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Regulation Of Crfr1 And 5-Ht2ar By Pdz Domain-Containing Proteins Sap97 And Psd-95, Henry A. Dunn
Regulation Of Crfr1 And 5-Ht2ar By Pdz Domain-Containing Proteins Sap97 And Psd-95, Henry A. Dunn
Electronic Thesis and Dissertation Repository
Previous studies identified a crosstalk mechanism whereby CRFR1 sensitized 5-HT2AR-mediated signaling via interactions with PDZ domain-containing proteins: a mechanism that may underlie stress-induced anxiety and depression. This prompted an investigation into uncovering which PDZ domain-containing proteins could regulate the crosstalk between these two receptors, and how they could be regulated individually. In the current studies, a subset of PDZ domain-containing proteins were identified that may interact with CRFR1 and 5-HT2AR. The focus narrowed to two candidates previously implicated in psychiatric disease: SAP97 and PSD-95. We confirmed SAP97 and PSD-95 as interacting partners of CRFR1 in adult …
Regulation Of Metabotropic Glutamate Receptor 5 Activity By Ca2+/Calmodulin-Dependent Protein Kinase Iiα, Fitore Raka
Regulation Of Metabotropic Glutamate Receptor 5 Activity By Ca2+/Calmodulin-Dependent Protein Kinase Iiα, Fitore Raka
Electronic Thesis and Dissertation Repository
The metabotropic glutamate receptor 5 (mGluR5) is a GPCR coupled to the heterotrimeric G protein Gaq/11 and activates signaling pathways important for excitatory synaptic transmission. Emerging studies reveal that Amyloid b (Ab) acts as an extracellular scaffold for mGluR5. We have identified Ca2+/Calmodulin-dependent protein Kinase IIα (CAMKIIα) as an interacting protein of mGluR5. We hypothesize that CaMKIIα plays a role in mGluR5 signaling and Ab produces differential effects on the regulation of mGluR5 by CAMKIIα. We find that overexpression of CAMKIIα significantly impairs mGluR5-mediated ERK1/2 phosphorylation but does not effect inositol phosphate formation or Ca2+ release. …