The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

GPR160  -  G protein-coupled receptor 160

Homo sapiens

Synonyms: G-protein coupled receptor GPCR1, GPCR1, GPCR150, hGPCR1
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of GPR160


Psychiatry related information on GPR160

  • Many drugs of abuse signal through receptors that couple to G proteins (GPCRs), so the factors that control GPCR signaling are likely to be important to the understanding of drug abuse [6].
  • Given the complexity of neurological disorders such as ischemic stroke, Alzheimer's disease and epilepsy, exploitation mGlu receptor-associated GPCR interactions may prove efficacious in the treatment of such disorders [7].

High impact information on GPR160

  • Future high-resolution structural studies of rhodopsin and other GPCRs will form a basis to elucidate the detailed molecular mechanism of GPCR-mediated signal transduction [8].
  • Significantly, GPCR-containing CCPs are also functionally distinct, as their surface residence time is regulated locally by GPCR cargo via PDZ-dependent linkage to the actin cytoskeleton [9].
  • Our results reveal a novel function of betaarr1 as a cytoplasm-nucleus messenger in GPCR signaling and elucidate an epigenetic mechanism for direct GPCR signaling from cell membrane to the nucleus through signal-dependent histone modification [10].
  • (2005) provide evidence that beta-arrestin 1 moves to the nucleus in response to GPCR stimulation, where it regulates gene expression by facilitating histone acetylation at specific gene promoters [11].
  • A nuclear function of beta-arrestin1 in GPCR signaling: regulation of histone acetylation and gene transcription [10].

Chemical compound and disease context of GPR160


Biological context of GPR160

  • In addition, GRK phosphorylation by several other kinases has recently been shown to modulate its functionality, thus putting forward new feedback mechanisms connecting different signalling pathways to G protein-coupled receptors (GPCR) regulation [17].
  • Protease-activated receptor 1 (PAR1), a G protein-coupled receptor (GPCR) for thrombin, has been correlated with cell proliferation [18].
  • Existence of multiple caveolin-rich microdomains and their expression of multiple modulators of signalling strengthen the evidence that caveolins and lipid rafts/caveolae organize and regulate GPCR signal transduction in eukaryotic cells [19].
  • G protein-coupled receptor kinases (GRKs) and arrestins are key participants in the canonical pathways leading to phosphorylation-dependent GPCR desensitization, endocytosis, intracellular trafficking and resensitization as well as in the modulation of important intracellular signaling cascades by GPCR [20].
  • We show that inhibition of proHB-EGF processing blocks GPCR-induced EGFR transactivation and downstream signals [21].

Anatomical context of GPR160

  • We hypothesized that the microtubular and actin cytoskeletons influence the expression and function of lipid rafts/caveolae, thereby regulating the distribution of GPCR signaling components that promote cAMP formation [22].
  • Microtubules and actin filaments regulate plasma membrane topography, but their role in compartmentation of caveolae-resident signaling components, in particular G protein-coupled receptors (GPCR) and their stimulation of cAMP production, has not been defined [22].
  • Recent evidence suggest that many G protein-coupled receptors (GPCR) and signalling molecules localize in microdomains of the plasma membrane [23].
  • Use of such approaches has documented that several G protein-coupled receptors (GPCR), and their cognate heterotrimeric G proteins and effectors, localize to lipid rafts/caveolae in neonatal cardiac myocytes [24].
  • Our data suggest that OA1 represents the first example of an exclusively intracellular GPCR and support the hypothesis that GPCR-mediated signal transduction systems also operate at the internal membranes in mammalian cells [25].

Associations of GPR160 with chemical compounds

  • Considerable evidence suggests that GPCR signalling components are organized together in membrane microdomains, in particular lipid rafts, enriched in cholesterol and sphingolipids, and caveolae, a subset of lipid rafts that also possess the protein caveolin, whose scaffolding domain may serve as an anchor for signalling components [19].
  • In this review, we demonstrate the role of lipid rafts in GPCR-G-protein signaling and also present our recent results showing that the wasp toxin mastoparan modifies G(q/11)-mediated phospholipase C activation through the interaction with gangliosides in lipid rafts [26].
  • We provide here structural evidence that the protein product of the ocular albinism type 1 gene (OA1), a pigment cell-specific integral membrane glycoprotein, represents a novel member of the GPCR superfamily and demonstrate that it binds heterotrimeric G proteins [25].
  • MAP kinase activation may result from stimulation of either tyrosine-kinase (RTK) receptors, which possess intrinsic tyrosine kinase activity, or G-protein-coupled receptors (GPCR) [27].
  • Over the past three years, three types of scaffolds for GPCR-directed complex assembly have been identified: transactivated receptor tyrosine kinases (RTKs), integrin-based focal adhesions, and GPCRs themselves [28].

