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Cytoplasmic STAT proteins associate prior to activation
Haan, Serge; Kortylewski, M.; Behrmann, Iris et al.
2000In Biochemical Journal, 345 Pt 3, p. 417-21
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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.
Disciplines :
Biochemistry, biophysics & molecular biology
Identifiers :
UNILU:UL-ARTICLE-2008-736
Author, co-author :
Haan, Serge ;  Rheinisch - Westfälische Technische Hochschule Aachen - RWTH > Institute for Biochemistry
Kortylewski, M.
Behrmann, Iris ;  Rheinisch - Westfälische Technische Hochschule Aachen - RWTH > Institute for Biochemistry
Müller-Esterl, W.
Heinrich, P. C.
Schaper, F.
External co-authors :
yes
Language :
English
Title :
Cytoplasmic STAT proteins associate prior to activation
Publication date :
2000
Journal title :
Biochemical Journal
ISSN :
1470-8728
Publisher :
Portland Press, London, United Kingdom
Volume :
345 Pt 3
Pages :
417-21
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBilu :
since 26 April 2013

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