GNAQ

Last updated
GNAQ
Protein GNAQ PDB 2bcj.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases GNAQ , CMC1, G-ALPHA-q, GAQ, SWS, G protein subunit alpha q
External IDs OMIM: 600998 MGI: 95776 HomoloGene: 1566 GeneCards: GNAQ
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_002072

NM_008139

RefSeq (protein)

NP_002063
NP_002063.2

NP_032165

Location (UCSC) Chr 9: 77.72 – 78.03 Mb Chr 19: 16.11 – 16.36 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Guanine nucleotide-binding protein G(q) subunit alpha is a protein that in humans is encoded by the GNAQ gene. [5] Together with GNA11 (its paralogue), it functions as a Gq alpha subunit. [6]

Function

Guanine nucleotide-binding proteins are a family of heterotrimeric proteins that couple cell surface, 7-transmembrane domain receptors to intracellular signaling pathways. Receptor activation catalyzes the exchange of GDP for GTP bound to the inactive G protein alpha subunit resulting in a conformational change and dissociation of the complex. The G protein alpha and beta-gamma subunits are capable of regulating various cellular effectors. Activation is terminated by a GTPase intrinsic to the G-alpha subunit. G-alpha-q is the alpha subunit of one of the heterotrimeric GTP-binding proteins that mediates stimulation of phospholipase C-beta (MIM 600230).[supplied by OMIM] [7]

Mutations in this gene have been found associated to cases of Sturge–Weber syndrome and port-wine stains. [8]

Interactions

GNAQ has been shown to interact with:

See also

Related Research Articles

<span class="mw-page-title-main">Heterotrimeric G protein</span> Class of enzymes

Heterotrimeric G protein, also sometimes referred to as the "large" G proteins are membrane-associated G proteins that form a heterotrimeric complex. The biggest non-structural difference between heterotrimeric and monomeric G protein is that heterotrimeric proteins bind to their cell-surface receptors, called G protein-coupled receptors, directly. These G proteins are made up of alpha (α), beta (β) and gamma (γ) subunits. The alpha subunit is attached to either a GTP or GDP, which serves as an on-off switch for the activation of G-protein.

G12/G13 alpha subunits are alpha subunits of heterotrimeric G proteins that link cell surface G protein-coupled receptors primarily to guanine nucleotide exchange factors for the Rho small GTPases to regulate the actin cytoskeleton. Together, these two proteins comprise one of the four classes of G protein alpha subunits. G protein alpha subunits bind to guanine nucleotides and function in a regulatory cycle, and are active when bound to GTP but inactive and associated with the G beta-gamma complex when bound to GDP. G12/G13 are not targets of pertussis toxin or cholera toxin, as are other classes of G protein alpha subunits.

<span class="mw-page-title-main">G alpha subunit</span>

G alpha subunits are one of the three types of subunit of guanine nucleotide binding proteins, which are membrane-associated, heterotrimeric G proteins.

<span class="mw-page-title-main">GNB1</span> Protein-coding gene in the species Homo sapiens

Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 is a protein that in humans is encoded by the GNB1 gene.

<span class="mw-page-title-main">GNAO1</span> Protein-coding gene in the species Homo sapiens

Guanine nucleotide-binding protein G(o) subunit alpha is a protein that in humans is encoded by the GNAO1 gene.

<span class="mw-page-title-main">GNAZ</span> Protein-coding gene in the species Homo sapiens

Guanine nucleotide-binding protein G(z) subunit alpha is a protein that in humans is encoded by the GNAZ gene.

<span class="mw-page-title-main">GNB2</span> Protein-coding gene in the species Homo sapiens

Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-2 is a protein that in humans is encoded by the GNB2 gene.

<span class="mw-page-title-main">GNG2</span> Protein-coding gene in the species Homo sapiens

Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 is a protein that in humans is encoded by the GNG2 gene.

<span class="mw-page-title-main">GNB5</span> Protein-coding gene in the species Homo sapiens

Guanine nucleotide-binding protein subunit beta-5 is a protein that in humans is encoded by the GNB5 gene. Alternatively spliced transcript variants encoding different isoforms exist.

<span class="mw-page-title-main">GNAT2</span> Protein-coding gene in the species Homo sapiens

Guanine nucleotide-binding protein G(t) subunit alpha-2 is a protein that in humans is encoded by the GNAT2 gene.

<span class="mw-page-title-main">GNG12</span> Protein-coding gene in the species Homo sapiens

Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-12 is a protein that in humans is encoded by the GNG12 gene.

<span class="mw-page-title-main">GNG3</span> Protein-coding gene in the species Homo sapiens

Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-3 is a protein that in humans is encoded by the GNG3 gene.

<span class="mw-page-title-main">GNB4</span> Protein-coding gene in the species Homo sapiens

Guanine nucleotide-binding protein subunit beta-4 is a protein that in humans is encoded by the GNB4 gene.

<span class="mw-page-title-main">GNAL</span> Protein-coding gene in the species Homo sapiens

Guanine nucleotide-binding protein G(olf) subunit alpha is a protein that in humans is encoded by the GNAL gene. Its main product is the heterotrimeric G-protein alpha subunit Golf-α, a member of the Gs alpha subunit family that is a key component of G protein-coupled receptor-regulated adenylyl cyclase signal transduction pathways in the olfactory system and the striatum in the brain. It also mediated D1 receptor signalling in the striatum and is hence involved in motor control.

<span class="mw-page-title-main">GNA13</span> Protein-coding gene in the species Homo sapiens

Guanine nucleotide-binding protein subunit alpha-13 is a protein that in humans is encoded by the GNA13 gene.

