ArticleProceedings of the National Academy of Sciences of the United States of America1998
Plasma membrane localization is required for RGS4 function in Saccharomyces cerevisiae.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 139 citations in OpenAlex.
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- Opioid receptors reveal a discrete cellular mechanism of endosomal G protein activation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The spatial distribution of GPCR and Gβγ activity across a cell dictates PIP3 dynamics.Scientific reports · 2023Article
- Directly light-regulated binding of RGS-LOV photoreceptors to anionic membrane phospholipids.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Group VII Ethylene Response Factors in Arabidopsis: Regulation and Physiological Roles.Plant physiology · 2018Review
- Yeast GPCR signaling reflects the fraction of occupied receptors, not the number.Molecular systems biology · 2016Article
- The dynamic role of regulator of G-protein signalling (RGS) proteins in partial agonism.The Journal of physiology · 2014Article
- Subcellular optogenetic inhibition of G proteins generates signaling gradients and cell migration.Molecular biology of the cell · 2014Article
- Modification and functional inhibition of regulator of G-protein signaling 4 (RGS4) by 4-hydroxy-2-nonenal.Chemical research in toxicology · 2013Article
- Reversible inhibitors of regulators of G-protein signaling identified in a high-throughput cell-based calcium signaling assay.Cellular signalling · 2013Article
- A physiologically required G protein-coupled receptor (GPCR)-regulator of G protein signaling (RGS) interaction that compartmentalizes RGS activity.The Journal of biological chemistry · 2013Article
- Zebrafish rgs4 is essential for motility and axonogenesis mediated by Akt signaling.Cellular and molecular life sciences : CMLS · 2013Article
- α-Synuclein disrupts stress signaling by inhibiting polo-like kinase Cdc5/Plk2.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Amino-terminal cysteine residues differentially influence RGS4 protein plasma membrane targeting, intracellular trafficking, and function.The Journal of biological chemistry · 2012Article
- A finer tuning of G-protein signaling through regulated control of RGS proteins.American journal of physiology. Heart and circulatory physiology · 2012Review
- A novel patch assembly domain in Num1 mediates dynein anchoring at the cortex during spindle positioning.The Journal of cell biology · 2012Article
- Neurabin scaffolding of adenosine receptor and RGS4 regulates anti-seizure effect of endogenous adenosine.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2012Article
- Regulator of G protein signaling (RGS16) inhibits hepatic fatty acid oxidation in a carbohydrate response element-binding protein (ChREBP)-dependent manner.The Journal of biological chemistry · 2011Article
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4 authors at 1 institution in 1 country.
Funding
Abstract
RGS4, a mammalian GTPase activating protein for G protein alpha subunits, was identified by its ability to inhibit the pheromone response pathway in Saccharomyces cerevisiae. To define regions of RGS4 necessary for its function in vivo, we assayed mutants for activity in this system. Deletion of the N-terminal 33 aa of RGS4 (Delta1-33) yielded a nonfunctional protein and loss of plasma membrane localization. These functions were restored by addition of a C-terminal membrane-targeting sequence to RGS4 (Delta1-33). Thus, plasma membrane localization is tightly coupled with the ability of RGS4 to inhibit signaling. Fusion of the N-terminal 33 aa of RGS4 to green fluorescent protein was sufficient to localize an otherwise soluble protein to the plasma membrane, defining this N-terminal region as a plasma membrane anchorage domain. RGS4 is palmitoylated, with Cys-2 and Cys-12 the likely sites of palmitoylation. Surprisingly, mutation of the cysteine residues within the N-terminal domain of RGS4 did not affect plasma membrane localization in yeast or the ability to inhibit signaling. Features of the N-terminal domain other than palmitoylation are responsible for the plasma membrane association of RGS4 and its ability to inhibit pheromone response in yeast.
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