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Rhodopsin-arrestin complex formation as a novel mechanism for light-dependent retinal degeneration.

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Call No.	QP671.V5 A45 2000
Author	Alloway, Paul Gregory
Title	Rhodopsin-arrestin complex formation as a novel mechanism for light-dependent retinal degeneration.
Date	2000
Abstract	Arrestins are regulatory proteins that participate in the termination of G protein-mediated signal transduction. The major arrestin in the Drosophila visual system, Arrestin 2 (Arr2), has been demonstrated to be essential for the termination of the visual signaling cascade in vivo. Arr2 is phosphorylated in a light-induced calcium-dependent manner by the Ca 2+ /calmodulin-dependent protein kinase, CamKII. Although it has been known for quite some time that Arr2 undergoes light-dependent phosphorylation, the role of this phosphorylation is unknown. One major goal of this study was the characterization of the role of the light-dependent phosphorylation of Arr2. Genetic and biochemical analysis revealed that the phosphorylation of Arr2 is necessary for its release from rhodopsin once rhodopsin has converted back to its inactive form. Thus, arrestin mutants that are incapable of being phosphorylated form stable rhodopsin-arrestin complexes. The formation of stable rhodopsin-arrestin complexes is also observed in flies carrying mutations in the eye-specific phospholipase C gene, norpA, as well as the phosphatidylinositol transfer protein, rdgB. In all cases, the abnormal persistence of complexes between rhodopsin and arrestin trigger apoptotic cell death and massive retinal degeneration. Moreover, genetic studies demonstrate that endocytosis is essential for the induction of cell death, which suggests that the internalization of the rhodopsin-arrestin complexes is an early step in the initiation of apoptosis in these retinal degeneration mutants. The formation of stable rhodopsin-arrestin complexes represents a novel mechanism to explain the light-dependent retinal degeneration that is observed in a subset of Drosophila visual system mutants. Stable complexes between rhodopsin and arrestin have also been observed in certain forms of autosomal dominant retinitis pigmentosa (ADRIP) and thus might be causal to the disease in humans.
Description	1 online resource (xii, 117 leaves) : illustrations
Format	application/pdf
Advisor	Jack, Tom P.
Subject	Visual pigments. ; Cellular signal transduction. ; Rhodopsin. ; G proteins. ; Phosphorylation. ; Photoreceptors. ; Retinal degeneration.
College	Dartmouth College -- Department of Biological Sciences.
Issuing Body	Dartmouth Dissertations are made available through the Dartmouth Digital Library.
Degree	Thesis (Ph.D)--Dartmouth College.
Copyright	In Copyright. This material is protected by copyright and/or related rights. You are free to use this material in any way that is permitted by copyright law that applies to your use. For other uses, you need to obtain permission from the rights-holder(s). http://rightsstatements.org/page/InC/1.0/
DOI	https://doi.org/10.1349/ddlp.2652

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