Evolution in protein interaction networks: co-evolution, rewiring and the role of duplication

Robertson, D. L. and Lovell, S. C. (2009) Evolution in protein interaction networks: co-evolution, rewiring and the role of duplication. Biochemical Society Transactions, 37(4), pp. 768-771. (doi: 10.1042/BST0370768) (PMID:19614591)

Abstract

Molecular function is the result of proteins working together, mediated by highly specific interactions. Maintenance and change of protein interactions can thus be considered one of the main links between molecular function and mutation. As a consequence, protein interaction datasets can be used to study functional evolution directly. In terms of constraining change, the co-evolution of interacting molecules is a very subtle process. This has implications for the signal being used to predict protein-protein interactions. In terms of functional change, the 'rewiring' of interaction networks, gene duplication is critically important. Interestingly, once duplication has occurred, the genes involved have different probabilities of being retained related to how they were generated. In the present paper, we discuss some of our recent work in this area.

• Item Type: Articles
• Status: Published
• Refereed: Yes
• Glasgow Author(s) Enlighten ID: Robertson, Professor David
• Authors: Robertson, D. L., and Lovell, S. C.
• College/School: College of Medical Veterinary and Life Sciences > School of Infection & Immunity; College of Medical Veterinary and Life Sciences > School of Infection & Immunity > Centre for Virus Research
• Journal Name: Biochemical Society Transactions
• Publisher: Portland Press
• ISSN: 0300-5127
• ISSN (Online): 1470-8752