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Updated: Jul 10, 2026

JUMPn: A Streamlined Application for Protein Co-Expression Clustering and Network Analysis in Proteomics
Published on: October 19, 2021
Modeling protein network evolution under genome duplication and domain shuffling.
Kirill Evlampiev1, Hervé Isambert
1RNA dynamics and Biomolecular Systems Lab, CNRS UMR168, Institut Curie, Section de Recherche, 11 rue P, & M, Curie, 75005 Paris, France. kirill.evlampiev@curie.fr
Genome duplication drives protein-protein interaction network evolution, creating scale-free topologies through asymmetric gene divergence and domain conservation. This explains network structure across eukaryotes.
Area of Science:
- Evolutionary biology
- Systems biology
- Bioinformatics
Background:
- Eukaryotic genomes have undergone successive whole genome duplications.
- These duplications significantly influence the evolution of protein-protein interaction (PPI) networks.
- Previous models focused on linear network growth, not accounting for exponential duplication events.
Purpose of the Study:
- To develop and solve a mathematical model for PPI network evolution under successive genome duplications.
- To demonstrate the intrinsic link between evolutionary conservation, scale-free topology, and genome duplication.
- To investigate the role of asymmetric gene duplicate divergence in PPI network formation.
Main Methods:
- Mathematical modeling of PPI network evolution.
- Analysis of gene duplication and divergence dynamics.
- Numerical simulations using S. cerevisiae PPI network data.
Main Results:
- Genome duplication leads to exponential network growth and scale-free topology.
- Asymmetric divergence of gene duplicates, particularly at protein-binding sites, is crucial.
- PPI network topology is robust to domain shuffling and detailed evolutionary parameters.
- The model accurately reproduces large-scale features of S. cerevisiae PPI networks.
Conclusions:
- Genome duplication is a primary driver of PPI network conservation and topology across eukaryotes.
- Scale-free network properties arise from conserved protein-binding domains and asymmetric duplication/divergence.
- Domain shuffling does not disrupt the fundamental scale-free nature of PPI networks.
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