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The spatio-temporal organization of proteins and the associated morphologicalchanges in membranes are of importance in cell signaling. Several mechanismsthat promote the aggregation of proteins at low cell surface concentrationshave been investigated in the past. We show, using Monte Carlo simulations,that the affinity of proteins for specific lipids can hasten its aggregationkinetics. The lipid membrane is modeled as a dynamically triangulated surfacewith the proteins defined as in-plane fields at the vertices. We show that,even at low protein concentrations, strong lipid-protein interactions canresult in large protein clusters indicating a route to lipid mediated signalamplification. At high protein concentrations the domains form buds similar tothat seen in lipid-lipid interaction induced phase separation. Proteininteraction induced domain budding is suppressed when proteins act asanisotropic inclusions and exhibit nematic orientational order. The kinetics ofprotein clustering and resulting conformational changes are shown to besignificantly different for the isotropic and anisotropic curvature inducingproteins.

Lipid-protein interaction induced domains: kinetics and conformational changes in multicomponent vesicles