GNAO1

Guanin nukleotid-vezujući protein (G protein), podjedinica koja aktivira polipeptid O
Guanin nukleotid-vezujući protein (G protein), podjedinica koja aktivira polipeptid O
Identifikatori
Simboli	GNAO1; DKFZp686O0962; G-ALPHA-o; GNAO
Vanjski ID	OMIM: 139311 MGI: 95775 HomoloGene: 39203 GeneCards: GNAO1 Gene
Ontologija gena
Molekularna funkcija	• nucleotidno vezivanje; • aktivnost GTPaze; • aktivnost receptorskog signalnog proteina; • GTP vezivanje;
Biološki proces	• kontrakcija mišića; • prenos signala; • signalni put G-protein spregnutog receptora; • signalni put dopaminskog receptora; • razvoj nervnog sistema; • vođenje aksona; • lokomotorno ponašanje; • regulacija kontrakcije srca;
Pregled RNK izražavanja
	podaci
Ortolozi
Vrsta	Čovek
Entrez	2775
Ensembl	ENSG00000087258
UniProt	P09471
RefSeq (mRNA)	NM_020988
RefSeq (protein)	NP_066268
Lokacija (UCSC)	Chr 16:; 54.78 - 54.95 Mb
PubMed pretraga	[1]

GNAO1, Guanin nukleotid-vezujući protein G(o), podjedinica alfa, je protein koji je kod čoveka kodiran GNAO1 genom.^[1]^[2]^[3]

Interakcije

Za GNAO1 je bilo pokazano da interaguje sa RGS20,^[4] RGS19,^[5]^[6] RIC8A^[7] i RGS5.^[8]^[9]

Reference

^ Murtagh JJ Jr; Eddy R; Shows TB; Moss J; Vaughan M (1991). „Different forms of Go alpha mRNA arise by alternative splicing of transcripts from a single gene on human chromosome 16”. Mol Cell Biol. 11 (2): 1146—55. PMC 359797 . PMID 1899283.
^ Kinoshita M, Nukada T, Asano T, Mori Y, Akaike A, Satoh M, Kaneko S (2001). „Binding of G alpha(o) N terminus is responsible for the voltage-resistant inhibition of alpha(1A) (P/Q-type, Ca(v)2.1) Ca(2+) channels”. J Biol Chem. 276 (31): 28731—8. PMID 11395521. doi:10.1074/jbc.M104806200.
^ „Entrez Gene: GNAO1 guanine nucleotide binding protein (G protein), alpha activating activity polypeptide O”.
^ Pagano, Mario; Jordan J Dedrick; et al. (2008). „Galphao/i-stimulated proteosomal degradation of RGS20: a mechanism for temporal integration of Gs and Gi pathways”. Cell. Signal. England. 20 (6): 1190—7. ISSN 0898-6568. PMID 18407463. doi:10.1016/j.cellsig.2008.02.008.
^ De Vries, L; Elenko E; et al. (1996). „GAIP is membrane-anchored by palmitoylation and interacts with the activated (GTP-bound) form of G alpha i subunits”. Proc. Natl. Acad. Sci. U.S.A. UNITED STATES. 93 (26): 15203—8. ISSN 0027-8424. PMC 26381 . PMID 8986788. doi:10.1073/pnas.93.26.15203.
^ Woulfe, D S; Stadel J M (1999). „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”. J. Biol. Chem. UNITED STATES. 274 (25): 17718—24. ISSN 0021-9258. PMID 10364213. doi:10.1074/jbc.274.25.17718.
^ Tall, Gregory G; Krumins Andrejs M; Gilman Alfred G (2003). „Mammalian Ric-8A (synembryn) is a heterotrimeric Galpha protein guanine nucleotide exchange factor”. J. Biol. Chem. United States. 278 (10): 8356—62. ISSN 0021-9258. PMID 12509430. doi:10.1074/jbc.M211862200.
^ Chen, C; Zheng B; et al. (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. ISSN 0021-9258. PMID 9079700. doi:10.1074/jbc.272.13.8679.
^ Zhou, J; Moroi K; et al. (2001). „Characterization of RGS5 in regulation of G protein-coupled receptor signaling”. Life Sci. England. 68 (13): 1457—69. ISSN 0024-3205. PMID 11253162. doi:10.1016/S0024-3205(01)00939-0.

