Sarah R. Metzbower

The paper maps the spatial relationships between NMDA receptor subunits and synaptic proteins, revealing a nanotopography that promotes NMDAR activation and synaptic transmission tuning.

This study uses super-resolution microscopy to show that SAP102 forms distinct nanoclusters at synapses, differing from PSD-95 in size, density, and co-localization patterns.

The paper identifies distinct molecular machineries for Ca2+ channel clustering and synaptic vesicle priming at active zones, showing that Liprin- and PTPσ specifically support priming site assembly.

The paper examines NMDA receptor activation by spontaneous neurotransmission in cultured rat hippocampal neurons, finding that GluN2B-NMDARs are primarily involved and activation varies independently of synapse size but correlates with distance from the soma.