RGS19

{{Short description|Protein-coding gene in the species Homo sapiens}}

{{Infobox_gene}}

Regulator of G-protein signaling 19 is a protein that in humans is encoded by the RGS19 gene.{{cite journal |vauthors=De Vries L, Mousli M, Wurmser A, Farquhar MG | title = GAIP, a protein that specifically interacts with the trimeric G protein G alpha i3, is a member of a protein family with a highly conserved core domain | journal = Proc Natl Acad Sci U S A | volume = 92 | issue = 25 | pages = 11916–20 |date=January 1996 | pmid = 8524874 | pmc = 40514 | doi =10.1073/pnas.92.25.11916 | doi-access = free }}{{cite web | title = Entrez Gene: RGS19 regulator of G-protein signalling 19| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10287| accessdate = }}

G proteins mediate a number of cellular processes. The protein encoded by this gene belongs to the RGS (regulators of G-protein signaling) family and specifically interacts with G protein, GAI3. This protein is a guanosine triphosphatase-activating protein that functions to down-regulate Galpha i/Galpha q-linked signaling.{{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= 445–452 |year= 1996 |pmid= 8756726 |doi=10.1016/S0092-8674(00)80117-8 |s2cid=12427406 |doi-access=free }}

Interactions

RGS19 has been shown to interact with GNAO1,{{cite journal |last=De Vries |first=L |author2=Elenko E |author3=Hubler L |author4=Jones T L |author5=Farquhar M G |date=Dec 1996 |title=GAIP is membrane-anchored by palmitoylation and interacts with the activated (GTP-bound) form of G alpha i subunits |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue=26 |pages=15203–8 |location = UNITED STATES| issn = 0027-8424| pmid = 8986788 | bibcode =1996PNAS...9315203D |doi=10.1073/pnas.93.26.15203 |pmc=26381 |doi-access=free }}{{cite journal |last=Woulfe |first=D S |author2=Stadel J M |date=June 1999 |title=Structural basis for the selectivity of the RGS protein, GAIP, for Galphai family members. Identification of a single amino acid determinant for selective interaction of Galphai subunits with GAIP |journal=J. Biol. Chem. |volume=274 |issue=25 |pages=17718–24 |location = UNITED STATES| issn = 0021-9258| pmid = 10364213 |doi=10.1074/jbc.274.25.17718 |doi-access=free }} GIPC1,{{cite journal |last=Lou |first=X |author2=Yano H |author3=Lee F |author4=Chao M V |author5=Farquhar M G |date=March 2001 |title=GIPC and GAIP form a complex with TrkA: a putative link between G protein and receptor tyrosine kinase pathways |journal=Mol. Biol. Cell |volume=12 |issue=3 |pages=615–27 |location = United States| issn = 1059-1524| pmid = 11251075 |pmc=30968 | doi=10.1091/mbc.12.3.615}} OSTM1,{{cite journal |last=Fischer |first=Thierry |author2=De Vries Luc |author3=Meerloo Timo |author4=Farquhar Marilyn Gist |date=July 2003 |title=Promotion of G alpha i3 subunit down-regulation by GIPN, a putative E3 ubiquitin ligase that interacts with RGS-GAIP |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=100 |issue=14 |pages=8270–5 |location = United States| issn = 0027-8424| pmid = 12826607 |doi = 10.1073/pnas.1432965100 | bibcode =2003PNAS..100.8270F |pmc=166218 |doi-access=free }} GNAI1, GNAI3 and GNAZ.{{cite journal |last=Fan |first=X |author2=Brass L F |author3=Poncz M |author4=Spitz F |author5=Maire P |author6=Manning D R |date=October 2000 |title=The alpha subunits of Gz and Gi interact with the eyes absent transcription cofactor Eya2, preventing its interaction with the six class of homeodomain-containing proteins |journal=J. Biol. Chem. |volume=275 |issue=41 |pages=32129–34 |location = UNITED STATES| issn = 0021-9258| pmid = 10906137 |doi = 10.1074/jbc.M004577200 |doi-access=free }}

