Photoactivatable Proteins

Photoactivatable proteins are engineered or naturally light-responsive proteins that remain inactive until illumination triggers a reversible or irreversible change in their structure or function. Light-sensitive domains or caged chemical groups absorb specific wavelengths, causing conformational rearrangements, bond cleavage, or fluorophore activation that exposes an active site or produces a detectable signal. In developmental biology, these proteins provide precise spatial and temporal control over signaling, gene expression, protein activity, and cell labeling in living tissues. Researchers use them to track cell lineages, analyze morphogen gradients, investigate cell migration, and connect brief molecular events with longer-term patterns of tissue formation.

Photoactivatable Proteins - Related Videos

Research

JoVE EoE - Immunodiagnostics

Evaluation of Controlled T Cell Activation with a Photoactivatable Peptide MHC

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2025

This video demonstrates a method of decaging a photoactivatable peptide-major histocompatibility complex using UV irradiation. The decaging process exposes the native peptide sequence, enabling precise T cell activation.

Imaging the Intracellular Trafficking of APP with Photoactivatable GFP

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Cited by 6 •

2015

While the transport of cell surface proteins is relatively easily studied, visualizing the trafficking of intracellular proteins is much more difficult. Here, we use constructs incorporating photoactivatable GFP and demonstrate a method to accurately follow the amyloid precursor protein from the Golgi apparatus to down-stream compartments and follow its clearance.

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

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Cited by 5 •

2018

This protocol describes an imaging-based method to activate T lymphocytes using photoactivatable peptide-MHC, enabling precise spatiotemporal control of T cell activation.

Research

JoVE Journal - Biology
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Green Fluorescent Protein-based Expression Screening of Membrane Proteins in Escherichia coli

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Cited by 34 •

2015

A streamlined approach to screening for the expression of recombinant membrane proteins in Escherichia coli based on fusion to green fluorescent protein is presented.

Research

JoVE Journal - Biochemistry
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Rapid Assessment of Membrane Protein Quality by Fluorescent Size Exclusion Chromatography

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Cited by 2 •

2023

The present protocol describes a procedure to perform fluorescent size exclusion chromatography (FSEC) on membrane proteins to assess their quality for downstream functional and structural analysis. Representative FSEC results collected for several G-protein coupled receptors (GPCRs) under detergent-solubilized and detergent-free conditions are presented.

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