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Protein Networks

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...

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Updated: Jun 9, 2025

Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay PCA in Living Cells

Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay PCA in Living Cells

Published on: March 3, 2015

Accurate and sensitive interactome profiling using a quantitative protein-fragment complementation assay.

Natalia Lazarewicz¹, Gaëlle Le Dez², Romina Cerjani²

¹University Rennes, CNRS, INSERM, Institut de Génétique et Développement de Rennes (IGDR), UMR6290, U1305, Rennes, France; Department of Genetics and Cell Physiology, Faculty of Biological Sciences, University of Wroclaw, Wroclaw, Poland.

Cell Reports Methods

|October 22, 2024

Summary

This summary is machine-generated.

Researchers developed a new method using NanoLuc Binary Technology (NanoBiT) to accurately map protein-protein interactions (PPIs). This quantitative approach enhances understanding of cellular systems by providing precise and sensitive protein interaction data.

Keywords:

CP: Systems biology Cdc53 Irc20 Met30 Nam7 NanoBiT Saccharomyces cerevisiae Upf1 budding yeast interactome protein-protein interaction

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A Protocol for the Identification of Protein-protein Interactions Based on 15N Metabolic Labeling, Immunoprecipitation, Quantitative Mass Spectrometry and Affinity Modulation

Published on: September 24, 2012

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A Protocol for the Identification of Protein-protein Interactions Based on 15N Metabolic Labeling, Immunoprecipitation, Quantitative Mass Spectrometry and Affinity Modulation

A Protocol for the Identification of Protein-protein Interactions Based on 15N Metabolic Labeling, Immunoprecipitation, Quantitative Mass Spectrometry and Affinity Modulation

Published on: September 24, 2012

Area of Science:

Molecular Biology
Systems Biology
Biochemistry

Background:

Understanding protein-protein interactions (PPIs) is crucial for elucidating cellular mechanisms.
Existing methods for mapping PPIs can be limited in precision and sensitivity.
Genome-wide PPI mapping is essential for comprehensive cellular system analysis.

Purpose of the Study:

To systematically probe protein-protein interactions using a novel quantitative assay.
To demonstrate the precision and sensitivity of NanoLuc Binary Technology (NanoBiT) for PPI mapping.
To establish a foundation for building accurate and comprehensive protein interaction maps.

Main Methods:

Construction of genome-wide yeast strain libraries.
Application of NanoLuc Binary Technology (NanoBiT), a quantitative protein-fragment complementation assay (PCA).
Investigation of known PPIs and the interactome of selected proteins (Upf1, Cdc53, Met30).

Main Results:

Demonstrated highly precise and sensitive mapping of protein-protein interactions using ratiometric NanoBiT measurements.
Successfully probed interactions of well-documented PPIs and specific proteins like Upf1, Cdc53, and Met30.
Validated NanoBiT as a robust tool for quantitative PPI analysis.

Conclusions:

NanoBiT enables accurate and sensitive mapping of protein-protein interactions.
This technology provides a foundation for assembling comprehensive protein interaction maps.
NanoBiT facilitates deeper functional investigations of protein interactions within cellular systems.