References

{{Reflist}}

Further reading

{{Refbegin | 2}}

  • {{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= 445–452 |year= 1996 |pmid= 8756726 |doi=10.1016/S0092-8674(00)80117-8 |s2cid=12427406 |doi-access=free }}
  • {{cite journal |vauthors=De Vries L, Elenko E, Hubler L, etal |title=GAIP is membrane-anchored by palmitoylation and interacts with the activated (GTP-bound) form of G alpha i subunits |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 26 |pages= 15203–8 |year= 1997 |pmid= 8986788 |doi=10.1073/pnas.93.26.15203 | pmc=26381 |bibcode=1996PNAS...9315203D |doi-access=free }}
  • {{cite journal |vauthors=Ogier-Denis E, Petiot A, Bauvy C, Codogno P |title=Control of the expression and activity of the Galpha-interacting protein (GAIP) in human intestinal cells |journal=J. Biol. Chem. |volume=272 |issue= 39 |pages= 24599–603 |year= 1997 |pmid= 9305927 |doi=10.1074/jbc.272.39.24599 |doi-access=free }}
  • {{cite journal |vauthors=De Vries L, Elenko E, McCaffery JM, etal |title=RGS-GAIP, a GTPase-activating protein for Galphai heterotrimeric G proteins, is located on clathrin-coated vesicles |journal=Mol. Biol. Cell |volume=9 |issue= 5 |pages= 1123–34 |year= 1998 |pmid= 9571244 |doi= 10.1091/mbc.9.5.1123| pmc=25334 }}
  • {{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= Proc Natl Acad Sci USA

