RGS16

From Wikipedia, the free encyclopedia

Regulator of G-protein signaling 16

PDB rendering based on 2ik8.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
2BT2, 2IK8

Identifiers

Symbols

RGS16; A28-RGS14; A28-RGS14P; RGS-R

External IDs

OMIM: 602514 MGI: 108407 HomoloGene: 2196 GeneCards: RGS16 Gene

Gene Ontology
Molecular function	• GTPase activator activity • protein binding • calmodulin binding
Cellular component	• cytoplasm • plasma membrane
Biological process	• visual perception • regulation of G-protein coupled receptor protein signaling pathway • termination of G-protein coupled receptor signaling pathway • positive regulation of GTPase activity
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 1:
182.57 – 182.57 Mb

Chr 1:
153.74 – 153.75 Mb

PubMed search

Regulator of G-protein signaling 16 is a protein that in humans is encoded by the RGS16 gene.^[1]^[2]

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.^[2]

Interactions

RGS16 has been shown to interact with GNAQ^[3] and GNAI3.^[4]^[5]

References

↑ Snow BE, Antonio L, Suggs S, Siderovski DP (March 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.
↑ 2.0 2.1 "Entrez Gene: RGS16 regulator of G-protein signalling 16".
↑ Johnson EN, Seasholtz TM, Waheed AA, Kreutz B, Suzuki N, Kozasa T, Jones TL, Brown JH, Druey KM (2003). "RGS16 inhibits signalling through the G alpha 13-Rho axis.". Nat Cell Biol 5 (12): 1095–103. doi:10.1038/ncb1065. PMID 14634662.
↑ Chen, C; Zheng B, Han J, Lin S C (March 1997). "Characterization of a novel mammalian RGS protein that binds to Galpha proteins and inhibits pheromone signaling in yeast". J. Biol. Chem. (UNITED STATES) 272 (13): 8679–85. doi:10.1074/jbc.272.13.8679. ISSN 0021-9258. PMID 9079700. Cite uses deprecated parameters (help)
↑ Beadling, C; Druey K M, Richter G, Kehrl J H, Smith K A (March 1999). "Regulators of G protein signaling exhibit distinct patterns of gene expression and target G protein specificity in human lymphocytes". J. Immunol. (UNITED STATES) 162 (5): 2677–82. ISSN 0022-1767. PMID 10072511. Cite uses deprecated parameters (help)

