# RGS9 > Mediated Wiki article. Canonical URL: https://mediated.wiki/source/RGS9 > Markdown URL: https://mediated.wiki/source/RGS9.md > Source: https://en.wikipedia.org/wiki/RGS9 > Source revision: 1300696061 > License: Creative Commons Attribution-ShareAlike 4.0 International (https://creativecommons.org/licenses/by-sa/4.0/) {{Short description|Protein-coding gene in the species Homo sapiens}} {{Infobox_gene}} '''Regulator of G-protein signalling 9''', also known as '''RGS9''', is a human [gene](/source/gene),{{cite web | title = Entrez Gene: RGS9 regulator of G-protein signalling 9| url = https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=8787}} which codes for a protein involved in regulation of [signal transduction](/source/signal_transduction) inside cells. Members of the [RGS family](/source/Regulator_of_G_protein_signalling), such as RGS9, are signaling proteins that suppress the activity of [G protein](/source/G_protein)s by promoting their deactivation.[supplied by OMIM] There are two splice isoforms of RGS9 with quite different properties and patterns of expression. RGS9-1 is mainly found in the eye and is involved in regulation of phototransduction in [rod and cone cells](/source/Photoreceptor_cell) of the [retina](/source/retina); genetic mutations in RGS9-1 cause the eye disease [bradyopsia](/source/bradyopsia). RGS9-2 is found in the brain, and regulates dopamine and opioid signaling in the [basal ganglia](/source/basal_ganglia).{{cite journal |vauthors=Martemyanov KA, Krispel CM, Lishko PV, Burns ME, Arshavsky VY |title=Functional comparison of RGS9 splice isoforms in a living cell |journal=Proceedings of the National Academy of Sciences of the United States of America |volume=105 |issue=52 |pages=20988–93 |date=December 2008 |pmid=19098104 |pmc=2634932 |doi=10.1073/pnas.0808941106 |bibcode=2008PNAS..10520988M |doi-access=free }} RGS9-2 is of particular interest as the most important RGS protein involved in terminating signalling by the [mu opioid receptor](/source/mu_opioid_receptor) (although [RGS4](/source/RGS4) and [RGS17](/source/RGS17) are also involved), and is thought to be important in the development of tolerance to opioid drugs.{{cite journal |vauthors=Garzón J, Rodríguez-Díaz M, López-Fando A, Sánchez-Blázquez P |title=RGS9 proteins facilitate acute tolerance to mu-opioid effects |journal=The European Journal of Neuroscience |volume=13 |issue=4 |pages=801–11 |date=February 2001 |pmid=11207815 |doi= 10.1046/j.0953-816x.2000.01444.x|hdl=10261/154868 |s2cid=23943994 |hdl-access=free }}{{cite journal |vauthors=Zachariou V, Georgescu D, Sanchez N, Rahman Z, DiLeone R, Berton O, Neve RL, Sim-Selley LJ, Selley DE, Gold SJ, Nestler EJ |title=Essential role for RGS9 in opiate action |journal=Proceedings of the National Academy of Sciences of the United States of America |volume=100 |issue=23 |pages=13656–61 |date=November 2003 |pmid=14595021 |pmc=263869 |doi=10.1073/pnas.2232594100 |bibcode=2003PNAS..10013656Z |doi-access=free }}{{cite journal |vauthors=Sánchez-Blázquez P, Rodríguez-Muñoz M, Montero C, Garzón J |title=RGS-Rz and RGS9-2 proteins control mu-opioid receptor desensitisation in CNS: the role of activated Galphaz subunits |journal=Neuropharmacology |volume=48 |issue=1 |pages=134–50 |date=January 2005 |pmid=15617734 |doi=10.1016/j.neuropharm.2004.08.016 |s2cid=40755580 }}{{cite journal |vauthors=Garzón J, Rodríguez-Muñoz M, López-Fando A, Sánchez-Blázquez P |title=Activation of mu-opioid receptors transfers control of Galpha subunits to the regulator of G-protein signaling RGS9-2: role in receptor desensitization |journal=The Journal of Biological Chemistry |volume=280 |issue=10 |pages=8951–60 |date=March 2005 |pmid=15632124 |doi=10.1074/jbc.M407005200 |doi-access=free }}{{cite journal |vauthors=Psifogeorgou K, Papakosta P, Russo SJ, Neve RL, Kardassis D, Gold SJ, Zachariou V |title=RGS9-2 is a negative modulator of mu-opioid receptor function |journal=Journal of Neurochemistry |volume=103 |issue=2 |pages=617–25 |date=October 2007 |pmid=17725581 |doi=10.1111/j.1471-4159.2007.04812.x |s2cid=23246884 |doi-access=free }}{{cite journal |vauthors=Hooks SB, Martemyanov K, Zachariou V |title=A role of RGS proteins in drug addiction |journal=[Biochemical Pharmacology](/source/Biochemical_Pharmacology_(journal)) |volume=75 |issue=1 |pages=76–84 |date=January 2008 |pmid=17880927 |doi=10.1016/j.bcp.2007.07.045 }}{{cite journal |vauthors=Traynor JR, Terzi D, Caldarone BJ, Zachariou V |title=RGS9-2: probing an intracellular modulator of behavior as a drug target |journal=Trends in Pharmacological Sciences |volume=30 |issue=3 |pages=105–11 |date=March 2009 |pmid=19211160 |doi=10.1016/j.tips.2008.11.006 |pmc=3394094}} RGS9-deficient mice exhibit some motor and cognitive difficulties however, so inhibition of this protein is likely to cause similar side effects.