Receptor demise from alteration of glycosylation site inDrosophilaopsin: Electrophysiology, microspectrophotometry, and electron microscopy
| العنوان: | Receptor demise from alteration of glycosylation site inDrosophilaopsin: Electrophysiology, microspectrophotometry, and electron microscopy |
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| المؤلفون: | De-Mao Chen, Ron Lee, Gary Brown, J. Scott Christianson, William S. Stark |
| المصدر: | Visual Neuroscience. 11:619-628 |
| بيانات النشر: | Cambridge University Press (CUP), 1994. |
| سنة النشر: | 1994 |
| مصطلحات موضوعية: | Rhodopsin, Opsin, Glycosylation, Physiology, Mutant, Electroretinography, medicine, Animals, Freeze Fracturing, Photopigment, biology, medicine.diagnostic_test, Rod Opsins, Wild type, Anatomy, biology.organism_classification, Rhabdomere, Sensory Systems, Cell biology, Drosophila melanogaster, Microspectrophotometry, biology.protein, Photoreceptor Cells, Invertebrate, Asparagine, Signal Transduction |
| الوصف: | In the δAsn20Drosophilastock, the N-linked glycosylation site of opsin in Rl-6 receptors (Rhl) is absent. We used electroretinography (ERG), microspectrophotometry (MSP), and electron microscopy (EM) to quantify visual cell defects. Positive controls,w9, had wild type Rhl. MSP revealed minimal photopigment in δAsn20for 6 days posteclosion;w9had near normal visual pigment. ERG sensitivity and prolonged depolarizing afterpotential (PDA) were compared for δAsn20andw9.δAsn20's Rl-6 function is decreased 100–fold at eclosion and diminishes until only R7/8 functions at 11 days. What little rhodopsin is routed to the rhabdomere functions. Morphometry showed smaller Rl-6 rhabdomeres in δAsn20for 8 days posteclosion. Rhabdomeres inw9were normal. A negative control,ninaE0117, a deletion of the Rhl gene, also has small rhabdomeres. δAsn20andninaE0117lack the extreme rhabdomere elimination ofora(outerrhabdomeresabsent), a nonsense mutant interrupting Rhl's coding sequence. δAsn20andorahave surplus membrane whileninaE0117does not. Freeze fracture reveals that δAsn20's rhabdomeric P-face particle count is as low as for vitamin A deprivation, consistent with an opsin defect. High particle density, organized into rows, is present in adjacent plasmalemma where surplus membrane accumulates. In summary, δAsn20interferes with either synthesis, deployment, or maintenance of opsin. |
| تدمد: | 1469-8714 0952-5238 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a2c77a342bbc4d853fc616ad54099ee5 https://doi.org/10.1017/s0952523800002509 |
| حقوق: | CLOSED |
| رقم الأكسشن: | edsair.doi.dedup.....a2c77a342bbc4d853fc616ad54099ee5 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 14698714 09525238 |
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