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Regulator of G-protein signaling 4

RGS4, regulator of G-protein signaling 4
Regulator of G protein signaling (RGS) family members are regulatory molecules that act as GTPase activating proteins (GAPs) for G alpha subunits of heterotrimeric G proteins. RGS proteins are able to deactivate G protein subunits of the Gi alpha, Go alpha and Gq alpha subtypes. They drive G proteins into their inactive GDP-bound forms. Regulator of G protein signaling 4 belongs to this family. All RGS proteins share a conserved 120-amino acid sequence termed the RGS domain. Regulator of G protein signaling 4 protein is 37% identical to RGS1 and 97% identical to rat Rgs4. This protein negatively regulate signaling upstream or at the level of the heterotrimeric G protein and is localized in the cytoplasm. Alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: RGS, CAN, RGS2, V1a, HAD
Papers using RGS4 antibodies
Identifying genetic networks underlying myometrial transition to labor.
Morty Rory Edward, In PLoS ONE, 2004
... cells, ASM cells were transduced by using Polybrene and lentiviral particles encoding RGS4-specific or scrambled non-coding 19–25 nt shRNA sequences (Santa Cruz Biotechnology).
Papers on RGS4
Roles for Regulator of G Protein Signaling Proteins in Synaptic Signaling and Plasticity.
Hepler et al., Atlanta, United States. In Mol Pharmacol, Feb 2016
Here, we review and highlight the current knowledge of specific RGS proteins (RGS2, RGS4, RGS7, RGS9-2, and RGS14) that have been clearly demonstrated to serve critical roles in modulating synaptic signaling and plasticity throughout the brain, and we consider their potential as future therapeutic targets.
Regulator of G-protein signaling 4: A novel tumor suppressor with prognostic significance in non-small cell lung cancer.
Tian et al., Jinan, China. In Biochem Biophys Res Commun, Feb 2016
In the current study, we identified RGS4 as a novel tumor suppressor with prognostic significance in non-small cell lung cancer (NSCLC).
Potent inhibition of angiotensin AT1 receptor signaling by RGS8: importance of the C-terminal third exon part of its RGS domain.
Kimura et al., Chiba, Japan. In J Recept Signal Transduct Res, Feb 2016
To evaluate intrinsic potency of these RGS proteins, we compared inhibitory effects of RGS1, RGS2, RGS3, RGS4, RGS5, RGS8 and RGS16 on AT1 receptor signaling.
Transcriptional Profiling of a Selective CREB Binding Protein Bromodomain Inhibitor Highlights Therapeutic Opportunities.
Jones et al., Cambridge, United States. In Chem Biol, Jan 2016
In addition, the CBP bromodomain inhibitor modulated the mRNA level of the regulator of G-protein signaling 4 (RGS4) gene in neurons, suggesting a potential therapeutic opportunity for CBP inhibitors in the treatment of neurological disorders.
M4 Muscarinic Receptor Signaling Ameliorates Striatal Plasticity Deficits in Models of L-DOPA-Induced Dyskinesia.
Surmeier et al., Chicago, United States. In Neuron, Dec 2015
Our studies show that in dSPNs, endogenous cholinergic signaling through M4 muscarinic receptors (M4Rs) promoted long-term depression of corticostriatal glutamatergic synapses, by suppressing regulator of G protein signaling type 4 (RGS4) activity, and blocked D1 dopamine receptor dependent long-term potentiation (LTP).
A putative RA-like region in the brain of the scale-backed antbird, Willisornis poecilinotus (Furnariides, Suboscines, Passeriformes, Thamnophilidae).
Schneider et al., Belém, Brazil. In Genet Mol Biol, Jul 2015
Specifically, a discrete domain with a distinct Nissl staining pattern and that expresses the RA marker RGS4 was found in the arcopallium where the oscine RA is localized.
Pharmacogenetics and antipsychotic treatment response.
Suturkova et al., Скопје, Macedonia. In Prilozi, 2014
It highlights the most important findings about the impact of functional polymorphisms in genes coding the CYP450 metabolizing enzymes, ABCB1 transporter gene, dopaminergic and serotonergic drug targets (DRD2, DRD3, DRD4, 5-HT1, 5HT-2A, 5HT-2C, 5HT6) as well as genes responsible for metabolism of neurotransmitters and G signalling pathways (5-HTTLPR, BDNF, COMT, RGS4) and points their role as potential biomarkers in everyday clinical practice.
Amino-terminal cysteine residues differentially influence RGS4 protein plasma membrane targeting, intracellular trafficking, and function.
