Tissue distribution and functional analyses of the constitutively active orphan G protein coupled receptors, GPR26 and GPR78
GPR26 and GPR78 are orphan GPCRs (oGPCRs) that share 51% amino acid sequence identity and are widely expressed in selected tissues of the human brain as well as the developing and adult mouse brain. Investigation of the functional activity of GPR26 and GPR78 via expression in HEK293 cells showed tha...
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| Published in | Biochimica et biophysica acta Vol. 1770; no. 6; pp. 890 - 901 |
|---|---|
| Main Authors | , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Netherlands
Elsevier B.V
01.06.2007
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| Abstract | GPR26 and GPR78 are orphan GPCRs (oGPCRs) that share 51% amino acid sequence identity and are widely expressed in selected tissues of the human brain as well as the developing and adult mouse brain. Investigation of the functional activity of GPR26 and GPR78 via expression in HEK293 cells showed that both proteins are constitutively active and coupled to elevated cAMP production. Accordingly, in yeast, GPR26 demonstrated apparent agonist-independent coupling to a chimeric Gpa1 protein in which the 5 C-terminal amino acids were from Gαs. A comparison of the proteins revealed an atypical glutamine residue in GPR78 in place of the conserved arginine residue (R3.50) in the so-called DRY box. Site-directed mutants R3.50 in GPR26 were constructed and retained their constitutive activity suggesting that these 2 receptors activate G proteins in a manner that is distinct from other group 1 GPCRs. |
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| AbstractList | GPR26 and GPR78 are orphan GPCRs (oGPCRs) that share 51% amino acid sequence identity and are widely expressed in selected tissues of the human brain as well as the developing and adult mouse brain. Investigation of the functional activity of GPR26 and GPR78 via expression in HEK293 cells showed that both proteins are constitutively active and coupled to elevated cAMP production. Accordingly, in yeast, GPR26 demonstrated apparent agonist-independent coupling to a chimeric Gpa1 protein in which the 5 C-terminal amino acids were from Galphas. A comparison of the proteins revealed an atypical glutamine residue in GPR78 in place of the conserved arginine residue (R3.50) in the so-called DRY box. Site-directed mutants R3.50 in GPR26 were constructed and retained their constitutive activity suggesting that these 2 receptors activate G proteins in a manner that is distinct from other group 1 GPCRs. GPR26 and GPR78 are orphan GPCRs (oGPCRs) that share 51% amino acid sequence identity and are widely expressed in selected tissues of the human brain as well as the developing and adult mouse brain. Investigation of the functional activity of GPR26 and GPR78 via expression in HEK293 cells showed that both proteins are constitutively active and coupled to elevated cAMP production. Accordingly, in yeast, GPR26 demonstrated apparent agonist-independent coupling to a chimeric Gpa1 protein in which the 5 C-terminal amino acids were from Gαs. A comparison of the proteins revealed an atypical glutamine residue in GPR78 in place of the conserved arginine residue (R3.50) in the so-called DRY box. Site-directed mutants R3.50 in GPR26 were constructed and retained their constitutive activity suggesting that these 2 receptors activate G proteins in a manner that is distinct from other group 1 GPCRs. GPR26 and GPR78 are orphan GPCRs (oGPCRs) that share 51% amino acid sequence identity and are widely expressed in selected tissues of the human brain as well as the developing and adult mouse brain. Investigation of the functional activity of GPR26 and GPR78 via expression in HEK293 cells showed that both proteins are constitutively active and coupled to elevated cAMP production. Accordingly, in yeast, GPR26 demonstrated apparent agonist-independent coupling to a chimeric Gpa1 protein in which the 5 C-terminal amino acids were from Galphas. A comparison of the proteins revealed an atypical glutamine residue in GPR78 in place of the conserved arginine residue (R3.50) in the so-called DRY box. Site-directed