RGS16: Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''Regulator of G-protein signaling 16''' is a [[protein]] that in humans is encoded by the ''RGS16'' [[gene]].<ref name="pmid9469939">{{cite journal | vauthors = Snow BE, Antonio L, Suggs S, Siderovski DP | title = Cloning of a retinally abundant regulator of G-protein signaling (RGS-r/RGS16): genomic structure and chromosomal localization of the human gene | journal = Gene | volume = 206 | issue = 2 | pages = 247–53 | date = Jan 1998 | pmid = 9469939 | pmc =  | doi = 10.1016/S0378-1119(97)00593-3 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: RGS16 regulator of G-protein signalling 16| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6004| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_RGS16_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2ik8.
| PDB = {{PDB2|2ik8}}
| Name = Regulator of G-protein signalling 16
| HGNCid = 9997
| Symbol = RGS16
| AltSymbols =; A28-RGS14; A28-RGS14P; RGS-R
| OMIM = 602514
| ECnumber = 
| Homologene = 2196
| MGIid = 108407
| GeneAtlas_image1 = PBB_GE_RGS16_209324_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_RGS16_209325_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004871 |text = signal transducer activity}} {{GNF_GO|id=GO:0005096 |text = GTPase activator activity}} {{GNF_GO|id=GO:0005516 |text = calmodulin binding}}
| Component =
| Process = {{GNF_GO|id=GO:0007601 |text = visual perception}} {{GNF_GO|id=GO:0008277 |text = regulation of G-protein coupled receptor protein signaling pathway}} {{GNF_GO|id=GO:0009968 |text = negative regulation of signal transduction}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 6004
    | Hs_Ensembl = ENSG00000143333
    | Hs_RefseqProtein = NP_002919
    | Hs_RefseqmRNA = NM_002928
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 180834381
    | Hs_GenLoc_end = 180840166
    | Hs_Uniprot = O15492
    | Mm_EntrezGene = 19734
    | Mm_Ensembl = ENSMUSG00000026475
    | Mm_RefseqmRNA = NM_011267
    | Mm_RefseqProtein = NP_035397
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 1
    | Mm_GenLoc_start = 155502566
    | Mm_GenLoc_end = 155507686
    | Mm_Uniprot = Q542U0
  }}
}}
'''Regulator of G-protein signalling 16''', also known as '''RGS16''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RGS16 regulator of G-protein signalling 16| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6004| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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.<ref name="entrez"/>
{{PBB_Summary
| section_title =
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: RGS16 regulator of G-protein signalling 16| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6004| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
RGS16 has been shown to [[Protein-protein interaction|interact]] with [[GNAQ]]<ref name="pmid14634662">{{cite journal | vauthors = Johnson EN, Seasholtz TM, Waheed AA, Kreutz B, Suzuki N, Kozasa T, Jones TL, Brown JH, Druey KM | title = RGS16 inhibits signalling through the G alpha 13-Rho axis | journal = Nature Cell Biology | volume = 5 | issue = 12 | pages = 1095–103 | date = Dec 2003 | pmid = 14634662 | doi = 10.1038/ncb1065 }}</ref> and [[GNAI3]].<ref name=pmid9079700>{{cite journal | vauthors = Chen C, Zheng B, Han J, Lin SC | title = Characterization of a novel mammalian RGS protein that binds to Galpha proteins and inhibits pheromone signaling in yeast | journal = The Journal of Biological Chemistry | volume = 272 | issue = 13 | pages = 8679–85 | date = Mar 1997 | pmid = 9079700 | doi = 10.1074/jbc.272.13.8679 }}</ref><ref name=pmid10072511>{{cite journal | vauthors = Beadling C, Druey KM, Richter G, Kehrl JH, Smith KA | title = Regulators of G protein signaling exhibit distinct patterns of gene expression and target G protein specificity in human lymphocytes | journal = Journal of Immunology | volume = 162 | issue = 5 | pages = 2677–82 | date = Mar 1999 | pmid = 10072511 }}</ref>
