Protein intrinsic disorder and network connectivity. The case of 14-3-3 proteins.

The understanding of networks is a common goal of an unprecedented array of<br/>traditional disciplines. One of the network properties most influenced by the<br/>structural contents of its nodes is the inter-connectivity. Recent studies in which<br/>structural information was included into the topological analysis of protein<br/>networks revealed that the content of intrinsic disorder in the nodes could<br/>modulate the network topology, rewire networks and change their inter-<br/>connectivity, which is defined by its clustering coefficient. Here, we review the<br/>role of intrinsic disorder present in the partners of the highly conserved 14-3-3<br/>protein family on its interaction networks. The 14-3-3s are phospho-<br/>serine/threonine binding proteins that have strong influence in the regulation of<br/>metabolism and signal transduction networks. Intrinsic disorder increases the<br/>clustering coefficients, namely the inter-connectivity of the nodes within each<br/>14-3-3 paralog networks. We also review two new ideas to measure intrinsic<br/>disorder independently of the primary sequence of proteins, a thermodynamic<br/>model and a method that uses protein structures and their solvent<br/>environment. This new methods could be useful to explain unsolved questions<br/>about versatility and fixation of intrinsic disorder through evolution. The<br/>relation between the intrinsic disorder and network topologies could be an<br/>interesting model to investigate new implicitness of the graph theory into<br/>biology.<br/>

Abstract licence: CC BY

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