The role that PSD organization plays in synaptic function and plasticity is only beginning to be understood. AMPARs play a well-established role in LTP; up-regulation of AMPARs within the postsynaptic density (PSD) is generally accepted to be the primary mechanism of NMDAR-dependent LTP. The function that AIDA-1 (Amyloid beta protein precursor intracellular domain-associated protein-1), a recently discovered component of the PSD, plays within synapses is less clear; however, in cultured hippocampal neurons, a portion of AIDA-1 translocates to the nucleus and increases downstream protein translation in response to NMDAR activation, Thus, experimental evidence suggests a role for AIDA-1 in synapse-to-nucleus signaling during NMDAR activation. My project uses electron microscopy and other histological techniques to determine the basal organization of AMPARs and AIDA-1 within the PSD. These data may provide better understanding of the roles these proteins play.
|Advisor:||Weinberg, Richard J.|
|Commitee:||Dudek, Serena M., Kash, Thomas L., Manis, Paul B., Philpot, Benjamin D.|
|School:||The University of North Carolina at Chapel Hill|
|School Location:||United States -- North Carolina|
|Source:||DAI-B 73/11(E), Dissertation Abstracts International|
|Subjects:||Neurosciences, Cellular biology|
|Keywords:||Aida-1, Ampar, Glua1, Glua3, Proteins, Psd, Synaptic plasticity|
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