Reference : Cytoplasmic STAT proteins associate prior to activation
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/10993/796
Cytoplasmic STAT proteins associate prior to activation
English
Haan, Serge mailto [Rheinisch - Westfälische Technische Hochschule Aachen - RWTH > Institute for Biochemistry]
Kortylewski, M. [> >]
Behrmann, Iris mailto [Rheinisch - Westfälische Technische Hochschule Aachen - RWTH > Institute for Biochemistry]
Müller-Esterl, W. [> >]
Heinrich, P. C. [> >]
Schaper, F. [> >]
2000
Biochemical Journal
Portland Press
345 Pt 3
417-21
Yes (verified by ORBilu)
International
0264-6021
1470-8728
London
United Kingdom
[en] 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
[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.
http://hdl.handle.net/10993/796

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