Heximer et al., Toronto, Canada. In J Biol Chem, 2012
Cys-2 and Cys-12 play markedly different roles in the regulation of RGS4 membrane localization, intracellular trafficking, and G(q) inhibitory function via mechanisms that are unrelated to RGS4 protein stabilization.
RGS4 overexpression in the rat dorsal striatum modulates mGluR5- and amphetamine-mediated behavior and signaling.
McGinty et al., Charleston, United States. In Psychopharmacology (berl), 2012
data demonstrate that RGS4 in the dorsal striatum attenuates amphetamine-induced ERK signaling and decreases the behavioral efficacy of acute amphetamine likely by limiting mGluR5 function
Schizophrenia-related RGS4 gene variations specifically disrupt prefrontal control of saccadic eye movements.
Smyrnis et al., Athens, Greece. In Psychol Med, 2012
RGS4 gene variations specifically disrupt prefrontal control of saccadic eye movements.
μ-Opioid receptors and regulators of G protein signaling (RGS) proteins: from a symposium on new concepts in mu-opioid pharmacology.
Traynor, Ann Arbor, United States. In Drug Alcohol Depend, 2012
Several members of this family, in particular RGS4 and RGS9-2 have been demonstrated to influence MOR signaling and morphine-induced behaviors, including reward.
An RGS4-mediated phenotypic switch of bronchial smooth muscle cells promotes fixed airway obstruction in asthma.
Panettieri et al., Philadelphia, United States. In Plos One, 2011
These studies indicate that increased RGS4 expression promotes a phenotypic switch of airway smooth muscle, evoking irreversible airway obstruction in subjects with severe asthma.
Genetic predisposition to schizophrenia: what did we learn and what does the future hold?
Mirnics et al., Budapest, Hungary. In Neuropsychopharmacol Hung, 2011
Vulnerability in DISC1, NRG1, DTNBP1, RGS4, KCNH2, COMT, AKT1 and other putative schizophrenia genes, together with copy number variants, leave unexplained the vast majority of diseased cases.
G protein-coupled receptor signaling and sphingosine-1-phosphate play a phylogenetically conserved role in endocrine pancreas morphogenesis.
Gavalas et al., Athens, Greece. In Mol Cell Biol, 2011
Rgs4 is expressed in endocrine progenitors of both zebrafish and mouse, and its expression in the mouse pancreatic epithelium is strictly dependent upon Ngn3, and loss of function of Rgs4 results in islet fragmentation in both organisms.
Recent advances in postmortem pathology and neurochemistry in schizophrenia.
Scarr et al., Australia. In Curr Opin Psychiatry, 2009
There appear to be complex changes in the expression of proposed candidate genes for schizophrenia such as NRG1, DISC1, RGS4 and DTNB1, and there are continued reports of alterations in central gamma-aminobutyric acidergic, dopaminergic, glutamatergic and cholinergic pathways in patients with the disorder.
Snapshot of activated G proteins at the membrane: the Galphaq-GRK2-Gbetagamma complex.
Tesmer et al., Austin, United States. In Science, 2006
Galphaq forms an effector-like interaction with the GRK2 regulator of G protein signaling (RGS) homology domain that is distinct from and does not overlap with that used to bind RGS proteins such as RGS4.
The N-end rule pathway as a nitric oxide sensor controlling the levels of multiple regulators.
Varshavsky et al., Pasadena, United States. In Nature, 2005
The levels of regulatory proteins bearing N-terminal cysteine, such as RGS4, RGS5 and RGS16, are greatly increased in mouse ATE1-/- embryos, which lack arginylation.
Spinophilin regulates Ca2+ signalling by binding the N-terminal domain of RGS2 and the third intracellular loop of G-protein-coupled receptors.
Muallem et al., Dallas, United States. In Nat Cell Biol, 2005
SPL also binds RGS1, RGS4, RGS16 and GAIP.
RGS16 inhibits signalling through the G alpha 13-Rho axis.
Druey et al., Rockville, United States. In Nat Cell Biol, 2003
In contrast, classical RGS proteins (such as RGS16 and RGS4) exhibit RGS domain-dependent GAP activity on G alpha i and G alpha q, but not G alpha 12 or G alpha 13 (ref 4).
Inhibition of brain Gz GAP and other RGS proteins by palmitoylation of G protein alpha subunits.
Ross et al., Dallas, United States. In Science, 1997
Palmitoylation of Galphaz also inhibited its response to the GAP activity of Galpha-interacting protein (GAIP), another RGS protein, and palmitoylation of Galphai1 inhibited its response to RGS4.
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