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
 
| citations =
* {{cite journal | vauthors = Berman DM, Wilkie TM, Gilman AG | title = GAIP and RGS4 are GTPase-activating proteins for the Gi subfamily of G protein alpha subunits | journal = Cell | volume = 86 | issue = 3 | pages = 445–52 | date = Aug 1996 | pmid = 8756726 | doi = 10.1016/S0092-8674(00)80117-8 }}
*{{cite journal | author=De Vries L, Zheng B, Fischer T, ''et al.'' |title=The regulator of G protein signaling family. |journal=Annu. Rev. Pharmacol. Toxicol. |volume=40 |issue= |pages= 235-71 |year= 2000 |pmid= 10836135 |doi= 10.1146/annurev.pharmtox.40.1.235 }}
* {{cite journal | vauthors = De Vries L, Zheng B, Fischer T, Elenko E, Farquhar MG | title = The regulator of G protein signaling family | journal = Annual Review of Pharmacology and Toxicology | volume = 40 | issue = | pages = 235–71 | year = 2000 | pmid = 10836135 | doi = 10.1146/annurev.pharmtox.40.1.235 }}
*{{cite journal | author=Chen CK, Wieland T, Simon MI |title=RGS-r, a retinal specific RGS protein, binds an intermediate conformation of transducin and enhances recycling. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 23 |pages= 12885-9 |year= 1996 |pmid= 8917514 |doi= }}
* {{cite journal | vauthors = Chen CK, Wieland T, Simon MI | title = RGS-r, a retinal specific RGS protein, binds an intermediate conformation of transducin and enhances recycling | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 93 | issue = 23 | pages = 12885–9 | date = Nov 1996 | pmid = 8917514 | pmc = 24015 | doi = 10.1073/pnas.93.23.12885 }}
*{{cite journal | author=Chen C, Zheng B, Han J, Lin SC |title=Characterization of a novel mammalian RGS protein that binds to Galpha proteins and inhibits pheromone signaling in yeast. |journal=J. Biol. Chem. |volume=272 |issue= 13 |pages= 8679-85 |year= 1997 |pmid= 9079700 |doi= }}
* {{cite journal | vauthors = Chen C, Zheng B, Han J, Lin SC | title = Characterization of a novel mammalian RGS protein that binds to Galpha proteins and inhibits pheromone signaling in yeast | journal = The Journal of Biological Chemistry | volume = 272 | issue = 13 | pages = 8679–85 | date = Mar 1997 | pmid = 9079700 | doi = 10.1074/jbc.272.13.8679 }}
*{{cite journal | author=Buckbinder L, Velasco-Miguel S, Chen Y, ''et al.'' |title=The p53 tumor suppressor targets a novel regulator of G protein signaling. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 15 |pages= 7868-72 |year= 1997 |pmid= 9223279 |doi= }}
* {{cite journal | vauthors = Buckbinder L, Velasco-Miguel S, Chen Y, Xu N, Talbott R, Gelbert L, Gao J, Seizinger BR, Gutkind JS, Kley N | title = The p53 tumor suppressor targets a novel regulator of G protein signaling | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 94 | issue = 15 | pages = 7868–72 | date = Jul 1997 | pmid = 9223279 | pmc = 21521 | doi = 10.1073/pnas.94.15.7868 }}
*{{cite journal | author=Natochin M, Lipkin VM, Artemyev NO |title=Interaction of human retinal RGS with G-protein alpha-subunits. |journal=FEBS Lett. |volume=411 |issue= 2-3 |pages= 179-82 |year= 1997 |pmid= 9271201 |doi= }}
* {{cite journal | vauthors = Luo X, Popov S, Bera AK, Wilkie TM, Muallem S | title = RGS proteins provide biochemical control of agonist-evoked [Ca2+]i oscillations | journal = Molecular Cell | volume = 7 | issue = 3 | pages = 651–60 | date = Mar 2001 | pmid = 11463389 | doi = 10.1016/S1097-2765(01)00211-8 }}
