메뉴 건너뛰기




Volumn 388, Issue 1, 2005, Pages 317-324

Role of the ERC motif in the proximal part of the second intracellular loop and the C-terminal domain of the human prostaglandin F2α receptor (hFP-R) in G-protein coupling control

Author keywords

Constitutively active mutant; ERC motif; G protein coupled receptor; Prostaglandin F2 receptor; Site directed mutagenesis; Structure function relationship

Indexed keywords

GLAUCOMA; INTRACELLULAR SIGNAL PATHWAYS; LIGAND BINDING; MUTANTS;

EID: 19544367952     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20041321     Document Type: Article
Times cited : (8)

References (41)
  • 2
    • 0032823306 scopus 로고    scopus 로고
    • Prostanoid receptors: Structures, properties, and functions
    • Narumiya, S., Sugimoto, Y. and Ushikubi, F. (1999) Prostanoid receptors: structures, properties, and functions Physiol. Rev. 79, 1193-1226
    • (1999) Physiol. Rev. , vol.79 , pp. 1193-1226
    • Narumiya, S.1    Sugimoto, Y.2    Ushikubi, F.3
  • 4
    • 0033544916 scopus 로고    scopus 로고
    • Activation of FP prostancid receptor isoforms leads to Rho-mediated changes in cell morphology and in the cell cytoskeleton
    • Pierce, K. L., Fujino, H., Srinivasan, D. and Repan, J. W. (1999) Activation of FP prostancid receptor isoforms leads to Rho-mediated changes in cell morphology and in the cell cytoskeleton. J. Biol. Chem. 274, 35944-35949
    • (1999) J. Biol. Chem. , vol.274 , pp. 35944-35949
    • Pierce, K.L.1    Fujino, H.2    Srinivasan, D.3    Repan, J.W.4
  • 6
    • 1842848649 scopus 로고    scopus 로고
    • Cloning and characterization of the novel isoforms for PGF2 alpha receptor in the bovine corpus luteum
    • Sakamoto, K., Ishii, Y., Onodera, T. and Sugano, T. (2002) Cloning and characterization of the novel isoforms for PGF2 alpha receptor in the bovine corpus luteum. DNA Seq. 13, 307-311
    • (2002) DNA Seq. , vol.13 , pp. 307-311
    • Sakamoto, K.1    Ishii, Y.2    Onodera, T.3    Sugano, T.4
  • 7
    • 0031675379 scopus 로고    scopus 로고
    • Female reproduction in mice lacking the prostaglandin F receptor. Roles of prostaglandin and oxytocin receptors in parturition
    • Sugimoto, Y., Segi, E., Tsuboi, K., Ichikawa, A. and Narumiya, S. (1998) Female reproduction in mice lacking the prostaglandin F receptor. Roles of prostaglandin and oxytocin receptors in parturition. Adv. Exp. Med. Biol. 449, 317-321
    • (1998) Adv. Exp. Med. Biol. , vol.449 , pp. 317-321
    • Sugimoto, Y.1    Segi, E.2    Tsuboi, K.3    Ichikawa, A.4    Narumiya, S.5
  • 11
    • 0038302713 scopus 로고    scopus 로고
    • Ldentification by site-directed mutagenesis of amino acids contributing to ligand-binding specificity or signal transduction properties of the human FP prostanoid receptor
    • Neuschäfer-Rube. F., Engemaier, E., Koch, S., Böer, U. and Püschel, G. P. (2003) ldentification by site-directed mutagenesis of amino acids contributing to ligand-binding specificity or signal transduction properties of the human FP prostanoid receptor. Biochem. J. 371, 443-449
    • (2003) Biochem. J. , vol.371 , pp. 443-449
    • Neuschäfer-Rube, F.1    Engemaier, E.2    Koch, S.3    Böer, U.4    Püschel, G.P.5
  • 12
    • 0031026413 scopus 로고    scopus 로고
