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Related Experiment Video

Updated: Jan 21, 2026

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

Published on: October 4, 2024

Reversible optogenetic control of protein function and localization.

Daniel Z Wu¹, Rachel M Lackner¹, Chanat Aonbangkhen¹

¹Roy and Diana Vagelos Laboratories, Department of Chemistry, University of Pennsylvania, Philadelphia, PA, United States.

Methods in Enzymology

|August 3, 2019

Summary

This summary is machine-generated.

This study introduces a novel optogenetic platform for reversible control of protein interactions using light. This technology precisely manipulates cellular processes like protein transport and mitosis with spatiotemporal resolution.

Keywords:

Chemically inducible dimerization Localization Mitosis Optogenetics Photoactivation Protein transport Reversible

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Area of Science:

Cell Biology
Molecular Biology
Optogenetics

Background:

Protein-protein interactions are crucial for cellular functions, requiring precise spatiotemporal control.
Photoactivatable chemically inducible dimerization (pCID) offers light-based manipulation of these interactions.
Existing pCID systems provide opportunities for enhanced control over biological processes.

Purpose of the Study:

To develop and describe an optogenetic platform for reversible control of protein dimerization.
To demonstrate precise spatiotemporal manipulation of cellular functions using light-activated protein interactions.

Main Methods:

Utilized an optogenetic platform enabling reversible control of genetically tagged protein dimerization.
Employed orthogonal wavelengths of light for photoactivation and photo-reversal.
Applied the system to control protein localization, transport, and spindle assembly checkpoint activity during mitosis.

Main Results:

Successfully demonstrated photoactivation and photo-reversal of protein localization and transport.
Showcased manipulation of mitosis by controlling the spindle assembly checkpoint through protein recruitment and release from kinetochores.
Validated the platform's ability to provide reversible, light-induced dimerization with molecular specificity.

Conclusions:

The developed optogenetic platform offers precise, reversible control over protein dimerization using light.
This technology enables fine-tuned manipulation of cellular dynamics, including protein transport and cell division.
The system holds significant potential for advancing research in cell biology and molecular dynamics.