RGS16

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RGS16
Protein RGS16 PDB 2ik8.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases RGS16, A28-RGS14, A28-RGS14P, RGS-R, regulator of G-protein signaling 16
External IDs MGI: 108407 HomoloGene: 2196 GeneCards: RGS16
RNA expression pattern
PBB GE RGS16 209325 s at fs.png

PBB GE RGS16 209324 s at fs.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_002928

NM_011267

RefSeq (protein)

NP_002919

NP_035397.2
NP_035397

Location (UCSC) Chr 1: 182.6 – 182.6 Mb Chr 1: 153.74 – 153.75 Mb
PubMed search [1] [2]
Wikidata
View/Edit Human View/Edit Mouse

Regulator of G-protein signaling 16 is a protein that in humans is encoded by the RGS16 gene.[3][4]

Function[edit]

The protein encoded by this gene belongs to the 'regulator of G protein signaling' family. It inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits. It also may play a role in regulating the kinetics of signaling in the phototransduction cascade.[4]

Interactions[edit]

RGS16 has been shown to interact with GNAQ[5] and GNAI3.[6][7]

References[edit]

  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ Snow BE, Antonio L, Suggs S, Siderovski DP (Jan 1998). "Cloning of a retinally abundant regulator of G-protein signaling (RGS-r/RGS16): genomic structure and chromosomal localization of the human gene". Gene. 206 (2): 247–53. doi:10.1016/S0378-1119(97)00593-3. PMID 9469939. 
  4. ^ a b "Entrez Gene: RGS16 regulator of G-protein signalling 16". 
  5. ^ Johnson EN, Seasholtz TM, Waheed AA, Kreutz B, Suzuki N, Kozasa T, Jones TL, Brown JH, Druey KM (Dec 2003). "RGS16 inhibits signalling through the G alpha 13-Rho axis". Nature Cell Biology. 5 (12): 1095–103. doi:10.1038/ncb1065. PMID 14634662. 
  6. ^ Chen C, Zheng B, Han J, Lin SC (Mar 1997). "Characterization of a novel mammalian RGS protein that binds to Galpha proteins and inhibits pheromone signaling in yeast". The Journal of Biological Chemistry. 272 (13): 8679–85. doi:10.1074/jbc.272.13.8679. PMID 9079700. 
  7. ^ Beadling C, Druey KM, Richter G, Kehrl JH, Smith KA (Mar 1999). "Regulators of G protein signaling exhibit distinct patterns of gene expression and target G protein specificity in human lymphocytes". Journal of Immunology. 162 (5): 2677–82. PMID 10072511. 

Further reading[edit]

