Stat3 as an oncogene
Article Abstract:
A study on the signal transducers and activators of transcription (STAT) reveals that a molecule that dimerizes spontaneously, binds to DNA and activates transcription is produced due to the substitution of two cysteine residues with the C-terminal loop of the STAT3 SH2 domain. The Stat3-C molecule is found to mediate cellular transformation. Results also suggest that constitutively active Stat3 has a pharmacological potential for inducing cell death and inhibiting human cancer cell growth.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1999
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Crystal structure of a tyrosine phosphorylated STAT-1 dimer bound to DNA
Article Abstract:
The crystal structure of a DNA complex of a 67kDAa core fragment of STAT-1 was analyzed. The structure, which lacks the N-domain and the C-terminal transcriptional activation domain, reveals the STAT proteins' molecular architecture and exhibits the mechanism which allows the STAT SH2 domain control the dimer formation and DNA binding. The crystal structure helps to have adept understanding of the mechanism of transcriptional activation of STAT and the role of tyrosine phosphorylation.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1998
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Maximal activation of transcription by Stat1 and Stat3 requires both tyrosine and serine phosphorylation
Article Abstract:
Stat1 and Stat3 are latent transcriptional factors stimulated in the beginning through phosphorylation on a single tyrosine remnant caused by cytokine and growth factor occupation of cell surface receptors. It is shown that phosphorylation on a single serine in each protein is also needed for maximal transcriptional activity. Both cytokines and growth factors are competent to stimulate the serine phosphorylation of Stat1 and Stat3.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1995
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