids of STAT3 can function as an independent transcription activation domain (TAD), particularly when a negative charge is introduced at position 727 by mutation of the serine residue into aspartate. The strong transcriptional activity of the C-terminal STAT3 Ser727Asp TAD is coupled to a constitutive association with the co-activator p300. In HepG2 cells, p300 associates with STAT3 upon IL-6 stimulation, and overexpression of p300 enhances the transcriptional activity of STAT3alpha, but not of STAT3beta or STAT3 Ser727Ala. We conclude that Ser727 phosphorylation in the C-terminal region of STAT3 is required for transactivation by association with p300." @default.
• W2094996941 created "2016-06-24" @default.
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• W2094996941 date "2001-04-19" @default.
• W2094996941 modified "2023-09-30" @default.
• W2094996941 title "Ser727-dependent transcriptional activation by association of p300 with STAT3 upon IL-6 stimulation" @default.
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• W2094996941 doi "https://doi.org/10.1016/s0014-5793(01)02354-7" @default.
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