Other interactions of GPR160


Analytical, diagnostic and therapeutic context of GPR160

  • Caveolae were originally identified based on their morphological appearance but their role in compartmentation of GPCR signalling has been primarily studied by biochemical techniques, such as subcellular fractionation and immunoprecipitation [19].
  • Graded reductions in GPCR expression can be achieved through antisense strategies or total gene ablation or replacement can be achieved through gene targeting strategies, and exogenous expression of wild-type or mutant GPCR isoforms can be accomplished with transgenic technologies [31].
  • Here, we report the molecular cloning of a novel GPCR for LTB(4), designated BLT2, which binds LTB(4) with a Kd value of 23 nM compared with 1.1 nM for BLT1, but still efficiently transduces intracellular signaling [32].
  • Techniques: GPCR assembly, pharmacology and screening by flow cytometry [33].
  • Using a degenerate PCR approach, we have identified 15 G protein-coupled receptors (GPCR) from human and rodent tissues [34].


  1. TACE cleavage of proamphiregulin regulates GPCR-induced proliferation and motility of cancer cells. Gschwind, A., Hart, S., Fischer, O.M., Ullrich, A. EMBO J. (2003) [Pubmed]
  2. A central role of EGF receptor transactivation in angiotensin II -induced cardiac hypertrophy. Shah, B.H., Catt, K.J. Trends Pharmacol. Sci. (2003) [Pubmed]
  3. p90 ribosomal S6 kinase 2 exerts a tonic brake on G protein-coupled receptor signaling. Sheffler, D.J., Kroeze, W.K., Garcia, B.G., Deutch, A.Y., Hufeisen, S.J., Leahy, P., Brüning, J.C., Roth, B.L. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  4. E-selectin permits communication between PAF receptors and TRPC channels in human neutrophils. McMeekin, S.R., Dransfield, I., Rossi, A.G., Haslett, C., Walker, T.R. Blood (2006) [Pubmed]
  5. The peripheral cannabinoid receptor Cb2, frequently expressed on AML blasts, either induces a neutrophilic differentiation block or confers abnormal migration properties in a ligand-dependent manner. Alberich Jordà, M., Rayman, N., Tas, M., Verbakel, S.E., Battista, N., van Lom, K., Löwenberg, B., Maccarrone, M., Delwel, R. Blood (2004) [Pubmed]
  6. Regulators of G protein signaling (RGS proteins): novel central nervous system drug targets. Neubig, R.R. J. Pept. Res. (2002) [Pubmed]
  7. Emerging signalling and protein interactions mediated via metabotropic glutamate receptors. Moldrich, R.X., Beart, P.M. Current drug targets. CNS and neurological disorders. (2003) [Pubmed]
  8. Rhodopsin: structural basis of molecular physiology. Menon, S.T., Han, M., Sakmar, T.P. Physiol. Rev. (2001) [Pubmed]
  9. Cargo regulates clathrin-coated pit dynamics. Puthenveedu, M.A., von Zastrow, M. Cell (2006) [Pubmed]
  10. A nuclear function of beta-arrestin1 in GPCR signaling: regulation of histone acetylation and gene transcription. Kang, J., Shi, Y., Xiang, B., Qu, B., Su, W., Zhu, M., Zhang, M., Bao, G., Wang, F., Zhang, X., Yang, R., Fan, F., Chen, X., Pei, G., Ma, L. Cell (2005) [Pubmed]
  11. Beta-arrestin goes nuclear. Beaulieu, J.M., Caron, M.G. Cell (2005) [Pubmed]
  12. Lysophosphatidic acid-induced squamous cell carcinoma cell proliferation and motility involves epidermal growth factor receptor signal transactivation. Gschwind, A., Prenzel, N., Ullrich, A. Cancer Res. (2002) [Pubmed]
  13. Pleiotropic coupling of G protein-coupled receptors to the mitogen-activated protein kinase cascade. Role of focal adhesions and receptor tyrosine kinases. Della Rocca, G.J., Maudsley, S., Daaka, Y., Lefkowitz, R.J., Luttrell, L.M. J. Biol. Chem. (1999) [Pubmed]
  14. The synthetic peptide derived from the NH2-terminal extracellular region of an orphan G protein-coupled receptor, GPR1, preferentially inhibits infection of X4 HIV-1. Jinno-Oue, A., Shimizu, N., Soda, Y., Tanaka, A., Ohtsuki, T., Kurosaki, D., Suzuki, Y., Hoshino, H. J. Biol. Chem. (2005) [Pubmed]
  15. Differential regulation of estrogen receptor alpha, glucocorticoid receptor and retinoic acid receptor alpha transcriptional activity by melatonin is mediated via different G proteins. Kiefer, T.L., Lai, L., Yuan, L., Dong, C., Burow, M.E., Hill, S.M. J. Pineal Res. (2005) [Pubmed]
