Related Experiment Video

Updated: Jul 22, 2025

Spatial and Temporal Control of T Cell Activation Using a Photoactivatable Agonist
07:48

Spatial and Temporal Control of T Cell Activation Using a Photoactivatable Agonist

Published on: April 25, 2018

6.3K

Regulation of IL-24/IL-20R2 complex formation using photocaged tyrosines and UV light

Phuong Ngoc Pham1,2, Jiří Zahradník3,4, Lucie Kolářová1

  • 1Laboratory of Biomolecular Recognition, Institute of Biotechnology of the Czech Academy of Sciences, Vestec, Czechia.

Frontiers in Molecular Biosciences
|July 24, 2023
PubMed

Insights

Researchers developed a method to control the binding of human interleukin 24 (IL-24) to its receptor using light. This technique allows for precise regulation of IL-24 interactions, potentially aiding in autoimmune disease and cancer therapies.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Immunology

Background:

  • Human interleukin 24 (IL-24) is a key cytokine in autoimmune diseases and cancer.
  • IL-24's function relies on its interaction with membrane receptors.
  • Regulating IL-24-receptor affinity offers therapeutic and research potential.

Purpose of the Study:

  • To develop a method for photocontrolling the binding affinity between IL-24 and its receptor IL-20R2.
  • To demonstrate the feasibility of using genetic code expansion for light-inducible protein interactions.

Main Methods:

  • Utilized recombinant soluble protein variants and genetic code expansion technology.
  • Introduced non-canonical ortho-nitrobenzyl-tyrosine (NBY) residues into IL-24 and IL-20R2.
  • Employed biophysical and cell signaling assays to screen NBY residue positions.

Main Results:

  • Identified tyrosine70 of IL-20R2 as a key site for NBY installation.
  • NBY at tyrosine70 of IL-20R2 impaired heterocomplex assembly in the dark.
  • 365-nm light irradiation restored IL-24 and IL-20R2 binding by decaging NBY.

Conclusions:

  • Successfully developed a photocaged IL-20R2 variant for light-controlled IL-24 binding.
  • This approach enables spatiotemporal regulation of IL-24 signaling pathways, such as JAK/STAT phosphorylation.
  • Potential applications in basic research and therapeutic strategies for IL-24-related conditions.

Keywords:
cytokinesgenetically encoded non-canonical amino acids (ncAA)interleukin-24optobindersortho-nitrobenzyltyrosine (NBY)photocaged proteinsphotoxenoprotein engineeringprotein-protein interactions (PPI)

More Related Videos

Visualization of IL-22-expressing Lymphocytes Using Reporter Mice10:30

Visualization of IL-22-expressing Lymphocytes Using Reporter Mice

Published on: January 25, 2017

8.9K
Myeloid Innate Signaling Pathway Regulation by MALT1 Paracaspase Activity07:09

Myeloid Innate Signaling Pathway Regulation by MALT1 Paracaspase Activity

Published on: January 7, 2019

7.5K

Related Concept Videos

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...
9.0K
Receptor Downregulation in MVBs01:15

Receptor Downregulation in MVBs

Multivesicular bodies (MVBs) are mature endosomes that sort ubiquitinated proteins and then fuse with lysosomes to degrade the sorted proteins. Epidermal growth factor (EGF) and its receptor (EGFR) form a complex that can be internalized through endocytosis, sorted into an MVB, and later degraded.
The EGFR can initiate signaling pathways that  lead to cell proliferation, migration, and differentiation. Overexpression of EGFR  stimulates cells to proliferate. Excessive  EGFR...
2.1K