mutants R3.50 in GPR26 were constructed and retained their constitutive activity suggesting that these 2 receptors activate G proteins in a manner that is distinct from other group 1 GPCRs.GPR26 and GPR78 are orphan GPCRs (oGPCRs) that share 51% amino acid sequence identity and are widely expressed in selected tissues of the human brain as well as the developing and adult mouse brain. Investigation of the functional activity of GPR26 and GPR78 via expression in HEK293 cells showed that both proteins are constitutively active and coupled to elevated cAMP production. Accordingly, in yeast, GPR26 demonstrated apparent agonist-independent coupling to a chimeric Gpa1 protein in which the 5 C-terminal amino acids were from Galphas. A comparison of the proteins revealed an atypical glutamine residue in GPR78 in place of the conserved arginine residue (R3.50) in the so-called DRY box. Site-directed mutants R3.50 in GPR26 were constructed and retained their constitutive activity suggesting that these 2 receptors activate G proteins in a manner that is distinct from other group 1 GPCRs. |
| Author | Nawoschik, Stanley P. Sreekumar, Kodangattil Pausch, Mark H. Zhang, Lynn Bates, Brian Johnson, Jeremy Jones, Philip G. Uveges, Albert J. He, Lan Tseng, Eugene Paulsen, Janet E. |
| Author_xml | – sequence: 1 givenname: Philip G. surname: Jones fullname: Jones, Philip G. organization: Neuroscience Discovery Research, Wyeth Research, CN8000, Princeton, NJ 08543, USA – sequence: 2 givenname: Stanley P. surname: Nawoschik fullname: Nawoschik, Stanley P. organization: Neuroscience Discovery Research, Wyeth Research, CN8000, Princeton, NJ 08543, USA – sequence: 3 givenname: Kodangattil surname: Sreekumar fullname: Sreekumar, Kodangattil organization: Biological Technologies, Wyeth Research, Cambridge, MA 02140, USA – sequence: 4 givenname: Albert J. surname: Uveges fullname: Uveges, Albert J. organization: Neuroscience Discovery Research, Wyeth Research, CN8000, Princeton, NJ 08543, USA – sequence: 5 givenname: Eugene surname: Tseng fullname: Tseng, Eugene organization: Neuroscience Discovery Research, Wyeth Research, CN8000, Princeton, NJ 08543, USA – sequence: 6 givenname: Lynn surname: Zhang fullname: Zhang, Lynn organization: Biological Technologies, Wyeth Research, Cambridge, MA 02140, USA – sequence: 7 givenname: Jeremy surname: Johnson fullname: Johnson, Jeremy organization: Biological Technologies, Wyeth Research, Cambridge, MA 02140, USA – sequence: 8 givenname: Lan surname: He fullname: He, Lan organization: Neuroscience Discovery Research, Wyeth Research, CN8000, Princeton, NJ 08543, USA – sequence: 9 givenname: Janet E. surname: Paulsen fullname: Paulsen, Janet E. organization: Biological Technologies, Wyeth Research, Cambridge, MA 02140, USA – sequence: 10 givenname: Brian surname: Bates fullname: Bates, Brian organization: Biological Technologies, Wyeth Research, Cambridge, MA 02140, USA – sequence: 11 givenname: Mark H. surname: Pausch fullname: Pausch, Mark H. email: pauschm@wyeth.com organization: Neuroscience Discovery Research, Wyeth Research, CN8000, Princeton, NJ 08543, USA |
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| SubjectTerms | Animals Base Sequence Brain - cytology Brain - metabolism Cell Line Constitutive activity Cyclic AMP - biosynthesis GTP-Binding Protein alpha Subunits - biosynthesis GTP-Binding Protein alpha Subunits - genetics GTP-Binding Protein alpha Subunits, Gq-G11 Humans In situ hybridization Male Mice Molecular Sequence Data Mutagenesis, Site-Directed Mutation, Missense Orphan receptor Receptors, G-Protein-Coupled - biosynthesis Receptors, G-Protein-Coupled - genetics Recombinant Fusion Proteins - biosynthesis Recombinant Fusion Proteins - genetics Saccharomyces cerevisiae Proteins - biosynthesis Saccharomyces cerevisiae Proteins - genetics Sequence Homology, Amino Acid Site-directed mutagenesis |
| Title | Tissue distribution and functional analyses of the constitutively active orphan G protein coupled receptors, GPR26 and GPR78 |
| URI | https://dx.doi.org/10.1016/j.bbagen.2007.01.013 https://www.ncbi.nlm.nih.gov/pubmed/17363172 https://www.proquest.com/docview/70430401 |
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