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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: Apr 15, 2026

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

Mapping biochemical networks with protein fragment complementation assays.

Ingrid Remy¹, Stephen W Michnick

¹Département de Biochimie, Université de Montréal, C.P. 6128, succursale centre-ville, Montréal, QC, Canada, H3C 3J7.

Methods in Molecular Biology (Clifton, N.J.)

|April 11, 2015

Summary

This study introduces a new method to study molecular interactions within living cells using Protein fragment Complementation Assays (PCA). This technique allows for quantitative probing of cellular biochemical pathways and macromolecular complexes.

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Last Updated: Apr 15, 2026

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

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Published on: April 15, 2011

Area of Science:

Cellular and Molecular Biology
Biochemistry
Systems Biology

Background:

Cellular biochemical pathways are dynamic, involving assembling and disassembling macromolecular complexes.
Current models of these pathways often rely on in vitro experiments, questioning their in vivo relevance.
Understanding in vivo molecular organization is crucial for comprehending cellular function.

Purpose of the Study:

To develop and present a general experimental strategy for quantitatively probing molecular interactions in intact, living cells.
To validate the in vivo organization of cellular biochemical machines.
To provide a framework for studying cellular pathways under various perturbations.

Main Methods:

Utilizes Protein fragment Complementation Assays (PCA) to detect protein interactions.
PCA couples protein interactions to enzyme refolding from cognate fragments.
Employs dihydrofolate reductase, green fluorescent protein, and β-lactamase as PCA reporters in mammalian cells.

Main Results:

Demonstrates a quantitative method for assessing protein interactions within living cells.
Establishes PCA as a viable tool for studying the dynamics of cellular biochemical pathways.
Provides protocols for applying PCA in mammalian systems.

Conclusions:

The developed PCA strategy enables accurate assessment of molecular interactions in vivo.
This approach offers insights into the true organization of cellular biochemical machines.
PCA is a versatile technique for dissecting cellular pathways and their responses to external factors.