Green-Light-Induced Inactivation of Receptor Signaling Using Cobalamin-Binding Domains
Stephanie Kainrath1, Manuela Stadler2, Eva Reichhart1
1Synthetic Physiology, Institute of Science and Technology Austria (IST Austria), Am Campus 1, 3400, Klosterneuburg, Austria.
Angewandte Chemie (International Ed. in English)
|March 21, 2017
Summary
Researchers developed a new optogenetic tool using green light to control protein interactions. This method allows for precise manipulation of cell signaling and biological processes, expanding the possibilities for multichromatic experiments.
Area of Science:
- Molecular Biology
- Biochemistry
- Cell Biology
Background:
- Optogenetics and photopharmacology offer precise control over biological processes.
- Existing optogenetic tools lack sensitivity to green light for breaking protein complexes, limiting multichromatic experiments.
Purpose of the Study:
- To develop novel green-light-sensitive optogenetic tools for controlling protein interactions.
- To enable the disruption of protein complexes using green light for advanced biological research.
Main Methods:
- Repurposed cobalamin (vitamin B12) binding domains from bacterial CarH transcription factors.
- Engineered fibroblast growth factor receptor 1 (FGFR1) fusions with these domains.
- Tested in cultured cells and zebrafish embryos to assess light-induced dissociation and signaling control.
Main Results:
- Observed light-induced dissociation of cobalamin-binding domains in cultured cells.
- Demonstrated green-light-mediated inactivation of FGFR1 signaling.
- Showed control over aberrant fibroblast growth factor signaling in developing zebrafish embryos.
Conclusions:
- Developed a novel green-light-induced receptor dissociation system.
- Expanded the optogenetic toolbox with light-inactivated receptors.
- Enabled precise spatiotemporal control over biological processes using green light.
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