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Keywords :
Amino Acid Sequence; Molecular Sequence Data; Phosphorylation; Precipitin Tests; STAT1 Transcription Factor; STAT3 Transcription Factor; Trans-Activators; Transfection; Tumor Cells, Cultured; Melanoma; Liver Neoplasms; Interleukin-6; Animals; COS Cells; Carcinoma, Hepatocellular; Cross Reactions; Cytoplasm; DNA-Binding Proteins; Dimerization; Humans; Tyrosine
Abstract :
[en] The commonly accepted model of STAT factor activation at the cytoplasmic part of the receptor assumes that signal transducers and activators of transcription (STATs) are recruited from a cytoplasmic pool of monomeric STAT proteins. Based on a previous observation that non-phosphorylated STAT3-Src homology 2 domains dimerize in vitro, we investigated whether the observed dimerization is of physiological relevance within the cellular context. We show that STAT1 and STAT3 are pre-associated in non-stimulated cells. Apparently, these complexes are not able to translocate into the nucleus. We provide evidence that the event of STAT activation is more complex than previously assumed.
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