Related Experiment Video
Updated: Apr 17, 2026
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
13.9K
The molecular basis for functional plasticity in type I interferon signaling
Gideon Schreiber1, Jacob Piehler2
1Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel.
Trends in Immunology
|February 18, 2015
Summary
Type I interferons (IFNs) play diverse roles beyond innate immunity. Quantitative analysis reveals how cells precisely control IFN signaling dynamics for efficient and safe immune responses.
Area of Science:
- Immunology
- Cell Biology
- Systems Biology
Background:
- Type I interferons (IFNs) are critical for innate immunity.
- IFNs also regulate adaptive immunity, cell proliferation, cancer surveillance, and immunomodulation.
- These diverse functions are mediated via a single cell surface receptor, influenced by ligand concentration, subtype, and activation timing.
Purpose of the Study:
- To review the functional plasticity of Type I interferon signaling.
- To explore how quantitative variations in signaling components lead to differential cellular responses.
- To understand how cells optimize IFN signaling for efficiency and safety.
Main Methods:
- Review of existing literature on Type I interferon signaling.
- Quantitative analysis of IFN signaling dynamics.
- Modeling of feedback mechanisms in IFN response pathways.
Main Results:
- IFN responses exhibit significant functional plasticity.
- Variations in ligand concentration, receptor availability, and activation kinetics modulate cellular outcomes.
- Feedback mechanisms are crucial for temporal control of IFN-driven cellular decisions.
Conclusions:
- Cellular decisions are differentially driven by precise temporal control of IFN signaling.
- Cells dynamically tune IFN signaling to balance efficacy and minimize adverse effects.
- A quantitative perspective is essential for understanding the complexity of IFN-mediated biological processes.
Related Concept Videos
01:30Inhibitors of Viral Protein Synthesis
37
Protein synthesis is indispensable for viral replication, as viruses lack the cellular machinery required for this process and must hijack the host's translational apparatus. In response, host cells deploy a critical innate immune defense involving interferons, specialized cytokines that play a central role in inhibiting viral propagation.Upon viral detection, infected cells release interferons that bind to receptors on adjacent uninfected cells, activating the JAK-STAT signaling pathway and...
37
02:26NF-kB-dependent Signaling Pathway
2.6K
2.6K
02:26NF-κB-dependent Signaling Pathway
10.9K
The transcription factor NF-κB was discovered in 1986 in the lab of Nobel laureate Professor David Baltimore, for its interaction with the immunoglobulin light chain enhancer in B-cells. After more than three decades of study, it is now evident that NF-κB regulates the expression of over 100 genes. Most of these genes play an essential role in the innate and adaptive immune responses as well as the inflammatory responses of animals.
NF-κB-dependent Signaling Mechanism
The...
NF-κB-dependent Signaling Mechanism
The...
10.9K
01:31Regulation of the Unfolded Protein Response
3.3K
Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
3.3K
01:16TGF - β Signaling Pathway
11.1K
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...
11.1K
01:20The JAK-STAT Signaling Pathway
14.2K
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...
14.2K