Stochastic self-assembly of reaction-diffusion patterns in synaptic membranes

Synaptic receptor and scaffold molecules self-assemble into membrane protein domains, which play an important role in signal transmission across chemical synapses. Experiment and theory have shown that the formation of receptor-scaffold domains of the characteristic size observed in nerve cells can be understood from the receptor and scaffold reaction and diffusion processes suggested by experiments. We employ here kinetic Monte Carlo (KMC) simulations to explore the self-assembly of synaptic receptor-scaffold domains in a stochastic lattice model of receptor and scaffold reaction-diffusion dynamics. For reaction and diffusion rates within the ranges of values suggested by experiments we find, in agreement with previous mean-field calculations, self-assembly of receptor-scaffold domains of a size similar to that observed in experiments. Comparisons between the results of our KMC simulations and mean-field solutions suggest that the intrinsic noise associated with receptor and scaffold reaction and diffusion processes accelerates the self-assembly of receptor-scaffold domains, and confers increased robustness to domain formation. In agreement with experimental observations, our KMC simulations yield a prevalence of scaffolds over receptors in receptor-scaffold domains. Our KMC simulations show that receptor and scaffold reaction-diffusion dynamics can inherently give rise to plasticity in the overall properties of receptor-scaffold domains, which may be utilized by nerve cells to regulate the receptor number at chemical synapses.

Automated summary

Experimental and theoretical studies have shown that synaptic receptor and scaffold molecules spontaneously assemble into membrane protein domains that facilitate signal transmission across chemical synapses. Using kinetic Monte Carlo simulations, it has been demonstrated that the reaction-diffusion dynamics of receptor and scaffold molecules can lead to the self-assembly of domains similar to those observed in nerve cells. The intrinsic noise associated with these processes accelerates the self-assembly of receptor-scaffold domains and contributes to their robustness.