  16. Involvement of metabotropic glutamate receptor 1, a G protein coupled receptor, in melanoma development. Marín, Y.E., Chen, S. J. Mol. Med. (2004) [Pubmed]
  17. Mechanisms of regulation of the expression and function of G protein-coupled receptor kinases. Penela, P., Ribas, C., Mayor, F. Cell. Signal. (2003) [Pubmed]
  18. Negative regulation of protease-activated receptor 1-induced Src kinase activity by the association of phosphocaveolin-1 with Csk. Lu, T.L., Kuo, F.T., Lu, T.J., Hsu, C.Y., Fu, H.W. Cell. Signal. (2006) [Pubmed]
  19. Compartmentation of G-protein-coupled receptors and their signalling components in lipid rafts and caveolae. Insel, P.A., Head, B.P., Patel, H.H., Roth, D.M., Bundey, R.A., Swaney, J.S. Biochem. Soc. Trans. (2005) [Pubmed]
  20. The G protein-coupled receptor kinase (GRK) interactome: Role of GRKs in GPCR regulation and signaling. Ribas, C., Penela, P., Murga, C., Salcedo, A., García-Hoz, C., Jurado-Pueyo, M., Aymerich, I., Mayor, F. Biochim. Biophys. Acta (2007) [Pubmed]
  21. EGF receptor transactivation by G-protein-coupled receptors requires metalloproteinase cleavage of proHB-EGF. Prenzel, N., Zwick, E., Daub, H., Leserer, M., Abraham, R., Wallasch, C., Ullrich, A. Nature (1999) [Pubmed]
  22. Microtubules and actin microfilaments regulate lipid raft/caveolae localization of adenylyl cyclase signaling components. Head, B.P., Patel, H.H., Roth, D.M., Murray, F., Swaney, J.S., Niesman, I.R., Farquhar, M.G., Insel, P.A. J. Biol. Chem. (2006) [Pubmed]
  23. Metabotropic glutamate type 1alpha receptor localizes in low-density caveolin-rich plasma membrane fractions. Burgueño, J., Enrich, C., Canela, E.I., Mallol, J., Lluis, C., Franco, R., Ciruela, F. J. Neurochem. (2003) [Pubmed]
  24. Caveolae and lipid rafts: G protein-coupled receptor signaling microdomains in cardiac myocytes. Insel, P.A., Head, B.P., Ostrom, R.S., Patel, H.H., Swaney, J.S., Tang, C.M., Roth, D.M. Ann. N. Y. Acad. Sci. (2005) [Pubmed]
  25. Ocular albinism: evidence for a defect in an intracellular signal transduction system. Schiaffino, M.V., d'Addio, M., Alloni, A., Baschirotto, C., Valetti, C., Cortese, K., Puri, C., Bassi, M.T., Colla, C., De Luca, M., Tacchetti, C., Ballabio, A. Nat. Genet. (1999) [Pubmed]
  26. The Role of Lipid Rafts in Trimeric G Protein-mediated Signal Transduction. Ohkubo, S., Nakahata, N. Yakugaku Zasshi (2007) [Pubmed]
  27. Receptor-tyrosine-kinase- and G beta gamma-mediated MAP kinase activation by a common signalling pathway. van Biesen, T., Hawes, B.E., Luttrell, D.K., Krueger, K.M., Touhara, K., Porfiri, E., Sakaue, M., Luttrell, L.M., Lefkowitz, R.J. Nature (1995) [Pubmed]
  28. Regulation of tyrosine kinase cascades by G-protein-coupled receptors. Luttrell, L.M., Daaka, Y., Lefkowitz, R.J. Curr. Opin. Cell Biol. (1999) [Pubmed]
  29. A constitutively internalizing and recycling mutant of the mu-opioid receptor. Segredo, V., Burford, N.T., Lameh, J., Sadée, W. J. Neurochem. (1997) [Pubmed]
  30. Integrins regulate opioid receptor signaling in trigeminal ganglion neurons. Berg, K.A., Zardeneta, G., Hargreaves, K.M., Clarke, W.P., Milam, S.B. Neuroscience (2007) [Pubmed]
  31. G protein-coupled receptors: functional and mechanistic insights through altered gene expression. Rohrer, D.K., Kobilka, B.K. Physiol. Rev. (1998) [Pubmed]
  32. A second leukotriene B(4) receptor, BLT2. A new therapeutic target in inflammation and immunological disorders. Yokomizo, T., Kato, K., Terawaki, K., Izumi, T., Shimizu, T. J. Exp. Med. (2000) [Pubmed]
  33. Techniques: GPCR assembly, pharmacology and screening by flow cytometry. Waller, A., Simons, P.C., Biggs, S.M., Edwards, B.S., Prossnitz, E.R., Sklar, L.A. Trends Pharmacol. Sci. (2004) [Pubmed]
  34. Trace amines: identification of a family of mammalian G protein-coupled receptors. Borowsky, B., Adham, N., Jones, K.A., Raddatz, R., Artymyshyn, R., Ogozalek, K.L., Durkin, M.M., Lakhlani, P.P., Bonini, J.A., Pathirana, S., Boyle, N., Pu, X., Kouranova, E., Lichtblau, H., Ochoa, F.Y., Branchek, T.A., Gerald, C. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
WikiGenes - Universities