Related Experiment Video

Updated: Aug 10, 2026

High-throughput Quantitative Real-time RT-PCR Assay for Determining Expression Profiles of Types I and III Interferon Subtypes
10:00

High-throughput Quantitative Real-time RT-PCR Assay for Determining Expression Profiles of Types I and III Interferon Subtypes

Published on: March 24, 2015

Soluble and membrane-anchored forms of the human IFN-alpha/beta receptor

D Novick1, B Cohen, N Tal

  • 1Department of Molecular Genetics and Virology, Weizmann Institute of Science, Rehovot, Israel.

Journal of Leukocyte Biology
|May 1, 1995
PubMed

Insights

The type I interferon-alpha/beta receptor (IFN-alpha/beta R) and its soluble p40 component were characterized. This research reveals IFN-alpha/beta R

Area of Science:

  • Immunology and Virology
  • Molecular and Cellular Biology

Background:

  • The type I interferon-alpha/beta receptor (IFN-alpha/beta R) is crucial for antiviral responses.
  • Understanding the structure and function of IFN-alpha/beta R is essential for developing antiviral therapies.

Purpose of the Study:

  • To characterize the ligand-binding component of the type I human IFN-alpha/beta R and its soluble analogue, p40.
  • To investigate the role of IFN-alpha/beta R in signal transduction.

Main Methods:

  • Cloning and sequencing of cDNA encoding IFN-alpha/beta R and p40.
  • Characterization of cellular forms of IFN-alpha/beta R using immunoprecipitation with anti-p40 antibodies.
  • Analysis of tyrosine phosphorylation and association with JAK1 kinase upon ligand binding.

Main Results:

  • p40 was identified as a potent inhibitor of type I IFNs, and antibodies against p40 blocked IFN activity.
  • Cellular IFN-alpha/beta R exists in 102-kDa (major) and 51-kDa (minor) forms.
  • A 1.5-kb cDNA codes for the transmembrane 51-kDa IFN-alpha/beta R, and a 4.5-kb cDNA codes for p40.
  • IFN-alpha/beta R undergoes tyrosine phosphorylation upon ligand binding and associates with JAK1.

Conclusions:

  • The soluble p40 component is critical for type I interferon activity and represents the ligand-binding domain of IFN-alpha/beta R.
  • IFN-alpha/beta R is directly involved in signal transduction, interacting with the JAK1 tyrosine kinase.

More Related Videos

An ELISA Based Binding and Competition Method to Rapidly Determine Ligand-receptor Interactions08:40

An ELISA Based Binding and Competition Method to Rapidly Determine Ligand-receptor Interactions

Published on: March 14, 2016

Development and Validation of an Ultrasensitive Single Molecule Array Digital Enzyme-linked Immunosorbent Assay for Human Interferon-α08:26

Development and Validation of an Ultrasensitive Single Molecule Array Digital Enzyme-linked Immunosorbent Assay for Human Interferon-α

Published on: June 14, 2018

Related Concept Videos

Internal Receptors01:31

Internal Receptors

Many cellular signals are hydrophilic and therefore cannot pass through the plasma membrane. However, small or hydrophobic signaling molecules can cross the hydrophobic core of the plasma membrane and bind to internal, or intracellular, receptors that reside within the cell. Many mammalian steroid hormones use this mechanism of cell signaling, as does nitric oxide (NO) gas.
The JAK-STAT Signaling Pathway01:20

The JAK-STAT Signaling Pathway

Several cytokine receptors have tightly bound Janus kinase or JAK proteins attached at their cytosolic tail. Small signaling molecules such as cytokines, growth hormones, or prolactins bind to the cytokine receptors and initiate their dimerization. The dimerization brings the cytosolic JAKs together that trans-phosphorylate and activates each other. The activated JAKs now phosphorylate cytosolic tails of the cytokine receptors, which serve as binding sites for adaptor proteins such as  SH2...
TGF - β Signaling Pathway01:16

TGF - β Signaling Pathway

The TGF-β signaling pathway regulates cell growth, differentiation, adhesion, motility, and development. TGF-β ligands that induce TGF-β signaling are synthesized in their latent form. Several proteases or cell surface receptors such as integrins act upon the latent form, releasing the active ligand. There are three types of mammalian TGF-βs: (TGF-β1, TGF-β2, and TGF-β3) that bind as homodimers or heterodimers to TGF-β receptors. The TGF-β receptors are of three kinds RI, RII, and RIII. The RI...
Activation and Inactivation of G Proteins01:22

Activation and Inactivation of G Proteins

Heterotrimeric G proteins are guanine nucleotide-binding proteins. As the name suggests, heterotrimeric G proteins are composed of three subunits: alpha, beta, and gamma. They remain GDP-bound or GTP-bound inside the cells and switch between inactive/active states. The Gα subunit possesses the nucleotide-binding pocket that binds guanine nucleotides and switches between GDP or GTP-bound states. In contrast, the Gꞵ and Gγ subunits are always bound together with high affinity and are together...
Integrins01:10

Integrins

Animal and protozoan cells do not have cell walls to help maintain shape and provide structural stability. Instead, these eukaryotic cells secrete a sticky mass of carbohydrates and proteins into the spaces between adjacent cells. This network of proteins and molecules is called an extracellular matrix or ECM.
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...
Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...