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Protein-protein Interfaces

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...

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Updated: Nov 14, 2025

Luciferase Complementation Imaging Assay in Nicotiana benthamiana Leaves for Transiently Determining Protein-protein Interaction Dynamics

Luciferase Complementation Imaging Assay in Nicotiana benthamiana Leaves for Transiently Determining Protein-protein Interaction Dynamics

Published on: November 20, 2017

Luciferase Controlled Protein Interactions.

Dalu Chang¹, Suihan Feng², Vladimir Girik²

¹School of Chemistry and Biochemistry, Department of Organic Chemistry, NCCR Chemical Biology, Faculty of Science, University of Geneva, 30 quai Ernest-Ansermet, Geneva 12004, Switzerland.

Journal of the American Chemical Society

|March 8, 2021

Summary

This summary is machine-generated.

Researchers developed a novel bioluminescence-triggered system for controlling protein interactions and cellular localization. This new method overcomes limitations of light-based systems, enabling precise regulation of cellular processes like lipid metabolism.

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Last Updated: Nov 14, 2025

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Investigating Protein-protein Interactions in Live Cells Using Bioluminescence Resonance Energy Transfer

Investigating Protein-protein Interactions in Live Cells Using Bioluminescence Resonance Energy Transfer

Published on: May 26, 2014

Area of Science:

Molecular Biology
Cell Biology
Biochemistry

Background:

Protein-protein interactions (PPIs) and protein trafficking are crucial for cellular regulation.
Chemically induced dimerization (CID) systems offer control over PPIs and protein localization.
Existing light-activated CID systems face challenges with light delivery and phototoxicity.

Purpose of the Study:

To design and validate a novel chemically induced dimerization (CID) system triggered by bioluminescence, overcoming limitations of light-dependent systems.
To demonstrate spatiotemporal control over protein interactions and localization using the bioluminescence-triggered CID system.
To investigate the impact of transiently activating the PI3K/mTOR pathway on lipid metabolism.

Main Methods:

Development of a bioluminescence-triggered CID system using self-labeling proteins and photocaged ligands.
Validation of protein dimerization kinetics and induced protein localization changes (nuclear and plasma membrane).
Transient activation of the PI3K/mTOR pathway and subsequent lipidomic analysis.

Main Results:

The bioluminescence-triggered CID system demonstrated fast dimerization kinetics.
Successful induction of target protein translocation to and from the nucleus and plasma membrane.
Observed effects on lipid synthesis and metabolism following PI3K/mTOR pathway activation.

Conclusions:

Bioluminescence-triggered CID offers a light-independent alternative for controlling protein interactions and localization.
This technology provides precise spatiotemporal control for studying cellular signaling pathways.
The system enables investigation of pathway activation effects on metabolic processes like lipid synthesis.