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Updated: Mar 26, 2026
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Using LEXY and LINuS Optogenetics Tools and Automated Image Analysis to Quantify Nucleocytoplasmic Transport Dynamics in Live Cells
Published on: July 22, 2025
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Optogenetic control of nuclear protein export
Dominik Niopek1,2,3, Pierre Wehler1, Julia Roensch1
1Department of Theoretical Bioinformatics, German Cancer Research Center (DKFZ), Im Neuenheimer Feld 280, 69120 Heidelberg, Germany.
Nature Communications
|February 9, 2016
Summary
Researchers developed a light-inducible nuclear export system (LEXY) for precise control over protein export. This optogenetic tool enables spatiotemporal regulation of protein localization and gene expression in eukaryotes.
Area of Science:
- Cell Biology
- Molecular Biology
- Biotechnology
Background:
- Nucleocytoplasmic transport is crucial for eukaryotic protein regulation.
- Optogenetic tools exist for nuclear protein import control.
- Spatiotemporal control of nuclear protein export remains a challenge.
Purpose of the Study:
- To develop a novel optogenetic system for light-inducible control of nuclear protein export.
- To enable precise spatiotemporal regulation of protein localization.
- To expand the optogenetic toolbox for cell and synthetic biology applications.
Main Methods:
- Development of a genetically encoded tag (LEXY) for light-inducible nuclear export.
- Creation of a LEXY variant for light-mediated inhibition of endogenous protein export via CRM1 sequestration.
- Application of LEXY to regulate synthetic repressors and human p53 transcriptional activity.
Main Results:
- Demonstrated precise spatiotemporal control over the export of tagged proteins using light.
- Showcased the ability to inhibit endogenous protein export by sequestering CRM1 receptors.
- Successfully regulated transcriptional activity of synthetic repressors and p53 with light.
Conclusions:
- LEXY provides a powerful new method for controlling nuclear export with light.
- This system offers novel applications in cell biology and synthetic biology.
- LEXY significantly advances optogenetic control over protein localization and function.
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