FEBS Letters | |
Ser727‐dependent transcriptional activation by association of p300 with STAT3 upon IL‐6 stimulation | |
Kruijer, Wiebe1  Schuringa, Jan-Jacob1  Vellenga, Edo2  Schepers, Hein1  | |
[1] Department of Genetics, Biological Center, Kerklaan 30, 9751 NN Haren, The Netherlands;Department of Hematology, University Hospital Groningen, 9700 RB Groningen, The Netherlands | |
关键词: Interleukin-6; Signal transducer and activator of transcription 3; Ser727 phosphorylation; Transactivation; p300; IL-6; interleukin-6; STAT3; signal transducer and activator of transcription 3; TAD; transcription activation domain; CBP; CREB binding protein; | |
DOI : 10.1016/S0014-5793(01)02354-7 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
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 STAT3α, but not of STAT3β or STAT3 Ser727Ala. We conclude that Ser727 phosphorylation in the C-terminal region of STAT3 is required for transactivation by association with p300.
【 授权许可】
Unknown
【 预 览 】
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