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Interaction of STAT6 with its co-activator SRC-1/NCoA-1 is regulated by dephosphorylation of the latter via PP2A

Tobias Münz1, Claudia M Litterst, Edith Pfitzner

  • 1Friedrich-Schiller-University, Jena Institute of Biochemistry and Biophysics, Center for Molecular Biomedicine, Hans-Knöll-Str 2, 07743 Jena, Germany.

Nucleic Acids Research
|December 15, 2010
PubMed

Insights

The phosphatase PP2A dephosphorylates NCoA-1, enabling STAT6 interaction and IL-4 gene activation. This process is linked to cell cycle progression, integrating gene regulation with cellular growth.

Area of Science:

  • Molecular Biology
  • Cellular Signaling
  • Gene Regulation

Background:

  • Signal-regulated gene expression is crucial for cellular responses.
  • STAT6 mediates Interleukin-4 (IL-4) stimulated gene activation by recruiting co-activator complexes.
  • NCoA-1 is a co-activator that interacts with STAT6 via its PAS-B domain and an LXXLL motif.

Purpose of the Study:

  • To investigate the regulation of the NCoA-1/STAT6 interaction.
  • To determine the role of NCoA-1 phosphorylation in STAT6-mediated gene activation.
  • To elucidate the connection between transcriptional regulation and cell cycle progression.

Main Methods:

  • Investigated NCoA-1/STAT6 interaction dynamics.
  • Utilized phosphatase and kinase inhibition assays.
  • Examined NCoA-1 phosphorylation during cell cycle arrest.

Main Results:

  • NCoA-1 dephosphorylation by PP2A is essential for STAT6 interaction and IL-4-dependent gene activation.
  • Simultaneous inhibition of phosphatases and cyclin-dependent kinases restored NCoA-1/STAT6 interaction.
  • NCoA-1 phosphorylation increases upon cell cycle arrest at G1/S phase.

Conclusions:

  • The NCoA-1/STAT6 interaction is dynamically regulated by PP2A and cyclin-dependent kinases.
  • This regulation integrates STAT6 transcriptional activity with cell cycle progression.
  • Phosphorylation state of NCoA-1 is a key regulatory mechanism for IL-4 signaling.

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