Major
Psychology
Anticipated Graduation Year
2026
Access Type
Open Access
Abstract
PSD-95 is a pivotal postsynaptic scaffolding protein that regulates synaptic maturation, receptor localization, and signaling proteins, including mediating NMDA receptor clustering and function in synaptic plasticity. NMDA receptor-dependent LTD is dependent on multiple post-translational modifications. One of these modifications, phosphorylation of PSD-95, destabilizes the protein which can prompt the exit of associated AMPARs from postsynaptic spines. Our investigations highlight a potential factor in PSD-95 destabilization, isomerization of phospho-T19 by Pin1. We hypothesize that Pin1 mediated phosphorylation of PSD-95 may either protect or target PSD-95 for ubiquitination, playing a critical role in NMDAR-LTD.
Faculty Mentors & Instructors
Dr. Jary Delgado, Assistant Professor, Department of Biology
Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 3.0 License.
Post-Translational Modifications of PSD-95 in Glutamatergic Synapses
PSD-95 is a pivotal postsynaptic scaffolding protein that regulates synaptic maturation, receptor localization, and signaling proteins, including mediating NMDA receptor clustering and function in synaptic plasticity. NMDA receptor-dependent LTD is dependent on multiple post-translational modifications. One of these modifications, phosphorylation of PSD-95, destabilizes the protein which can prompt the exit of associated AMPARs from postsynaptic spines. Our investigations highlight a potential factor in PSD-95 destabilization, isomerization of phospho-T19 by Pin1. We hypothesize that Pin1 mediated phosphorylation of PSD-95 may either protect or target PSD-95 for ubiquitination, playing a critical role in NMDAR-LTD.