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.
Mesh Terms:
Animals, B-Lymphocytes, COS Cells, Carrier Proteins, Cell Line, Genes, Reporter, High Mobility Group Proteins, Humans, Interleukin-5, Intracellular Signaling Peptides and Proteins, Membrane Proteins, Mice, Mitogen-Activated Protein Kinases, Phosphorylation, Point Mutation, Protein Structure, Tertiary, Receptors, Interleukin, Receptors, Interleukin-5, Recombinant Fusion Proteins, SOXC Transcription Factors, Sequence Deletion, Signal Transduction, Syntenins, Trans-Activators, Transcriptional Activation, Transfection, Two-Hybrid System Techniques
Science
Date: Aug. 10, 2001
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