The N-Terminus of PSD-93 as a Target for Calmodulin: Structural and Functional Analysis

Author

• Keyaa Dilip Shah, The University of Texas Rio Grande Valley

Date of Award

8-1-2026

Document Type

Thesis

Degree Name

Master of Science (MS)

Department

Biochemistry and Molecular Biology

First Advisor

Yonghong Zhang

Second Advisor

Frank Dean

Third Advisor

Arnulfo Mar

Abstract

Postsynaptic Density Protein-93 (PSD-93) is a membrane-associated guanylate kinase(MAGUK) scaffolding protein that regulates synaptic signaling by organizing signaling complexes at the post synapses including stabilizing neurotransmitter receptors on the postsynaptic membrane. The N-terminus of PSD-93 contains palmitoylation sites required for targeting PSD-93 to the membrane. The role of calcium-activated calmodulin (CaM) in the regulation of palmitoylation of MAGUK family members has been reported previously. However, the mechanisms and sites of interaction between CaM and the N-terminus of PSD-93 remain incompletely understood. Here, we applied computational docking modeling, biochemical and biophysical (NMR, fluorescence-based), and cellular approaches to elucidate the functional relationship between CaM and the PSD-93 N-terminus. Particularly, we performed protein-protein interaction analyses, NMR-based structural changes of PSD-93 upon CaM interaction, and examined the impact of these interactions on PSD-93 palmitoylation. Overall, the data obtained shed light on the molecular mechanism of regulation of PSD-93 by CaM/Ca2+ and provide additional information and new insight regarding the structure-function relationships in this important MAGUK protein.

Comments

Copyright 2026 Keyaa Dilip Shah. All Rights Reserved. https://proquest.com/docview/3409129348

Recommended Citation

Shah, K. (2026). The N-Terminus of PSD-93 as a Target for Calmodulin: Structural and Functional Analysis [Master's thesis, The University of Texas Rio Grande Valley]. ScholarWorks @ UTRGV. https://scholarworks.utrgv.edu/etd/2081