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Disease-causing mutations usually change the interacting partners of mutantproteins. In this article, we propose that the biological consequences ofmutation are directly related to the alteration of corresponding proteinprotein interaction networks (PPIN). Mutation of Huntingtin (HTT) which causesHuntington's disease (HD) and mutations to TP53 which is associated withdifferent cancers are studied as two example cases. We construct the PPIN ofwild type and mutant proteins separately and identify the structural modules ofeach of the networks. The functional role of these modules are then assessed byGene Ontology (GO) enrichment analysis for biological processes (BPs). We findthat a large number of significantly enriched (p<0.0001) GO terms in mutantPPIN were absent in the wild type PPIN indicating the gain of BPs due tomutation. Similarly some of the GO terms enriched in wild type PPIN cease toexist in the modules of mutant PPIN, representing the loss. GO terms common inmodules of mutant and wild type networks indicate both loss and gain of BPs. Wefurther assign relevant biological function(s) to each module by classifyingthe enriched GO terms associated with it. It turns out that most of thesebiological functions in HTT networks are already known to be altered in HD andthose of TP53 networks are altered in cancers. We argue that gain of BPs, andthe corresponding biological functions, are due to new interacting partnersacquired by mutant proteins. The methodology we adopt here could be applied togenetic diseases where mutations alter the ability of the protein to interactwith other proteins.

Comparison of Modules of Wild Type and Mutant Huntingtin and TP53 Protein Interaction Networks: Implications in Biological Processes and Functions