Literatura

Raymond JR; Mukhin YV; Gelasco A; et al. (2002). „Multiplicity of mechanisms of serotonin receptor signal transduction.”. Pharmacol. Ther. 92 (2-3): 179—212. PMID 11916537. doi:10.1016/S0163-7258(01)00169-3.
Coupry I, Duzic E, Lanier SM (1992). „Factors determining the specificity of signal transduction by guanine nucleotide-binding protein-coupled receptors. II. Preferential coupling of the alpha 2C-adrenergic receptor to the guanine nucleotide-binding protein, Go.”. J. Biol. Chem. 267 (14): 9852—7. PMID 1349607.
Denker BM, Neer EJ, Schmidt CJ (1992). „Mutagenesis of the amino terminus of the alpha subunit of the G protein Go. In vitro characterization of alpha o beta gamma interactions.”. J. Biol. Chem. 267 (9): 6272—7. PMID 1556134.
Yi F, Denker BM, Neer EJ (1991). „Structural and functional studies of cross-linked Go protein subunits.”. J. Biol. Chem. 266 (6): 3900—6. PMID 1899868.
Tsukamoto T; Toyama R; Itoh H; et al. (1991). „Structure of the human gene and two rat cDNAs encoding the alpha chain of GTP-binding regulatory protein Go: two different mRNAs are generated by alternative splicing.”. Proc. Natl. Acad. Sci. U.S.A. 88 (8): 2974—8. PMC 51366 . PMID 1901650. doi:10.1073/pnas.88.8.2974.
Gabrion J; Brabet P; Nguyen Than Dao B; et al. (1990). „Ultrastructural localization of the GTP-binding protein Go in neurons.”. Cell. Signal. 1 (1): 107—23. PMID 2518353. doi:10.1016/0898-6568(89)90025-9.
Lavu S; Clark J; Swarup R; et al. (1988). „Molecular cloning and DNA sequence analysis of the human guanine nucleotide-binding protein Go alpha.”. Biochem. Biophys. Res. Commun. 150 (2): 811—5. PMID 3124840. doi:10.1016/0006-291X(88)90463-9.
Zumbihl R; Breuiller-Fouché M; Carrette J; et al. (1995). „Up-regulation in late pregnancy of both Go1 alpha and Go2 alpha isoforms in human myometrium.”. Eur. J. Pharmacol. 288 (1): 9—15. PMID 7705473.
Grassie MA, Milligan G (1995). „Analysis of the relative interactions between the alpha 2C10 adrenoceptor and the guanine-nucleotide-binding proteins G(o)1 alpha and Gi 2 alpha following co-expression of these polypeptides in rat 1 fibroblasts.”. Biochem. J. 306 (Pt 2): 525—30. PMC 1136549 . PMID 7887906.
Wu HC, Lin CT (1994). „Association of heterotrimeric GTP binding regulatory protein (Go) with mitosis.”. Lab. Invest. 71 (2): 175—81. PMID 8078296.
Nitta K; Uchida K; Kawashima A; et al. (1994). „Identification of GTP-binding proteins in human glomeruli.”. Nippon Jinzo Gakkai shi. 36 (1): 9—12. PMID 8107314.
Georgoussi Z, Carr C, Milligan G (1993). „Direct measurements of in situ interactions of rat brain opioid receptors with the guanine nucleotide-binding protein Go.”. Mol. Pharmacol. 44 (1): 62—9. PMID 8393523.
Laugwitz KL; Allgeier A; Offermanns S; et al. (1996). „The human thyrotropin receptor: a heptahelical receptor capable of stimulating members of all four G protein families.”. Proc. Natl. Acad. Sci. U.S.A. 93 (1): 116—20. PMC 40189 . PMID 8552586. doi:10.1073/pnas.93.1.116.
Kawano N; Ito T; Kitamura H; et al. (1997). „Immunoexpression of the alpha subunit of a guanine nucleotide-binding protein (Go) in pulmonary neuroendocrine cells and neoplasms.”. Pathol. Int. 46 (6): 393—8. PMID 8869990. doi:10.1111/j.1440-1827.1996.tb03629.x.
De Vries L; Elenko E; Hubler L; et al. (1997). „GAIP is membrane-anchored by palmitoylation and interacts with the activated (GTP-bound) form of G alpha i subunits.”. Proc. Natl. Acad. Sci. U.S.A. 93 (26): 15203—8. PMC 26381 . PMID 8986788. doi:10.1073/pnas.93.26.15203.
Valenzuela D; Han X; Mende U; et al. (1997). „G alpha(o) is necessary for muscarinic regulation of Ca2+ channels in mouse heart.”. Proc. Natl. Acad. Sci. U.S.A. 94 (5): 1727—32. PMC 19984 . PMID 9050846. doi:10.1073/pnas.94.5.1727.
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. PMID 9079700. doi:10.1074/jbc.272.13.8679.
Natochin M, Lipkin VM, Artemyev NO (1997). „Interaction of human retinal RGS with G-protein alpha-subunits.”. FEBS Lett. 411 (2-3): 179—82. PMID 9271201. doi:10.1016/S0014-5793(97)00687-X.
Busconi L, Denker BM (1998). „Analysis of the N-terminal binding domain of Go alpha.”. Biochem. J. 328 (Pt 1): 23—31. PMC 1218882 . PMID 9359829.

