Specificity and stability in topology of protein networks

TL;DR

This paper investigates the topological properties of protein interaction and regulatory networks, revealing patterns that suppress highly connected node interactions and promote modularity, which enhances cellular robustness.

Contribution

It provides a quantitative analysis of network topology, showing how specific connectivity patterns influence cellular function and robustness, a novel insight into molecular network organization.

Findings

Links between highly connected proteins are suppressed.

Links between highly and low-connected proteins are favored.

Network topology promotes modularity and robustness.

Abstract

Molecular networks guide the biochemistry of a living cell on multiple levels: its metabolic and signalling pathways are shaped by the network of interacting proteins, whose production, in turn, is controlled by the genetic regulatory network. To address topological properties of these two networks we quantify correlations between connectivities of interacting nodes and compare them to a null model of a network, in which al links were randomly rewired. We find that for both interaction and regulatory networks, links between highly connected proteins are systematically suppressed, while those between a highly-connected and low-connected pairs of proteins are favored. This effect decreases the likelihood of cross talk between different functional modules of the cell, and increases the overall robustness of a network by localizing effects of deleterious perturbations.