|volume=94

|issue=14

|pages= 7216–20

|year= 1997

|pmid=9207071

|doi=10.1073/pnas.94.14.7216

|pmc=23796|bibcode=1997PNAS...94.7216P|doi-access= free

}}

  • {{cite journal |vauthors=Wang J, Ducret A, Tu Y, etal |title=RGSZ1, a Gz-selective RGS protein in brain. Structure, membrane association, regulation by Galphaz phosphorylation, and relationship to a Gz gtpase-activating protein subfamily |journal=J. Biol. Chem. |volume=273 |issue= 40 |pages= 26014–25 |year= 1998 |pmid= 9748280 |doi=10.1074/jbc.273.40.26014 |doi-access=free }}
  • {{cite journal |vauthors=De Vries L, Lou X, Zhao G, etal |title=GIPC, a PDZ domain containing protein, interacts specifically with the C terminus of RGS-GAIP |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 21 |pages= 12340–5 |year= 1998 |pmid= 9770488 |doi=10.1073/pnas.95.21.12340 | pmc=22833 |bibcode=1998PNAS...9512340D |doi-access=free }}
  • {{cite journal |vauthors=Fischer T, Elenko E, McCaffery JM, etal |title=Clathrin-coated vesicles bearing GAIP possess GTPase-activating protein activity in vitro |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 12 |pages= 6722–7 |year= 1999 |pmid= 10359779 |doi=10.1073/pnas.96.12.6722 | pmc=21982 |bibcode=1999PNAS...96.6722F |doi-access=free }}
  • {{cite journal |vauthors=Woulfe DS, Stadel JM |title=Structural basis for the selectivity of the RGS protein, GAIP, for Galphai family members. Identification of a single amino acid determinant for selective interaction of Galphai subunits with GAIP |journal=J. Biol. Chem. |volume=274 |issue= 25 |pages= 17718–24 |year= 1999 |pmid= 10364213 |doi=10.1074/jbc.274.25.17718 |doi-access=free }}
  • {{cite journal |vauthors=de Alba E, De Vries L, Farquhar MG, Tjandra N |title=Solution structure of human GAIP (Galpha interacting protein): a regulator of G protein signaling |journal=J. Mol. Biol. |volume=291 |issue= 4 |pages= 927–39 |year= 1999 |pmid= 10452897 |doi= 10.1006/jmbi.1999.2989 |url= https://zenodo.org/record/1229890 }}
  • {{cite journal |vauthors=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=10.1073/pnas.97.8.3999 | pmc=18131 |bibcode=2000PNAS...97.3999Z |doi-access=free }}
  • {{cite journal |vauthors=Fischer T, Elenko E, Wan L, etal |title=Membrane-associated GAIP is a phosphoprotein and can be phosphorylated by clathrin-coated vesicles |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 8 |pages= 4040–5 |year= 2000 |pmid= 10760275 |doi=10.1073/pnas.97.8.4040 | pmc=18141 |bibcode=2000PNAS...97.4040F |doi-access=free }}
  • {{cite journal |vauthors=Ogier-Denis E, Pattingre S, El Benna J, Codogno P |title=Erk1/2-dependent phosphorylation of Galpha-interacting protein stimulates its GTPase accelerating activity and autophagy in human colon cancer cells |journal=J. Biol. Chem. |volume=275 |issue= 50 |pages= 39090–5 |year= 2001 |pmid= 10993892 |doi= 10.1074/jbc.M006198200 |doi-access= free }}
  • {{cite journal |vauthors=Ito E, Xie G, Maruyama K, Palmer PP |title=A core-promoter region functions bi-directionally for human opioid-receptor-like gene ORL1 and its 5'-adjacent gene GAIP |journal=J. Mol. Biol. |volume=304 |issue= 3 |pages= 259–70 |year= 2000 |pmid= 11090272 |doi= 10.1006/jmbi.2000.4212 }}
  • {{cite journal |vauthors=Lou X, Yano H, Lee F, etal |title=GIPC and GAIP form a complex with TrkA: a putative link between G protein and receptor tyrosine kinase pathways |journal=Mol. Biol. Cell |volume=12 |issue= 3 |pages= 615–27 |year= 2001 |pmid= 11251075 |doi= 10.1091/mbc.12.3.615| pmc=30968 }}
  • {{cite journal |vauthors=Deloukas P, Matthews LH, Ashurst J, etal |title=The DNA sequence and comparative analysis of human chromosome 20 |journal=Nature |volume=414 |issue= 6866 |pages= 865–71 |year= 2002 |pmid= 11780052 |doi= 10.1038/414865a |bibcode=2001Natur.414..865D |doi-access=free }}
  • {{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 |year=2002 |pmid=11829488 |doi=10.1006/geno.2002.6693 |s2cid=16065132 }}
  • {{cite journal |vauthors=Kirikoshi H, Katoh M |title=Expression of human GIPC1 in normal tissues, cancer cell lines, and primary tumors |journal=Int. J. Mol. Med. |volume=9 |issue= 5 |pages= 509–13 |year= 2002 |pmid= 11956658 |doi= 10.3892/ijmm.9.5.509}}
  • {{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=Xie GX, Han X, Ito E, etal |title=Gene structure, dual-promoters and mRNA alternative splicing of the human and mouse regulator of G protein signaling GAIP/RGS19 |journal=J. Mol. Biol. |volume=325 |issue= 4 |pages= 721–32 |year= 2003 |pmid= 12507475 |doi=10.1016/S0022-2836(02)01283-4 }}
  • {{cite journal |vauthors=Fischer T, De Vries L, Meerloo T, Farquhar MG |title=Promotion of G alpha i3 subunit down-regulation by GIPN, a putative E3 ubiquitin ligase that interacts with RGS-GAIP |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=100 |issue= 14 |pages= 8270–5 |year= 2003 |pmid= 12826607 |doi= 10.1073/pnas.1432965100 | pmc=166218 |bibcode=2003PNAS..100.8270F |doi-access=free }}

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