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Self-assembly of protein monomers into distinct membrane protein oligomersprovides a general mechanism for diversity in the molecular architectures, andresulting biological functions, of membrane proteins. We develop a generalphysical framework describing the thermodynamic competition between differentoligomeric states of membrane proteins. Using the mechanosensitive channel oflarge conductance as a model system, we show how the dominant oligomeric statesof membrane proteins emerge from the interplay of protein concentration in thecell membrane, protein-induced lipid bilayer deformations, and directmonomer-monomer interactions. Our results suggest general physical mechanismsand principles underlying regulation of protein function via control ofmembrane protein oligomeric state.

Thermodynamic competition between membrane protein oligomeric states