| Literature DB >> 30976840 |
Javier Sancho-Pelluz1,2,3, Xuan Cui2,3,4, Winston Lee3, Yi-Ting Tsai2,3,5, Wen-Hsuan Wu2,3,5, Sally Justus2,3,6, Ilyas Washington3, Chun-Wei Hsu2,3, Karen Sophia Park2,3, Susanne Koch2,3,5, Gabriel Velez7,8,9, Alexander G Bassuk10, Vinit B Mahajan7,8, Chyuan-Sheng Lin11, Stephen H Tsang12,13,14,15.
Abstract
D190N, a missense mutation in rhodopsin, causes photoreceptor degeneration in patients with autosomal dominant retinitis pigmentosa (adRP). Two competing hypotheses have been developed to explain why D190N rod photoreceptors degenerate: (a) defective rhodopsin trafficking prevents proteins from correctly exiting the endoplasmic reticulum, leading to their accumulation, with deleterious effects or (b) elevated mutant rhodopsin expression and unabated signaling causes excitotoxicity. A knock-in D190N mouse model was engineered to delineate the mechanism of pathogenesis. Wild type (wt) and mutant rhodopsin appeared correctly localized in rod outer segments of D190N heterozygotes. Moreover, the rhodopsin glycosylation state in the mutants appeared similar to that in wt mice. Thus, it seems plausible that the injurious effect of the heterozygous mutation is not related to mistrafficking of the protein, but rather from constitutive rhodopsin activity and a greater propensity for chromophore isomerization even in the absence of light.Entities:
Keywords: D190N; Excitotoxicity; GPCR; Mouse model; Retina; Retinitis pigmentosa; Rhodopsin
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Year: 2019 PMID: 30976840 PMCID: PMC7144803 DOI: 10.1007/s00018-019-03090-9
Source DB: PubMed Journal: Cell Mol Life Sci ISSN: 1420-682X Impact factor: 9.261