{{cite journal |vauthors=Blundell J, Hoang CV, Potts B, Gold SJ, Powell CM |title=Motor coordination deficits in mice lacking RGS9 |journal=Brain Research |volume=1190 |pages=78–85 |date=January 2008 |pmid=18073128 |pmc=2241663 |doi=10.1016/j.brainres.2007.11.017 }} RGS9 is differentially regulated by Guanine nucleotide-binding protein subunit beta-5 ([GNB5](/source/GNB5)) via the [DEP domain](/source/DEP_domain) and DEP helical-extension domain in protein stability and membrane anchor association.{{Cite journal | last1 = Masuho | first1 = I. | last2 = Wakasugi-Masuho | first2 = H. | last3 = Posokhova | first3 = E. N. | last4 = Patton | first4 = J. R. | last5 = Martemyanov | first5 = K. A. | title = Type 5 G Protein Subunit (G 5) Controls the Interaction of Regulator of G Protein Signaling 9 (RGS9) with Membrane Anchors | doi = 10.1074/jbc.M111.241513 | journal = Journal of Biological Chemistry | volume = 286 | issue = 24 | pages = 21806–21813 | year = 2011 | pmid = 21511947 | pmc =3122235 | doi-access = free }} ==References== {{reflist}} ==Further reading== {{refbegin | 2}} *{{cite journal |vauthors=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery |journal=Genome Res. |volume=6 |issue= 9 |pages= 791–806 |year= 1997 |pmid= 8889548 |doi=10.1101/gr.6.9.791 |doi-access=free }} *{{cite journal |vauthors=Cowan CW, Fariss RN, Sokal I, etal |title=High expression levels in cones of RGS9, the predominant GTPase accelerating protein of rods |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 9 |pages= 5351–6 |year= 1998 |pmid= 9560279 |doi=10.1073/pnas.95.9.5351 | pmc=20264 |bibcode=1998PNAS...95.5351C |doi-access=free }} *{{cite journal |vauthors=Granneman JG, Zhai Y, Zhu Z, etal |title=Molecular characterization of human and rat RGS 9L, a novel splice variant enriched in dopamine target regions, and chromosomal localization of the RGS 9 gene |journal=Mol. Pharmacol. |volume=54 |issue= 4 |pages= 687–94 |year= 1998 |pmid= 9765512 }} *{{cite journal |vauthors=Zhang K, Howes KA, He W, etal |title=Structure, alternative splicing, and expression of the human RGS9 gene |journal=Gene |volume=240 |issue= 1 |pages= 23–34 |year= 2000 |pmid= 10564809 |doi=10.1016/S0378-1119(99)00393-5 }} *{{cite journal |vauthors=Yu H, Bondarenko VA, Yamazaki A |title=Inhibition of retinal guanylyl cyclase by the RGS9-1 N-terminus |journal=Biochem. Biophys. Res. Commun. |volume=286 |issue= 1 |pages= 12–9 |year= 2001 |pmid= 11485301 |doi= 10.1006/bbrc.2001.5346 }} *{{cite journal |vauthors=Hu G, Wensel TG |title=R9AP, a membrane anchor for the photoreceptor GTPase accelerating protein, RGS9-1 |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 15 |pages= 9755–60 |year= 2002 |pmid= 12119397 |doi= 10.1073/pnas.152094799 | pmc=125004 |bibcode=2002PNAS...99.9755H |doi-access=free }} *{{cite journal |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |bibcode=2002PNAS...9916899M |doi-access=free }} *{{cite journal |vauthors=Martemyanov KA, Lishko PV, Calero N, etal |title=The DEP domain determines subcellular targeting of the GTPase activating protein RGS9 in vivo |journal=J. Neurosci. |volume=23 |issue= 32 |pages= 10175–81 |year= 2003 |pmid= 14614075 |doi= 10.1523/JNEUROSCI.23-32-10175.2003|pmc= 6741003 }} *{{cite journal |vauthors=Nishiguchi KM, Sandberg MA, Kooijman AC, etal |title=Defects in RGS9 or its anchor protein R9AP in patients with slow photoreceptor deactivation |journal=Nature |volume=427 |issue= 6969 |pages= 75–8 |year= 2004 |pmid= 14702087 |doi= 10.1038/nature02170 |bibcode=2004Natur.427...75N |s2cid=953980 }} *{{cite journal |vauthors=Ajit SK, Young KH |title=Enhancement of pheromone response by RGS9 and Gbeta5 in yeast |journal=Biochem. Biophys. Res. Commun. |volume=324 |issue= 2 |pages= 686–91 |year= 2004 |pmid= 15474482 |doi= 10.1016/j.bbrc.2004.09.100 }} *{{cite journal |vauthors=Cheng JY, Luu CD, Yong VH, etal |title=Bradyopsia in an Asian man |journal=Arch. Ophthalmol. |volume=125 |issue= 8 |pages= 1138–40 |year= 2007 |pmid= 17698770 |doi= 10.1001/archopht.125.8.1138 }} {{refend}} == External links == * {{PDBe-KB2|O54828|Mouse Regulator of G-protein signaling 9}} {{PDB Gallery|geneid=8787}} {{gene-17-stub}} --- Adapted from the Wikipedia article [RGS9](https://en.wikipedia.org/wiki/RGS9) by Wikipedia contributors ([contributor history](https://en.wikipedia.org/wiki/RGS9?action=history)). Available under [Creative Commons Attribution-ShareAlike 4.0 International](https://creativecommons.org/licenses/by-sa/4.0/). Changes may have been made.