Molecular basis of glutamatergic synapse function in different neuron populations  

From electrophysiological experiments it is known that glutamatergic (excitatory) synapses in different neuronal populations have different properties and "rules" for plasticity. However, the molecular basis supporting these differences is poorly understood. Our lab is particularly interested in the composition, and regulation, of glutamatergic synapses located within GABAergic (inhibitory) interneurons. We seek to identify and evaluate proteins that are enriched at glutamatergic synapses in inhibitory interneurons. One such protein is Btbd11, for which we recently published a paper.   
In the long term, we believe this research could uncover new ways to manipulate glutamatergic synapse in a cell type-specific manner--to help regulate neuronal circuit function.     

Manipulating liquid-liquid phase separation at the synapse

Liquid-liquid phase separation (LLPS) or biomolecular condensation describes the process through which molecules can de-mix to form "liquids within liquids". In biological contexts, this leads to a novel class of membrane-less organelles that can aid the organisation of intracellular space. Interestingly, many synaptic proteins appear to undergo LLPS--leading to speculation that synaptic sites could exists, at least partially, in a phase separated state. We aim to develop optogentic tools to manipulate LLPS at the synapse, to conduct causative experiments to understand how LLPS could impact synapse function.    
This research could shed light on the importance of LLPS at the synapse for proper neuronal function.   

Research Methods

We utilize broad methods to evaluate glutamatergic synapse function including:


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