The WD motif-containing protein RACK-1 functions as a scaffold protein within the type I IFN receptor-signaling complex.

The WD repeat-containing protein receptor for activated protein kinase C (RACK)-1 has been linked to a variety of signaling systems including protein kinase C, growth factors, and IFNs. In the IFN system, RACK-1 functions as an adaptor recruiting the transcription factor STAT1 to the receptor complex. However, RACK-1 should play ...
a broader role in type I IFN signaling because mutation of the RACK-1 binding site in the IFN-alpha receptor 2/beta subunit of the type I IFN receptor abrogates not only STAT1, but also STAT2, activation. In this study, we demonstrate that RACK-1 serves as a scaffold protein for a multiprotein complex that includes the IFN-alpha receptor 2/beta-chain of the receptor, STAT1, Janus kinase 1, and tyrosine kinase 2. In vitro data further suggest that within this complex tyrosine kinase 2 is the tyrosine kinase responsible for the phosphorylation of STAT1. Finally, we provide evidence that RACK-1 may also serve as a scaffold protein in other cytokine systems such as IL-2, IL-4, and erythropoietin.
Mesh Terms:
Amino Acid Motifs, Animals, Cell Line, Tumor, DNA-Binding Proteins, Humans, Interferon Type I, Janus Kinase 1, Membrane Proteins, Mice, Nuclear Matrix-Associated Proteins, Phosphorylation, Protein Subunits, Protein-Tyrosine Kinases, Proteins, Receptor, Interferon alpha-beta, Receptors, Cell Surface, Receptors, Cytokine, Receptors, Interferon, Repetitive Sequences, Amino Acid, STAT1 Transcription Factor, Signal Transduction, TYK2 Kinase, Trans-Activators
J. Immunol.
Date: Sep. 15, 2003
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