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Related Experiment Videos

Cytoplasmic STAT proteins associate prior to activation.

S Haan1, M Kortylewski, I Behrmann

  • 1Institut für Biochemie, Rheinisch-Westfälische Technische Hochschule Aachen, Pauwelsstrasse 30, D-52074 Aachen, Germany.

The Biochemical Journal
|January 22, 2000
PubMed
Summary

Signal transducers and activators of transcription (STATs) exist as pre-associated complexes in non-stimulated cells. These STAT1 and STAT3 complexes do not translocate to the nucleus, indicating a more complex activation process than previously understood.

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Area of Science:

  • Cellular signaling pathways
  • Molecular biology
  • Signal transduction

Background:

  • The canonical model posits that signal transducers and activators of transcription (STATs) are recruited as monomers from the cytoplasm to activated receptors.
  • Previous in vitro studies indicated that non-phosphorylated STAT3-Src homology 2 domains can dimerize.

Purpose of the Study:

  • To investigate the physiological relevance of STAT dimerization within the cellular context.
  • To determine if STAT proteins exist as pre-associated complexes in non-stimulated cells.

Main Methods:

  • Cellular assays to examine STAT protein interactions.
  • Investigating the localization and translocation of STAT complexes.

Main Results:

Related Experiment Videos

  • Signal transducers and activators of transcription (STATs), specifically STAT1 and STAT3, are found to be pre-associated in non-stimulated cells.
  • These pre-associated STAT complexes are unable to translocate into the nucleus in their non-phosphorylated state.

Conclusions:

  • The current model of STAT activation requires revision.
  • STAT activation is a more intricate process than the simple recruitment of monomeric units.
  • Pre-association of STAT proteins suggests alternative regulatory mechanisms prior to receptor stimulation.