6533b82bfe1ef96bd128e2ef
RESEARCH PRODUCT
Cytoplasmic STAT proteins associate prior to activation
Marcin KortylewskiWerner Müller-esterlFred SchaperIris BehrmannSerge HaanPeter C. Heinrichsubject
STAT3 Transcription FactorCytoplasmCarcinoma HepatocellularMolecular Sequence DataCross ReactionsTransfectionCytoplasmic partBiochemistrystatTumor Cells CulturedAnimalsHumansProtein inhibitor of activated STATAmino Acid SequenceSTAT1PhosphorylationSTAT3MelanomaMolecular BiologySTAT4STAT6biologyInterleukin-6Liver NeoplasmsCell BiologyPrecipitin TestsMolecular biologyCell biologyDNA-Binding ProteinsSTAT1 Transcription FactorCOS CellsTrans-Activatorsbiology.proteinSTAT proteinTyrosineDimerizationResearch Articledescription
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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2000-01-25 | Biochemical Journal |