title: Nanodomains in Biomembranes with Recycling.
abstract: Cell membranes are out of thermodynamic equilibrium notably because of membrane recycling, i.e., active exchange of material with the cytosol. We propose an analytically tractable model of biomembrane predicting the effects of recycling on the size of protein nanodomains also called protein clusters. The model includes a short-range attraction between proteins and a weaker long-range repulsion which ensures the existence of so-called cluster phases in equilibrium, where monomeric proteins coexist with finite-size domains. Our main finding is that, when taking recycling into account, the typical cluster size at steady state increases logarithmically with the recycling rate at fixed protein concentration. Using physically realistic model parameters, the predicted 2-fold increase due to recycling in living cells is most likely experimentally measurable with the help of super-resolution microscopy.
authors.affiliation: Laboratoire de Physique Théorique, IRSAMC, Université de Toulouse, CNRS, UPS, 118 route de Narbonne, F-31062 Toulouse, France.
authors.forename: Mareike
authors.initials: M
authors.lastname: Berger
authors.affiliation: Laboratoire de Physique Théorique, IRSAMC, Université de Toulouse, CNRS, UPS, 118 route de Narbonne, F-31062 Toulouse, France.
authors.forename: Manoel
authors.initials: M
authors.lastname: Manghi
authors.affiliation: Laboratoire de Physique Théorique, IRSAMC, Université de Toulouse, CNRS, UPS, 118 route de Narbonne, F-31062 Toulouse, France.
authors.forename: Nicolas
authors.initials: N
authors.lastname: Destainville
mesh_terms: D002462:Cell Membrane / Q000737:chemistry / Q000378:metabolism*; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism; D008962:Models, Theoretical; D049329:Nanostructures / Q000737:chemistry*; D013816:Thermodynamics
chemical_list: D008565:Membrane Proteins