RGS16

Regulator of G-protein signaling 16

PDB rendering based on 2ik8.

Available structures
PDB	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	• signal transducer activity • GTPase activator activity • calmodulin binding
Cellular component	• membrane fraction • cytoplasm • plasma membrane • membrane raft
Biological process	• visual perception • regulation of G-protein coupled receptor protein signaling pathway • negative regulation of signal transduction • positive regulation of GTPase activity • 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:
155.59 – 155.59 Mb

PubMed search

[1]

[2]

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 (Mar 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.
^ ^a ^b "Entrez Gene: RGS16 regulator of G-protein signalling 16". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6004.
^ 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 (Mar. 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.
^ Beadling, C; Druey K M, Richter G, Kehrl J H, Smith K A (Mar. 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.

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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=24015.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=21521.
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.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=18131.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
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.

PDB gallery

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

RGS16

Interactions

References

Further reading