Ran binding protein 9 (RanBPM) binds IFN-λR1 in the IFN-λ signaling pathway.
Like the type I interferons (IFNs), the recently discovered cytokine IFN-λ displays antiviral, antiproliferative, and proapoptotic activities, mediated by a heterodimeric IFN-λ receptor complex composed of a unique IFN-λR1 chain and the IL-10R2 chain. However, the molecular mechanism of the IFN-λ-regulated pathway remains unclear. In this study, we newly identified ... RAN-binding protein M (RanBPM) as a binding partner of IFN-λR1. The interaction between RanBPM and IFN-λR1 was identified with a glutathione S-transferase pull-down assay and coimmunoprecipitation experiments. IFN-λ1 stimulates this interaction and affects the cellular distribution of RanBPM. However, the interaction between RanBPM and IFN-λR1 does not correlate with their conserved TRAF6-binding sites. Furthermore, we also found that RanBPM is a scaffolding protein with a modulatory function that regulates the activities of IFN-stimulated response elements. Therefore, RanBPM plays a novel role in the IFN-λ-regulated signaling pathway.
Mesh Terms:
Adaptor Proteins, Signal Transducing, Binding Sites, Cell Line, Transformed, Cell Line, Tumor, Cytoskeletal Proteins, HEK293 Cells, Humans, Immunoprecipitation, Interferon-Stimulated Gene Factor 3, gamma Subunit, Interleukins, Nuclear Proteins, Protein Binding, Receptors, Cytokine, Response Elements, Signal Transduction, TNF Receptor-Associated Factor 6, Ubiquitination
Adaptor Proteins, Signal Transducing, Binding Sites, Cell Line, Transformed, Cell Line, Tumor, Cytoskeletal Proteins, HEK293 Cells, Humans, Immunoprecipitation, Interferon-Stimulated Gene Factor 3, gamma Subunit, Interleukins, Nuclear Proteins, Protein Binding, Receptors, Cytokine, Response Elements, Signal Transduction, TNF Receptor-Associated Factor 6, Ubiquitination
Sci China Life Sci
Date: Sep. 01, 2017
PubMed ID: 28547582
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