"In signal transduction, all you need are oligomers! Dynamic signal encoding, homeostasis, bistability and more"
Homo-oligomerisation of proteins is a ubiquitous phenomenon whose exact role remains unclear in many cases. This talk will explore general dynamical mathematical models of homo-oligomerisation. I show that homo-oligomerisation on its own allows for a remarkable variety of complex dynamic and steady state regulatory behaviour such as transient overshoots or homeostatic control of monomer concentration. Post-translational modifications could make homo-oligomerisation even more versatile: by enabling pseudo-multisite modification and kinetic pseudo-cooperativity via multi-enzyme regulation, homo-oligomerisation can lead to bistability, thereby constituting a novel motif for bistable modification reactions. If modification and demodification follow different kinetic mechanisms the modification status of homo-oligomers can furthermore exhibit sustained oscillations. Due to these potential signal processing capabilities, homo-oligomerisation could play far more versatile roles in biochemical signal transduction than previously appreciated.