Phase Separation of Intracellular Proteins Influences Synaptic Bistability

Scaffold protein phase separation at model membranes creates an attractive interaction between otherwise repulsive receptors, enhancing receptor clustering as scaffold condensation increases.

• Why it matters: Synaptic bistability is linked to receptor cluster nucleation, but the biophysical mechanism of inter-receptor attraction is unclear, especially when scaffold proteins can undergo phase transitions.
• What they did: Using Langevin dynamics simulations with coarse-grained scaffold macromolecules and interacting membrane receptors, the authors varied receptor number and scaffold phase behavior, including two scaffold types and their interaction strength.
• The result: Receptor clustering propensity increases with scaffold condensation, and clustering can be reduced when scaffold macromolecules co-phase separate, highlighting competing interactions that reshape condensed-phase organization.

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