ArticleProceedings of the National Academy of Sciences of the United States of America2001
Expression of gamma-aminobutyric acid rho 1 and rho 1 Delta 450 as gene fusions with the green fluorescent protein.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 10 citations in OpenAlex.
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- Antagonistic effect of dopamine structural analogues on human GABAρ1 receptor.Scientific reports · 2017Article
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- Development and preliminary validation of a plate-based CB1/CB2 receptor functional assay.Analytical biochemistry · 2013Article
- Use of multicomponent reactions in developing small-molecule tools to study GABAA receptor mechanism and function.Future medicinal chemistry · 2011Review
- An Update on GABAρ Receptors.Current neuropharmacology · 2010Article
- Functional characterization of N-terminally GFP-tagged GLP-1 receptor.Journal of biomedicine & biotechnology · 2009Article
- Properties of GluR3 receptors tagged with GFP at the amino or carboxyl terminus.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Functional expression in frog oocytes of human rho 1 receptors produced in Saccharomyces cerevisiae.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- The single-channel properties of human acetylcholine alpha 7 receptors are altered by fusing alpha 7 to the green fluorescent protein.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- Some properties of human neuronal alpha 7 nicotinic acetylcholine receptors fused to the green fluorescent protein.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The functional characteristics and cellular localization of the gamma aminobutyric acid (GABA) rho 1 receptor and its nonfunctional isoform rho 1 Delta 450 were investigated by expressing them as gene fusions with the enhanced version of the green fluorescent protein (GFP). Oocytes injected with rho 1-GFP had receptors that gated chloride channels when activated by GABA. The functional characteristics of these receptors were the same as for those of wild-type rho 1 receptors. Fluorescence, because of the chimeric receptors expressed, was over the whole oocyte but was more intense near the cell surface and more abundant in the animal hemisphere. Similar to the wild type, rho 1 Delta 450-GFP did not lead to the expression of functional GABA receptors, and injected oocytes failed to generate currents even after exposure to high concentrations of GABA. Nonetheless, the fluorescence displayed by oocytes expressing rho 1 Delta 450-GFP was distributed similarly to that of rho 1-GFP. Mammalian cells transfected with the rho 1-GFP or rho 1 Delta 450-GFP constructs showed mostly intracellularly distributed fluorescence in confocal microscope images. A sparse localization of fluorescence was observed in the plasma membrane regardless of the cell line used. We conclude that rho 1 Delta 450 is expressed and transported close to, and perhaps incorporated into, the plasma membrane. Thus, rho 1- and rho 1 Delta 450-GFP fusions provide a powerful tool to visualize the traffic of GABA type C receptors.
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