[pmid1899283-1] Murtagh JJ Jr; Eddy R; Shows TB; Moss J; Vaughan M (1991). „Different forms of Go alpha mRNA arise by alternative splicing of transcripts from a single gene on human chromosome 16”. Mol Cell Biol. 11 (2): 1146—55. PMC 359797 . PMID 1899283.

[pmid11395521-2] Kinoshita M, Nukada T, Asano T, Mori Y, Akaike A, Satoh M, Kaneko S (2001). „Binding of G alpha(o) N terminus is responsible for the voltage-resistant inhibition of alpha(1A) (P/Q-type, Ca(v)2.1) Ca(2+) channels”. J Biol Chem. 276 (31): 28731—8. PMID 11395521. doi:10.1074/jbc.M104806200.

[entrez-3] „Entrez Gene: GNAO1 guanine nucleotide binding protein (G protein), alpha activating activity polypeptide O”.

[pmid18407463-4] Pagano, Mario; Jordan J Dedrick; et al. (2008). „Galphao/i-stimulated proteosomal degradation of RGS20: a mechanism for temporal integration of Gs and Gi pathways”. Cell. Signal. England. 20 (6): 1190—7. ISSN 0898-6568. PMID 18407463. doi:10.1016/j.cellsig.2008.02.008.

[pmid8986788-5] De Vries, L; Elenko E; et al. (1996). „GAIP is membrane-anchored by palmitoylation and interacts with the activated (GTP-bound) form of G alpha i subunits”. Proc. Natl. Acad. Sci. U.S.A. UNITED STATES. 93 (26): 15203—8. ISSN 0027-8424. PMC 26381 . PMID 8986788. doi:10.1073/pnas.93.26.15203.

[pmid10364213-6] Woulfe, D S; Stadel J M (1999). „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”. J. Biol. Chem. UNITED STATES. 274 (25): 17718—24. ISSN 0021-9258. PMID 10364213. doi:10.1074/jbc.274.25.17718.

[pmid12509430-7] Tall, Gregory G; Krumins Andrejs M; Gilman Alfred G (2003). „Mammalian Ric-8A (synembryn) is a heterotrimeric Galpha protein guanine nucleotide exchange factor”. J. Biol. Chem. United States. 278 (10): 8356—62. ISSN 0021-9258. PMID 12509430. doi:10.1074/jbc.M211862200.

[pmid9079700-8] Chen, C; Zheng B; et al. (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. ISSN 0021-9258. PMID 9079700. doi:10.1074/jbc.272.13.8679.

[pmid11253162-9] Zhou, J; Moroi K; et al. (2001). „Characterization of RGS5 in regulation of G protein-coupled receptor signaling”. Life Sci. England. 68 (13): 1457—69. ISSN 0024-3205. PMID 11253162. doi:10.1016/S0024-3205(01)00939-0.

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