*{{cite journal | author=Snow BE, Antonio L, Suggs S, Siderovski DP |title=Cloning of a retinally abundant regulator of G-protein signaling (RGS-r/RGS16): genomic structure and chromosomal localization of the human gene. |journal=Gene |volume=206 |issue= 2 |pages= 247-53 |year= 1998 |pmid= 9469939 |doi= }}
* {{cite journal | vauthors = Natochin M, Lipkin VM, Artemyev NO | title = Interaction of human retinal RGS with G-protein alpha-subunits | journal = FEBS Letters | volume = 411 | issue = 2–3 | pages = 179–82 | date = Jul 1997 | pmid = 9271201 | doi = 10.1016/S0014-5793(97)00687-X }}
*{{cite journal | author=Beadling C, Druey KM, Richter G, ''et al.'' |title=Regulators of G protein signaling exhibit distinct patterns of gene expression and target G protein specificity in human lymphocytes. |journal=J. Immunol. |volume=162 |issue= 5 |pages= 2677-82 |year= 1999 |pmid= 10072511 |doi= }}
* {{cite journal | vauthors = Beadling C, Druey KM, Richter G, Kehrl JH, Smith KA | title = Regulators of G protein signaling exhibit distinct patterns of gene expression and target G protein specificity in human lymphocytes | journal = Journal of Immunology | volume = 162 | issue = 5 | pages = 2677–82 | date = Mar 1999 | pmid = 10072511 | doi =  }}
*{{cite journal | author=Druey KM, Ugur O, Caron JM, ''et al.'' |title=Amino-terminal cysteine residues of RGS16 are required for palmitoylation and modulation of Gi- and Gq-mediated signaling. |journal=J. Biol. Chem. |volume=274 |issue= 26 |pages= 18836-42 |year= 1999 |pmid= 10373502 |doi=  }}
* {{cite journal | vauthors = Druey KM, Ugur O, Caron JM, Chen CK, Backlund PS, Jones TL | title = Amino-terminal cysteine residues of RGS16 are required for palmitoylation and modulation of Gi- and Gq-mediated signaling | journal = The Journal of Biological Chemistry | volume = 274 | issue = 26 | pages = 18836–42 | date = Jun 1999 | pmid = 10373502 | doi = 10.1074/jbc.274.26.18836 }}
*{{cite journal | author=Popov SG, Krishna UM, Falck JR, Wilkie TM |title=Ca2+/Calmodulin reverses phosphatidylinositol 3,4, 5-trisphosphate-dependent inhibition of regulators of G protein-signaling GTPase-activating protein activity. |journal=J. Biol. Chem. |volume=275 |issue= 25 |pages= 18962-8 |year= 2000 |pmid= 10747990 |doi= 10.1074/jbc.M001128200 }}
* {{cite journal | vauthors = Pashkov V, Huang J, Parameswara VK, Kedzierski W, Kurrasch DM, Tall GG, Esser V, Gerard RD, Uyeda K, Towle HC, Wilkie TM | title = Regulator of G protein signaling (RGS16) inhibits hepatic fatty acid oxidation in a carbohydrate response element-binding protein (ChREBP)-dependent manner | journal = The Journal of Biological Chemistry | volume = 286 | issue = 17 | pages = 15116–25 | date = Apr 2011 | pmid = 21357625 | doi = 10.1074/jbc.M110.216234 | pmc=3083217}}
*{{cite journal | author=Zheng B, Chen D, Farquhar MG |title=MIR16, a putative membrane glycerophosphodiester phosphodiesterase, interacts with RGS16. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 8 |pages= 3999-4004 |year= 2000 |pmid= 10760272 |doi= }}
* {{cite journal | vauthors = Popov S, Yu K, Kozasa T, Wilkie TM | title = The regulators of G protein signaling (RGS) domains of RGS4, RGS10, and GAIP retain GTPase activating protein activity in vitro | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 94 | issue = 14 | pages = 7216–20 | date = Jul 1997 | pmid = 9207071 | pmc = 23796 | doi = 10.1073/pnas.94.14.7216 }}
*{{cite journal | author=Chatterjee TK, Fisher RA |title=Cytoplasmic, nuclear, and golgi localization of RGS proteins. Evidence for N-terminal and RGS domain sequences as intracellular targeting motifs. |journal=J. Biol. Chem. |volume=275 |issue= 31 |pages= 24013-21 |year= 2000 |pmid= 10791963 |doi= 10.1074/jbc.M002082200 }}
