Biochemical and cell biology studies reveal that postsynaptic density condensates of neuronal synapses and actin cytoskeletons can directly communicate with each other in a phase separation-dependent manner.

The α1 isoform of synGAP restricts the binding of AMPA-receptors and other regulatory proteins to PSD-95, and thus regulates synaptic strength.

Deletion of one copy of the postsynaptic density protein synGAP in rodents causes an increase in the level of the AMPA receptor auxiliary protein TARP in PSDs only in females.

Maintenance of ubiquitin homeostasis is essential for proper control of the size of postsynaptic density and the growth of specialized membrane structure.

Excitatory and inhibitory postsynaptic receptors are maintained at corresponded postsynaptic sites with the different dependency of presynaptic neurons in the mature mammalian brain.

Anti-gephyrin synthetic protein binders were screened and developed to specifically and robustly detect gephyrin protein and gephyrin-interacting protein partners in the mouse brain, generating a useful tool set for neuroscience.

Autism-associated SHANK3 missense mutations result in differential protein folding, stability, and intramolecular dynamics affecting its turnover at the synapse.

Genetic and cell biological analyses reveal a new role of Drp1 in postsynaptic endocytosis during brain development beyond mitochondrial division GTPase.

Binding of ligands to PSD-95 PDZ domains induces a conformational change within the C-terminal domain module that enables differential binding to synaptic interactors.