ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2010
Membrane anchoring subunits specify selective regulation of RGS9·Gbeta5 GAP complex in photoreceptor neurons.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2010. 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, 11 citations in OpenAlex.
- Effect of Rhodopsin Phosphorylation on Dark Adaptation in Mouse Rods.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2016Article
- Orphan Receptor GPR158 Is an Allosteric Modulator of RGS7 Catalytic Activity with an Essential Role in Dictating Its Expression and Localization in the Brain.The Journal of biological chemistry · 2015Article
- Differential function of Gγ13 in rod bipolar and ON cone bipolar cells.The Journal of physiology · 2015Article
- G protein signaling in the retina and beyond: the Cogan lecture.Investigative ophthalmology & visual science · 2014Article
- R9AP targeting to rod outer segments is independent of rhodopsin and is guided by the SNARE homology domain.Molecular biology of the cell · 2014Article
- Photoreceptors in whirler mice show defective transducin translocation and are susceptible to short-term light/dark changes-induced degeneration.Experimental eye research · 2014Article
- Membrane attachment is key to protecting transducin GTPase-activating complex from intracellular proteolysis in photoreceptors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2011Article
- Type 5 G protein beta subunit (Gbeta5) controls the interaction of regulator of G protein signaling 9 (RGS9) with membrane anchors.The Journal of biological chemistry · 2011Article
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Authors and funding
5 authors at 2 institutions in 1 country.
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Abstract
The RGS9·Gβ5 complex is the key regulator of neuronal G-protein signaling and shows remarkable selectivity of subunit composition. In retinal photoreceptors, RGS9·Gβ5 is bound to the membrane anchor R9AP and the complex regulates visual signaling. In the basal ganglia neurons, RGS9·Gβ5 is instead associated with a homologous protein, R7BP, and regulates reward circuit. Switching this selective subunit composition of the complex in rod photoreceptors allowed us to study the molecular underpinning of signaling specificity in diverse G-protein pathways. We have found that both membrane anchoring subunits play a conserved role in regulating protein levels of RGS9·Gβ5 and enhancing the ability of RGS·Gβ5 complexes to stimulate GTPase activity of G proteins. However, notable differences exist in the subcellular targeting of alternatively configured complexes. Unlike R9AP, which relies on passive targeting mechanisms for the delivery to the outer segments of the photoreceptors, R7BP is excluded from this location and is instead specifically targeted to the plasma membrane. R7BP-containing complexes could be rerouted to the outer segments, where they are capable of regulating the phototransduction cascade by the active targeting signals derived from rhodopsin. These findings illustrate the diversity of the G-protein signaling regulation by RGS·Gβ5 complexes achieved by differential recruitment of the membrane anchors.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.