* {{cite journal | vauthors = Popov SG, Krishna UM, Falck JR, Wilkie TM | title = Ca2+/Calmodulin reverses phosphatidylinositol 3,4, 5-trisphosphate-dependent inhibition of regulators of G protein-signaling GTPase-activating protein activity | journal = The Journal of Biological Chemistry | volume = 275 | issue = 25 | pages = 18962–8 | date = Jun 2000 | pmid = 10747990 | doi = 10.1074/jbc.M001128200 }}
*{{cite journal | author=Wieland T, Bahtijari N, Zhou XB, ''et al.'' |title=Polarity exchange at the interface of regulators of G protein signaling with G protein alpha-subunits. |journal=J. Biol. Chem. |volume=275 |issue= 37 |pages= 28500-6 |year= 2000 |pmid= 10878019 |doi= 10.1074/jbc.M004187200 }}
* {{cite journal | vauthors = Zheng B, Chen D, Farquhar MG | title = MIR16, a putative membrane glycerophosphodiester phosphodiesterase, interacts with RGS16 | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 97 | issue = 8 | pages = 3999–4004 | date = Apr 2000 | pmid = 10760272 | pmc = 18131 | doi = 10.1073/pnas.97.8.3999 }}
*{{cite journal | author=Chen C, Wang H, Fong CW, Lin SC |title=Multiple phosphorylation sites in RGS16 differentially modulate its GAP activity. |journal=FEBS Lett. |volume=504 |issue= 1-2 |pages= 16-22 |year= 2001 |pmid= 11522288 |doi= }}
* {{cite journal | vauthors = Chatterjee TK, Fisher RA | title = Cytoplasmic, nuclear, and golgi localization of RGS proteins. Evidence for N-terminal and RGS domain sequences as intracellular targeting motifs | journal = The Journal of Biological Chemistry | volume = 275 | issue = 31 | pages = 24013–21 | date = Aug 2000 | pmid = 10791963 | doi = 10.1074/jbc.M002082200 }}
*{{cite journal | author=Derrien A, Druey KM |title=RGS16 function is regulated by epidermal growth factor receptor-mediated tyrosine phosphorylation. |journal=J. Biol. Chem. |volume=276 |issue= 51 |pages= 48532-8 |year= 2002 |pmid= 11602604 |doi= 10.1074/jbc.M108862200 }}
* {{cite journal | vauthors = Wieland T, Bahtijari N, Zhou XB, Kleuss C, Simon MI | title = Polarity exchange at the interface of regulators of G protein signaling with G protein alpha-subunits | journal = The Journal of Biological Chemistry | volume = 275 | issue = 37 | pages = 28500–6 | date = Sep 2000 | pmid = 10878019 | doi = 10.1074/jbc.M004187200 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |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 }}
* {{cite journal | vauthors = Chen C, Wang H, Fong CW, Lin SC | title = Multiple phosphorylation sites in RGS16 differentially modulate its GAP activity | journal = FEBS Letters | volume = 504 | issue = 1–2 | pages = 16–22 | date = Aug 2001 | pmid = 11522288 | doi = 10.1016/S0014-5793(01)02757-0 }}
*{{cite journal | author=Derrien A, Zheng B, Osterhout JL, ''et al.'' |title=Src-mediated RGS16 tyrosine phosphorylation promotes RGS16 stability. |journal=J. Biol. Chem. |volume=278 |issue= 18 |pages= 16107-16 |year= 2003 |pmid= 12588871 |doi= 10.1074/jbc.M210371200 }}
* {{cite journal | vauthors = Derrien A, Druey KM | title = RGS16 function is regulated by epidermal growth factor receptor-mediated tyrosine phosphorylation | journal = The Journal of Biological Chemistry | volume = 276 | issue = 51 | pages = 48532–8 | date = Dec 2001 | pmid = 11602604 | doi = 10.1074/jbc.M108862200 }}
*{{cite journal | author=Osterhout JL, Waheed AA, Hiol A, ''et al.'' |title=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. |journal=J. Biol. Chem. |volume=278 |issue= 21 |pages= 19309-16 |year= 2003 |pmid= 12642592 |doi= 10.1074/jbc.M210124200 }}
* {{cite journal | vauthors = Derrien A, Zheng B, Osterhout JL, Ma YC, Milligan G, Farquhar MG, Druey KM | title = Src-mediated RGS16 tyrosine phosphorylation promotes RGS16 stability | journal = The Journal of Biological Chemistry | volume = 278 | issue = 18 | pages = 16107–16 | date = May 2003 | pmid = 12588871 | doi = 10.1074/jbc.M210371200 }}
