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Tip60 interacts with human interleukin-9 receptor alpha-chain

D Sliva1, Y X Zhu, S Tsai

  • 1Department of Medicine (Hematology/Oncology), Indiana University School of Medicine, and Indiana Cancer Research Institute, 1044 W. Walnut Street, R4-272, Indianapolis, Indiana 46202, USA.

Biochemical and Biophysical Research Communications
|September 16, 1999
PubMed

Insights

Researchers discovered Tip60, an HIV-1 Tat cofactor, interacts with the Interleukin-9 Receptor (IL-9R) alpha-chain. This finding suggests Tip60

Area of Science:

  • Molecular Biology
  • Cell Signaling
  • Immunology

Background:

  • Interleukin-9 (IL-9) mediates cellular functions via the IL-9 receptor (IL-9R) complex.
  • The IL-9R complex comprises the IL-9R alpha-chain and the IL-2R gamma-chain.

Purpose of the Study:

  • To identify proteins interacting with the intracellular domain of the human IL-9R alpha-chain (hIL-9Ralpha).
  • To investigate the functional implications of identified interactions in IL-9 signaling pathways.

Main Methods:

  • Modified yeast two-hybrid system to screen for interacting proteins.
  • Coimmunoprecipitation and colocalization studies to confirm interactions.
  • Amino acid mapping to identify critical interaction domains.

Main Results:

  • Tip60, a known HIV-1 Tat transcription cofactor, was identified as an interacting protein with hIL-9Ralpha.
  • Interaction between hIL-9Ralpha and Tip60 was validated through coimmunoprecipitation and colocalization.
  • Specific amino acid regions in both hIL-9Ralpha (411-423) and Tip60 (100-147) were found crucial for binding.
  • The Tip60 binding site on hIL-9Ralpha is adjacent to the Stat3 binding site.

Conclusions:

  • Tip60 directly associates with the hIL-9Ralpha membrane receptor, a novel finding.
  • Tip60 may function as a cofactor for Stat3 or an adaptor protein in IL-9 signaling.
  • This interaction could elucidate new mechanisms in IL-9 mediated cellular responses.

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