Berman DM, Wilkie TM, Gilman AG (1996). "GAIP and RGS4 are GTPase-activating proteins for the Gi subfamily of G protein alpha subunits.". Cell 86 (3): 445–452. doi:10.1016/S0092-8674(00)80117-8. PMID 8756726.
De Vries L, Zheng B, Fischer T, et al. (2000). "The regulator of G protein signaling family.". Annu. Rev. Pharmacol. Toxicol. 40: 235–71. doi:10.1146/annurev.pharmtox.40.1.235. PMID 10836135.
Chen CK, Wieland T, Simon MI (1996). "RGS-r, a retinal specific RGS protein, binds an intermediate conformation of transducin and enhances recycling.". Proc. Natl. Acad. Sci. U.S.A. 93 (23): 12885–9. doi:10.1073/pnas.93.23.12885. PMC 24015. PMID 8917514.
Chen C, Zheng B, Han J, Lin SC (1997). "Characterization of a novel mammalian RGS protein that binds to Galpha proteins and inhibits pheromone signaling in yeast.". J. Biol. Chem. 272 (13): 8679–85. doi:10.1074/jbc.272.13.8679. PMID 9079700.
Buckbinder L, Velasco-Miguel S, Chen Y, et al. (1997). "The p53 tumor suppressor targets a novel regulator of G protein signaling.". Proc. Natl. Acad. Sci. U.S.A. 94 (15): 7868–72. doi:10.1073/pnas.94.15.7868. PMC 21521. PMID 9223279.
Luo X, Popov S, Bera AK, Wilkie TM, Muallem S (2001). "RGS proteins provide biochemical control of agonist-evoked [Ca2+]i oscillations". Molecular Cell 7 (3): 651–660. doi:10.1016/S1097-2765(01)00211-8. PMID 11463389.
Natochin M, Lipkin VM, Artemyev NO (1997). "Interaction of human retinal RGS with G-protein alpha-subunits.". FEBS Lett. 411 (2–3): 179–82. doi:10.1016/S0014-5793(97)00687-X. PMID 9271201.
Beadling C, Druey KM, Richter G, et al. (1999). "Regulators of G protein signaling exhibit distinct patterns of gene expression and target G protein specificity in human lymphocytes". J. Immunol. 162 (5): 2677–82. PMID 10072511.
Druey KM, Ugur O, Caron JM, et al. (1999). "Amino-terminal cysteine residues of RGS16 are required for palmitoylation and modulation of Gi- and Gq-mediated signaling". J. Biol. Chem. 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 (2011). "Regulator of G protein signaling (RGS16) inhibits hepatic fatty acid oxidation in a carbohydrate response element-binding protein (ChREBP)-dependent manner.". J Biol Chem 286 (17): 15116–15125. doi:10.1074/jbc.M110.216234. PMID 21357625.
Popov S, Yu K, Kozasa T, Wilkie TM (1997). "The regulators of G protein signaling (RGS) domains of RGS4, RGS10 and GAIP retain GTPase activating protein activity in vitro". Proc Natl Acad Sci USA 94 (14): 7216–20. doi:10.1073/pnas.94.14.7216. PMC 23796. PMID 9207071.
Popov SG, Krishna UM, Falck JR, Wilkie TM (2000). "Ca2+/Calmodulin reverses phosphatidylinositol 3,4, 5-trisphosphate-dependent inhibition of regulators of G protein-signaling GTPase-activating protein activity". J. Biol. Chem. 275 (25): 18962–8. doi:10.1074/jbc.M001128200. PMID 10747990.
Zheng B, Chen D, Farquhar MG (2000). "MIR16, a putative membrane glycerophosphodiester phosphodiesterase, interacts with RGS16". Proc. Natl. Acad. Sci. U.S.A. 97 (8): 3999–4004. doi:10.1073/pnas.97.8.3999. PMC 18131. PMID 10760272.
Chatterjee TK, Fisher RA (2000). "Cytoplasmic, nuclear, and golgi localization of RGS proteins. Evidence for N-terminal and RGS domain sequences as intracellular targeting motifs". J. Biol. Chem. 275 (31): 24013–21. doi:10.1074/jbc.M002082200. PMID 10791963.
Wieland T, Bahtijari N, Zhou XB, et al. (2000). "Polarity exchange at the interface of regulators of G protein signaling with G protein alpha-subunits". J. Biol. Chem. 275 (37): 28500–6. doi:10.1074/jbc.M004187200. PMID 10878019.
Chen C, Wang H, Fong CW, Lin SC (2001). "Multiple phosphorylation sites in RGS16 differentially modulate its GAP activity". FEBS Lett. 504 (1–2): 16–22. doi:10.1016/S0014-5793(01)02757-0. PMID 11522288.
Derrien A, Druey KM (2002). "RGS16 function is regulated by epidermal growth factor receptor-mediated tyrosine phosphorylation". J. Biol. Chem. 276 (51): 48532–8. doi:10.1074/jbc.M108862200. PMID 11602604.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Derrien A, Zheng B, Osterhout JL, et al. (2003). "Src-mediated RGS16 tyrosine phosphorylation promotes RGS16 stability". J. Biol. Chem. 278 (18): 16107–16. doi:10.1074/jbc.M210371200. PMID 12588871.
Osterhout JL, Waheed AA, Hiol A, et al. (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". J. Biol. Chem. 278 (21): 19309–16. doi:10.1074/jbc.M210124200. PMID 12642592.
Hiol A, Davey PC, Osterhout JL, et al. (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". J. Biol. Chem. 278 (21): 19301–8. doi:10.1074/jbc.M210123200. PMID 12642593.
Johnson EN, Seasholtz TM, Waheed AA, et al. (2004). "RGS16 inhibits signalling through the G alpha 13-Rho axis". Nat. Cell Biol. 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 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 (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): 567–580. doi:10.1242/dmm.003210. PMID 20616094.
Wilkie TM, Kinch L (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.

PDB gallery

2ik8: Crystal structure of the heterodimeric complex of human RGS16 and activated Gi alpha 1

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RGS16

Interactions

References

Further reading