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 ![]() | |
Kortylewski, M. [> >] | |
Behrmann, Iris ![]() | |
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 |
There is no file associated with this reference.
All documents in ORBilu are protected by a user license.