*{{cite journal | author=Hiol A, Davey PC, Osterhout JL, ''et al.'' |title=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. |journal=J. Biol. Chem. |volume=278 |issue= 21 |pages= 19301-8 |year= 2003 |pmid= 12642593 |doi= 10.1074/jbc.M210123200 }}
* {{cite journal | vauthors = Osterhout JL, Waheed AA, Hiol A, Ward RJ, Davey PC, Nini L, Wang J, Milligan G, Jones TL, Druey KM | title = 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 | journal = The Journal of Biological Chemistry | volume = 278 | issue = 21 | pages = 19309–16 | date = May 2003 | pmid = 12642592 | doi = 10.1074/jbc.M210124200 }}
*{{cite journal | author=Johnson EN, Seasholtz TM, Waheed AA, ''et al.'' |title=RGS16 inhibits signalling through the G alpha 13-Rho axis. |journal=Nat. Cell Biol. |volume=5 |issue= 12 |pages= 1095-103 |year= 2004 |pmid= 14634662 |doi= 10.1038/ncb1065 }}
* {{cite journal | vauthors = Hiol A, Davey PC, Osterhout JL, Waheed AA, Fischer ER, Chen CK, Milligan G, Druey KM, Jones TL | title = 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 | journal = The Journal of Biological Chemistry | volume = 278 | issue = 21 | pages = 19301–8 | date = May 2003 | pmid = 12642593 | doi = 10.1074/jbc.M210123200 }}
}}
* {{cite journal | vauthors = Johnson EN, Seasholtz TM, Waheed AA, Kreutz B, Suzuki N, Kozasa T, Jones TL, Brown JH, Druey KM | title = RGS16 inhibits signalling through the G alpha 13-Rho axis | journal = Nature Cell Biology | volume = 5 | issue = 12 | pages = 1095–103 | date = Dec 2003 | pmid = 14634662 | doi = 10.1038/ncb1065 }}
* {{cite journal | vauthors = Ross EM, Wilkie TM | title = GTPase-activating proteins for heterotrimeric G proteins: regulators of G protein signaling (RGS) and RGS-like proteins | journal = Annual Review of Biochemistry | volume = 69 | pages = 795–827 | year = 2000 | pmid = 10966476 | doi = 10.1146/annurev.biochem.69.1.795 }}
* {{cite journal | vauthors = 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 | title = Evolution of the regulators of G-protein signaling multigene family in mouse and human | journal = Genomics | volume = 79 | issue = 2 | pages = 177–85 | date = Feb 2002 | pmid = 11829488 | doi = 10.1006/geno.2002.6693 }} 
* {{cite journal | vauthors = Villasenor A, Wang ZV, Rivera LB, Ocal O, Asterholm IW, Scherer PE, Brekken RA, Cleaver O, Wilkie TM | title = Rgs16 and Rgs8 in embryonic endocrine pancreas and mouse models of diabetes | journal = Disease Models & Mechanisms | volume = 3 | issue = 9–10 | pages = 567–80 | year = 2010 | pmid = 20616094 | doi = 10.1242/dmm.003210 | pmc=2931535}}
* {{cite journal | vauthors = Wilkie TM, Kinch L | title = New roles for Galpha and RGS proteins: communication continues despite pulling sisters apart | journal = Current Biology | volume = 15 | issue = 20 | pages = R843-54 | date = Oct 2005 | pmid = 16243026 | doi = 10.1016/j.cub.2005.10.008 }}
{{refend}}
{{refend}}


{{protein-stub}}
{{PDB Gallery|geneid=6004}}
{{WikiDoc Sources}}

Latest revision as of 02:00, 27 October 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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

Function

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

  1. ↑ 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.
  2. ↑ 2.0 2.1 "Entrez Gene: RGS16 regulator of G-protein signalling 16".
  3. ↑ 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.
  4. ↑ 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.
  5. ↑ 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

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