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An ELISA Based Binding and Competition Method to Rapidly Determine Ligand-receptor Interactions
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Ran binding protein 9 (RanBPM) binds IFN-λR1 in the IFN-λ signaling pathway.

Junwen Zhang1,2, Xiaojie Cong1, Jiajie Zhaoqiao1

  • 1National Laboratory of Medical Molecular Biology, Department of Biochemistry and Molecular Biology, Institute of Basic Medical Sciences, Chinese Academy of Medical Sciences & Peking Union Medical College, Beijing, 100005, China.

Science China. Life Sciences
|May 27, 2017
PubMed
Summary
This summary is machine-generated.

Researchers identified RAN-binding protein M (RanBPM) as a novel partner in the interferon-lambda (IFN-λ) signaling pathway. This interaction modulates cellular responses, revealing a new regulatory mechanism for IFN-λ activity.

Keywords:
IFN-λIFN-λR1RanBPMinteraction

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Area of Science:

  • Immunology
  • Molecular Biology
  • Cell Signaling

Background:

  • Type I interferons (IFNs) and the cytokine IFN-λ share antiviral, antiproliferative, and proapoptotic functions.
  • IFN-λ signaling is mediated by a receptor complex including IFN-λR1 and IL-10R2.
  • The precise molecular mechanisms governing IFN-λ pathways are not fully understood.

Purpose of the Study:

  • To elucidate the molecular mechanism of the IFN-λ-regulated signaling pathway.
  • To identify novel binding partners of the IFN-λ receptor subunit, IFN-λR1.
  • To investigate the functional role of identified partners in IFN-λ signaling.

Main Methods:

  • Glutathione S-transferase (GST) pull-down assays to detect protein interactions.
  • Coimmunoprecipitation experiments to confirm binding partners.
  • Analysis of cellular distribution and protein interactions upon IFN-λ1 stimulation.

Main Results:

  • RAN-binding protein M (RanBPM) was identified as a novel binding partner of IFN-λR1.
  • IFN-λ1 stimulation enhances the interaction between RanBPM and IFN-λR1, altering RanBPM's cellular distribution.
  • The RanBPM-IFN-λR1 interaction occurs independently of conserved TRAF6-binding sites.
  • RanBPM functions as a scaffolding protein, modulating the activity of IFN-stimulated response elements (ISREs).

Conclusions:

  • RanBPM plays a previously unrecognized role in the IFN-λ signaling pathway.
  • RanBPM acts as a crucial modulator, regulating the transcriptional activity downstream of IFN-λ receptor engagement.
  • This discovery provides new insights into the complexity of interferon signaling networks.