ArticleThe Biochemical journal1989
Cholera toxin treatment produces down-regulation of the alpha-subunit of the stimulatory guanine-nucleotide-binding protein (Gs).
Article in The Biochemical journal, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Latrophilin-1-Mediated GCells · 2026Article
- HDAC11 inhibition triggers bimodal thermogenic pathways to circumvent adipocyte catecholamine resistance.The Journal of clinical investigation · 2023Article
- HDAC11 inhibition triggers bimodal thermogenic pathways to circumvent adipocyte catecholamine resistance.bioRxiv : the preprint server for biology · 2023Article
- The cytopathic activity of cholera toxin requires a threshold quantity of cytosolic toxin.Cellular signalling · 2023Article
- Bioluminescence resonance energy transfer-based biosensors allow monitoring of ligand- and transducer-mediated GPCR conformational changes.Communications biology · 2018Article
- Spatial intensity distribution analysis quantifies the extent and regulation of homodimerization of the secretin receptor.The Biochemical journal · 2017Article
- Type 1 cannabinoid receptor ligands display functional selectivity in a cell culture model of striatal medium spiny projection neurons.The Journal of biological chemistry · 2014Article
- Article
- Modification of heterotrimeric G-proteins in Swiss 3T3 cells stimulated with Pasteurella multocida toxin.PloS one · 2012Article
- Stimulation of beta(3)-adrenoceptors causes phosphorylation of p38 mitogen-activated protein kinase via a stimulatory G protein-dependent pathway in 3T3-L1 adipocytes.British journal of pharmacology · 2002Article
- Gonadotrophin-releasing hormone receptor agonist-mediated down-regulation of Gq alpha/G11 alpha (pertussis toxin-insensitive) G proteins in alpha T3-1 gonadotroph cells reflects increased G protein turnover but not alterations in mRNA levels.Proceedings of the National Academy of Sciences of the United States of America · 1995Article
- Overexpression of Gs alpha subunit in thyroid tumors bearing a mutated Gs alpha gene.Journal of cancer research and clinical oncology · 1995Article
- Enhanced degradation of the phosphoinositidase C-linked guanine-nucleotide-binding protein Gq alpha/G11 alpha following activation of the human M1 muscarinic acetylcholine receptor expressed in CHO cells.The Biochemical journal · 1993Article
- A novel N-terminal motif for palmitoylation of G-protein alpha subunits.The Biochemical journal · 1993Article
- Gs alpha is a substrate for mono(ADP-ribosyl)transferase of NG108-15 cells. ADP-ribosylation regulates Gs alpha activity and abundance.The Biochemical journal · 1992Article
- Gi3 does not contribute to the inhibition of adenylate cyclase when stimulation of an alpha 2-adrenergic receptor causes activation of both Gi2 and Gi3.The Biochemical journal · 1992Article
- Cholera toxin impairment of opioid-mediated inhibition of adenylate cyclase in neuroblastoma x glioma hybrid cells is due to a toxin-induced decrease in opioid receptor levels.The Biochemical journal · 1991Article
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3 authors.
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Abstract
The effect of activation of the alpha-subunit(s) of the stimulatory guanine-nucleotide-binding protein, Gs, on levels of this polypeptide(s) associated with the plasma membrane of L6 skeletal myoblasts was ascertained. Incubation of these cells with cholera toxin led to a time- and concentration-dependent 'down-regulation' of both 44 and 42 kDa forms of Gs alpha as assessed by immunoblotting with an anti-peptide antiserum (CS1) able to identify the extreme C-terminus of Gs. The effect of cholera toxin was specific for Gs; levels of Gi alpha in membranes of cholera toxin-treated cells were not different from untreated cells. Down-regulation of Gs was absolutely dependent upon prior ADP-ribosylation, and hence activation of Gs and was not mimicked by other agents which elevate intracellular levels of cyclic AMP. Pretreatment with pertussis toxin, which catalyses ADP-ribosylation of Gi but not of Gs, did not down-regulate either Gi or Gs, demonstrating that covalent modification by ADP-ribosylation is alone not a signal for removal of G-proteins from the plasma membrane.
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