Abstract
The neuronal post-synaptic structure consists of nano-scale domains that need to be precisely apposed to the pre-synaptic neurotransmitter release sites. This exquisite assembly of post-synaptic receptors and scaffold proteins is essential for proper synaptic function. However, the biophysical mechanisms that retain receptors and scaffold proteins at the post-synapse are not well understood. Specifically, a mechanism that can induce clusters of PSD95, a key scaffold protein, at low concentrations, such as those expected before the formation of functional post-synapses, and which can induce long-term retention of post-synaptic receptors, remains to be hardly known.
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