ArticleThe EMBO journal1997
Site-directed mutagenesis of highly conserved amino acids in the first cytoplasmic loop of Drosophila Rh1 opsin blocks rhodopsin synthesis in the nascent state.
Article in The EMBO journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 28 citations in OpenAlex.
- In vivo identification of Drosophila rhodopsin interaction partners by biotin proximity labeling.Scientific reports · 2024Article
- The Role of ICL1 and H8 in Class B1 GPCRs; Implications for Receptor Activation.Frontiers in endocrinology · 2021Article
- Immunocytochemical Labeling of Rhabdomeric Proteins inThe journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2019Article
- Functional characterization of the three Drosophila retinal degeneration C (RDGC) protein phosphatase isoforms.PloS one · 2018Article
- The latency of the light response is modulated by the phosphorylation state of Drosophila TRP at a specific site.Channels (Austin, Tex.) · 2017Article
- Drosophila Rhodopsin 7 can partially replace the structural role of Rhodopsin 1, but not its physiological function.Journal of comparative physiology. A, Neuroethology, sensory, neural, and behavioral physiology · 2017Article
- Article
- Honeybee blue- and ultraviolet-sensitive opsins: cloning, heterologous expression in Drosophila, and physiological characterization.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1998Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The cytoplasmic surface of Drosophila melanogaster Rh1 rhodopsin (ninaE) harbours amino acids which are highly conserved among G-protein-coupled receptors. Site-directed mutations which cause Leu81Gln or Asn86Ile amino acid substitutions in the first cytoplasmic loop of the Rh1 opsin protein, are shown to block rhodopsin synthesis in the nascent, glycosylated state from which the mutant opsin is degraded rapidly. In mutants Leu81Gln and Asn86Ile, only 20-30% and <2% respectively, of functional rhodopsins are synthesized and transported to the photoreceptive membrane. Thus, conserved amino acids in opsin's cytoplasmic surface are a critical factor in the interaction of opsin with proteins of the rhodopsin processing machinery. Photoreceptor cells expressing mutant rhodopsins undergo age-dependent degeneration in a recessive manner.
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