<span class="mw-page-title-main">GNAI3</span> Protein-coding gene in humans

Guanine nucleotide-binding protein G(k) subunit alpha is a protein that in humans is encoded by the GNAI3 gene.

<span class="mw-page-title-main">GNA11</span> Protein-coding gene in the species Homo sapiens

Guanine nucleotide-binding protein subunit alpha-11 is a protein that in humans is encoded by the GNA11 gene. Together with GNAQ, it functions as a Gq alpha subunit.

<span class="mw-page-title-main">GNA12</span> Protein-coding gene in the species Homo sapiens

Guanine nucleotide-binding protein subunit alpha-12 is a protein that in humans is encoded by the GNA12 gene.

<span class="mw-page-title-main">GNAT3</span> Protein-coding gene in the species Homo sapiens

Guanine nucleotide-binding protein G(t) subunit alpha-3, also known as gustducin alpha-3 chain, is a protein subunit that in humans is encoded by the GNAT3 gene.

<span class="mw-page-title-main">GoLoco motif</span> Protein structural motif

GoLoco motif is a protein structural motif. In heterotrimeric G-protein signalling, cell surface receptors (GPCRs) are coupled to membrane-associated heterotrimers comprising a GTP-hydrolyzing subunit G-alpha and a G-beta/G-gamma dimer. The inactive form contains the alpha subunit bound to GDP and complexes with the beta and gamma subunit. When the ligand is associated to the receptor, GDP is displaced from G-alpha and GTP is bound. The GTP/G-alpha complex dissociates from the trimer and associates to an effector until the intrinsic GTPase activity of G-alpha returns the protein to GDP bound form. Reassociation of GDP-bound G-alpha with G-beta/G-gamma dimer terminates the signal. Several mechanisms regulate the signal output at different stage of the G-protein cascade. Two classes of intracellular proteins act as inhibitors of G protein activation: GTPase activating proteins (GAPs), which enhance GTP hydrolysis, and guanine dissociation inhibitors (GDIs), which inhibit GDP dissociation. The GoLoco or G-protein regulatory (GPR) motif found in various G-protein regulators. acts as a GDI on G-alpha(i).

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000156052 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000024639 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Dong Q, Shenker A, Way J, Haddad BR, Lin K, Hughes MR, McBride OW, Spiegel AM, Battey J (February 1997). "Molecular cloning of human G alpha q cDNA and chromosomal localization of the G alpha q gene (GNAQ) and a processed pseudogene". Genomics. 30 (3): 470–75. doi:10.1006/geno.1995.1267. PMID   8825633.
  6. 139313 GUANINE NUCLEOTIDE-BINDING PROTEIN, ALPHA-11; GNA11 at OMIM. Retrieved January 1, 2015.
  7. "Entrez Gene: GNAQ guanine nucleotide binding protein (G protein), q polypeptide".
  8. Shirley MD, Tang H, Gallione CJ, Baugher JD, Frelin LP, Cohen B, North PE, Marchuk DA, Comi AM, Pevsner J (May 23, 2013). "Sturge-Weber syndrome and port-wine stains caused by somatic mutation in GNAQ". The New England Journal of Medicine. 368 (21): 1971–9. doi:10.1056/NEJMoa1213507. PMC   3749068 . PMID   23656586.
  9. Day PW, Carman CV, Sterne-Marr R, Benovic JL, Wedegaertner PB (August 2003). "Differential interaction of GRK2 with members of the G alpha q family". Biochemistry. 42 (30): 9176–84. doi:10.1021/bi034442+. PMID   12885252.
  10. Ma YC, Huang XY (October 1998). "Identification of the binding site for Gqalpha on its effector Bruton's tyrosine kinase". Proc. Natl. Acad. Sci. U.S.A. 95 (21): 12197–201. Bibcode:1998PNAS...9512197M. doi: 10.1073/pnas.95.21.12197 . PMC   22808 . PMID   9770463.
  11. Druey KM, Sullivan BM, Brown D, Fischer ER, Watson N, Blumer KJ, Gerfen CR, Scheschonka A, Kehrl JH (July 1998). "Expression of GTPase-deficient Gialpha2 results in translocation of cytoplasmic RGS4 to the plasma membrane". J. Biol. Chem. 273 (29): 18405–10. doi: 10.1074/jbc.273.29.18405 . PMID   9660808.
  12. Klattenhoff C, Montecino M, Soto X, Guzmán L, Romo X, García MA, Mellstrom B, Naranjo JR, Hinrichs MV, Olate J (May 2003). "Human brain synembryn interacts with Gsalpha and Gqalpha and is translocated to the plasma membrane in response to isoproterenol and carbachol". J. Cell. Physiol. 195 (2): 151–7. doi:10.1002/jcp.10300. hdl: 10533/174200 . PMID   12652642. S2CID   84975473.
  13. Tall GG, Krumins AM, Gilman AG (March 2003). "Mammalian Ric-8A (synembryn) is a heterotrimeric Galpha protein guanine nucleotide exchange factor". J. Biol. Chem. 278 (10): 8356–62. doi: 10.1074/jbc.M211862200 . PMID   12509430.
  14. Rochdi MD, Watier V, La Madeleine C, Nakata H, Kozasa T, Parent JL (October 2002). "Regulation of GTP-binding protein alpha q (Galpha q) signaling by the ezrin-radixin-moesin-binding phosphoprotein-50 (EBP50)". J. Biol. Chem. 277 (43): 40751–9. doi: 10.1074/jbc.M207910200 . PMID   12193606.

Further reading