Talk Title :
How perfect can protein interactomes be?
Date / Time / Location:
Thursday, November 12th 2009 – 6:00 pm
Room 232, Leacock Building
855 Sherbrooke Street West
Evolutionary theory tells us that biological systems need not be optimized and may very well accumulate nonfunctional elements. Mutational and demographic processes contribute to the cluttering of eukaryotic genomes and transcriptional networks with “junk” DNA and spurious DNA binding sites. Here, I question whether such a notion should be applied to protein interactomes- that is, whether these protein interactomes are expected to contain a fraction of nonselected, nonfunctional protein-protein interactions. I discuss evidence for the existence of these non-functional interactions in kinase-substrate networks from the analysis of the evolution of phosphoproteomes of mammals and fungi.