  • Berman DM, Wilkie TM, Gilman AG (Aug 1996). "GAIP and RGS4 are GTPase-activating proteins for the Gi subfamily of G protein alpha subunits". Cell. 86 (3): 445–52. doi:10.1016/S0092-8674(00)80117-8. PMID 8756726. 
  • De Vries L, Zheng B, Fischer T, Elenko E, Farquhar MG (2000). "The regulator of G protein signaling family". Annual Review of Pharmacology and Toxicology. 40: 235–71. doi:10.1146/annurev.pharmtox.40.1.235. PMID 10836135. 
  • Chen CK, Wieland T, Simon MI (Nov 1996). "RGS-r, a retinal specific RGS protein, binds an intermediate conformation of transducin and enhances recycling". Proceedings of the National Academy of Sciences of the United States of America. 93 (23): 12885–9. doi:10.1073/pnas.93.23.12885. PMC 24015Freely accessible. PMID 8917514. 
  • Chen C, Zheng B, Han J, Lin SC (Mar 1997). "Characterization of a novel mammalian RGS protein that binds to Galpha proteins and inhibits pheromone signaling in yeast". The Journal of Biological Chemistry. 272 (13): 8679–85. doi:10.1074/jbc.272.13.8679. PMID 9079700. 
  • Buckbinder L, Velasco-Miguel S, Chen Y, Xu N, Talbott R, Gelbert L, Gao J, Seizinger BR, Gutkind JS, Kley N (Jul 1997). "The p53 tumor suppressor targets a novel regulator of G protein signaling". Proceedings of the National Academy of Sciences of the United States of America. 94 (15): 7868–72. doi:10.1073/pnas.94.15.7868. PMC 21521Freely accessible. PMID 9223279. 
  • Luo X, Popov S, Bera AK, Wilkie TM, Muallem S (Mar 2001). "RGS proteins provide biochemical control of agonist-evoked [Ca2+]i oscillations". Molecular Cell. 7 (3): 651–60. doi:10.1016/S1097-2765(01)00211-8. PMID 11463389. 
  • Natochin M, Lipkin VM, Artemyev NO (Jul 1997). "Interaction of human retinal RGS with G-protein alpha-subunits". FEBS Letters. 411 (2-3): 179–82. doi:10.1016/S0014-5793(97)00687-X. PMID 9271201. 
  • Beadling C, Druey KM, Richter G, Kehrl JH, Smith KA (Mar 1999). "Regulators of G protein signaling exhibit distinct patterns of gene expression and target G protein specificity in human lymphocytes". Journal of Immunology. 162 (5): 2677–82. PMID 10072511. 
  • Druey KM, Ugur O, Caron JM, Chen CK, Backlund PS, Jones TL (Jun 1999). "Amino-terminal cysteine residues of RGS16 are required for palmitoylation and modulation of Gi- and Gq-mediated signaling". The Journal of Biological Chemistry. 274 (26): 18836–42. doi:10.1074/jbc.274.26.18836. PMID 10373502. 
  • Pashkov V, Huang J, Parameswara VK, Kedzierski W, Kurrasch DM, Tall GG, Esser V, Gerard RD, Uyeda K, Towle HC, Wilkie TM (Apr 2011). "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. 286 (17): 15116–25. doi:10.1074/jbc.M110.216234. PMID 21357625. 
  • Popov S, Yu K, Kozasa T, Wilkie TM (Jul 1997). "The regulators of G protein signaling (RGS) domains of RGS4, RGS10, and GAIP retain GTPase activating protein activity in vitro". Proceedings of the National Academy of Sciences of the United States of America. 94 (14): 7216–20. doi:10.1073/pnas.94.14.7216. PMC 23796Freely accessible. PMID 9207071. 
  • Popov SG, Krishna UM, Falck JR, Wilkie TM (Jun 2000). "Ca2+/Calmodulin reverses phosphatidylinositol 3,4, 5-trisphosphate-dependent inhibition of regulators of G protein-signaling GTPase-activating protein activity". The Journal of Biological Chemistry. 275 (25): 18962–8. doi:10.1074/jbc.M001128200. PMID 10747990. 
  • Zheng B, Chen D, Farquhar MG (Apr 2000). "MIR16, a putative membrane glycerophosphodiester phosphodiesterase, interacts with RGS16". Proceedings of the National Academy of Sciences of the United States of America. 97 (8): 3999–4004. doi:10.1073/pnas.97.8.3999. PMC 18131Freely accessible. PMID 10760272. 
  • Chatterjee TK, Fisher RA (Aug 2000). "Cytoplasmic, nuclear, and golgi localization of RGS proteins. Evidence for N-terminal and RGS domain sequences as intracellular targeting motifs". The Journal of Biological Chemistry. 275 (31): 24013–21. doi:10.1074/jbc.M002082200. PMID 10791963. 
  • Wieland T, Bahtijari N, Zhou XB, Kleuss C, Simon MI (Sep 2000). "Polarity exchange at the interface of regulators of G protein signaling with G protein alpha-subunits". The Journal of Biological Chemistry. 275 (37): 28500–6. doi:10.1074/jbc.M004187200. PMID 10878019. 
  • Chen C, Wang H, Fong CW, Lin SC (Aug 2001). "Multiple phosphorylation sites in RGS16 differentially modulate its GAP activity". FEBS Letters. 504 (1-2): 16–22. doi:10.1016/S0014-5793(01)02757-0. PMID 11522288. 
  • Derrien A, Druey KM (Dec 2001). "RGS16 function is regulated by epidermal growth factor receptor-mediated tyrosine phosphorylation". The Journal of Biological Chemistry. 276 (51): 48532–8. doi:10.1074/jbc.M108862200. PMID 11602604. 
  • Derrien A, Zheng B, Osterhout JL, Ma YC, Milligan G, Farquhar MG, Druey KM (May 2003). "Src-mediated RGS16 tyrosine phosphorylation promotes RGS16 stability". The Journal of Biological Chemistry. 278 (18): 16107–16. doi:10.1074/jbc.M210371200. PMID 12588871. 
  • Osterhout JL, Waheed AA, Hiol A, Ward RJ, Davey PC, Nini L, Wang J, Milligan G, Jones TL, Druey KM (May 2003). "Palmitoylation regulates regulator of G-protein signaling (RGS) 16 function. II. Palmitoylation of a cysteine residue in the RGS box is critical for RGS16 GTPase accelerating activity and regulation of Gi-coupled signalling". The Journal of Biological Chemistry. 278 (21): 19309–16. doi:10.1074/jbc.M210124200. PMID 12642592. 
  • Hiol A, Davey PC, Osterhout JL, Waheed AA, Fischer ER, Chen CK, Milligan G, Druey KM, Jones TL (May 2003). "Palmitoylation regulates regulators of G-protein signaling (RGS) 16 function. I. Mutation of amino-terminal cysteine residues on RGS16 prevents its targeting to lipid rafts and palmitoylation of an internal cysteine residue". The Journal of Biological Chemistry. 278 (21): 19301–8. doi:10.1074/jbc.M210123200. PMID 12642593. 
  • Johnson EN, Seasholtz TM, Waheed AA, Kreutz B, Suzuki N, Kozasa T, Jones TL, Brown JH, Druey KM (Dec 2003). "RGS16 inhibits signalling through the G alpha 13-Rho axis". Nature Cell Biology. 5 (12): 1095–103. doi:10.1038/ncb1065. PMID 14634662. 
  • Ross EM, Wilkie TM (2000). "GTPase-activating proteins for heterotrimeric G proteins: regulators of G protein signaling (RGS) and RGS-like proteins". Annual Review of Biochemistry. 69: 795–827. doi:10.1146/annurev.biochem.69.1.795. PMID 10966476. 
  • Sierra DA, Gilbert DJ, Householder D, Grishin NV, Yu K, Ukidwe P, Barker SA, He W, Wensel TG, Otero G, Brown G, Copeland NG, Jenkins NA, Wilkie TM (Feb 2002). "Evolution of the regulators of G-protein signaling multigene family in mouse and human". Genomics. 79 (2): 177–85. doi:10.1006/geno.2002.6693. PMID 11829488. 
  • Villasenor A, Wang ZV, Rivera LB, Ocal O, Asterholm IW, Scherer PE, Brekken RA, Cleaver O, Wilkie TM (2010). "Rgs16 and Rgs8 in embryonic endocrine pancreas and mouse models of diabetes". Disease Models & Mechanisms. 3 (9-10): 567–80. doi:10.1242/dmm.003210. PMID 20616094. 
  • Wilkie TM, Kinch L (Oct 2005). "New roles for Galpha and RGS proteins: communication continues despite pulling sisters apart". Current Biology. 15 (20): R843–54. doi:10.1016/j.cub.2005.10.008. PMID 16243026.