@phdthesis{oai:oist.repo.nii.ac.jp:00002816,
 author = {Acharya, Saahil},
 month = {2023-12-31, 2022-10-12},
 note = {The post-synaptic structure consists of nano-scale domains that need to be precisely apposed to 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 postulated. In this thesis, I show that SynGAP forms phase-separated condensates through homophilic interactions mediated by its C-terminal coiled-coil domain as well as its intrinsically disordered region. SynGAP recruits PSD95 into these condensates, and this allows recruitment and immobilization of receptors such as Neuroligin and AMPA receptors (via TARPs), which have PDZ binding sites. I also found that oligomerization of Neuroligin and AMPA receptors anchors these receptors in SynGAP condensates. Functional oligomeric Neuroligin and AMPA receptors (GluA1 subunits linked to TARP ɤ2) are immobilized for longer durations as they diffuse through phase-separated condensates containing PSD95, compared to monomeric Neuroligin and TARP ɤ2. Together, these discoveries reveal how liquid-like assemblies of SynGAP can recruit PSD95 molecules, and retain trans-membrane receptors like Neuroligin and AMPA receptors depending on their oligomerization state.},
 school = {Okinawa Institute of Science and Technology Graduate University},
 title = {興奮性シナプスにおける、基盤構造の生成：SynGAP凝集体はPSD95を介して受容体を選択的に保持する},
 year = {}
}