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Cytokine-specific transcriptional regulation through an IL-5Ralpha interacting protein.

Cytokine receptors consist of multiple subunits, which are often shared between different receptors, resulting in the functional redundancy sometimes observed between cytokines. The interleukin 5 ( IL-5) receptor consists of an IL-5-specific alpha-subunit (IL-5Ralpha) and a signal-transducing beta-subunit (betac) shared with the IL-3 and granulocyte-macrophage colony- stimulating factor ( GM-CSF) receptors. In this study, we sought to find a role for the cytoplasmic domain of IL-5Ralpha. We show that syntenin, a protein containing PSD-95/Discs large/zO-1 (PDZ) domains, associates with the cytoplasmic tail of the IL-5Ralpha. Syntenin was found to directly associate with the transcription factor Sox4. Association of syntenin with IL-5Ralpha was required for IL-5- mediated activation of Sox4. These studies identify a mechanism of transcriptional activation by cytokine-specific receptor subunits.[1]

References

  1. Cytokine-specific transcriptional regulation through an IL-5Ralpha interacting protein. Geijsen, N., Uings, I.J., Pals, C., Armstrong, J., McKinnon, M., Raaijmakers, J.A., Lammers, J.W., Koenderman, L., Coffer, P.J. Science (2001) [Pubmed]
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