    • Substitution of charged amino acid residues in transmembrane regions 6 and 7 affect ligand binding and signal transduction of the prostaglandin EP3 receptor
    • Audoly, and Breyer, R. M. (1997) Substitution of charged amino acid residues in transmembrane regions 6 and 7 affect ligand binding and signal transduction of the prostaglandin EP3 receptor. Mol. Pharmacol. 51, 61-68
    • (1997) Mol. Pharmacol. , vol.51 , pp. 61-68
    • Audoly1    Breyer, R.M.2
  • 14
    • 0033554660 scopus 로고    scopus 로고
    • Phenylalanlne 138 in the second intracellular loop of human thromboxane receptor is critical for receptor-G-protein coupling
    • Zhou, H., Yan, F., Yamamoto, S. and Tai, H. H. (1999) Phenylalanlne 138 in the second intracellular loop of human thromboxane receptor is critical for receptor-G-protein coupling. Bioctem. Biophys. Res. Commun. 264, 171-175
    • (1999) Bioctem. Biophys. Res. Commun. , vol.264 , pp. 171-175
    • Zhou, H.1    Yan, F.2    Yamamoto, S.3    Tai, H.H.4
  • 15
    • 0030999720 scopus 로고    scopus 로고
    • Constitutive activity of human prostaglandin e receptor EP3 isoforms
    • Jin, J., Mao, G. F. and Ashby, B. (1997) Constitutive activity of human prostaglandin E receptor EP3 isoforms. Br. J. Pharmacol. 121, 317-323
    • (1997) Br. J. Pharmacol. , vol.121 , pp. 317-323
    • Jin, J.1    Mao, G.F.2    Ashby, B.3
  • 16
    • 0030049389 scopus 로고    scopus 로고
    • Two isoforms of the proslaglandin e receptor EP3 subtype different in agonist-independent constitutive activity
    • Hasegawa, H., Negishi, M. and Ichikawa, A. (1996) Two isoforms of the proslaglandin E receptor EP3 subtype different in agonist-independent constitutive activity. J. Biol. Chem. 271, 1857-1860
    • (1996) J. Biol. Chem. , vol.271 , pp. 1857-1860
    • Hasegawa, H.1    Negishi, M.2    Ichikawa, A.3
  • 17
    • 0031590012 scopus 로고    scopus 로고
    • Two isoforms of prostagiandir EP3 receptor exhibiting constitutive activity and agonist-dependent activity in Rho-mediated stress liber formation
    • Hasegawa, H., Negishi, M., Katoh, H. and Ichikawa, A. (1997) Two isoforms of prostagiandir EP3 receptor exhibiting constitutive activity and agonist-dependent activity in Rho-mediated stress liber formation. Biochem. Biophys. Res. Commun 234, 631-636
    • (1997) Biochem. Biophys. Res. Commun , vol.234 , pp. 631-636
    • Hasegawa, H.1    Negishi, M.2    Katoh, H.3    Ichikawa, A.4
  • 18
    • 0031392753 scopus 로고    scopus 로고
    • Three isoforms of the prostaglandin e receptor EP3 subtype different in agonist-independent constitutive Gi activity and agonist-dependent Gs activity
    • Ichikawa, A., Negishi, M. and Hasegawa, H. (1997) Three isoforms of the prostaglandin E receptor EP3 subtype different in agonist-independent constitutive Gi activity and agonist-dependent Gs activity. Adv. Exp. Med. Biol. 433, 239-242
    • (1997) Adv. Exp. Med. Biol. , vol.433 , pp. 239-242
    • Ichikawa, A.1    Negishi, M.2    Hasegawa, H.3
  • 19
    • 0028169594 scopus 로고
    • The C-terminus of the prostaglandin-E-receplor EP3 subtype is essential for activation of GTP-binding protein
    • Irie, A., Sugimoto, Y., Namba, T., Asano, T., Ichikawa, A. and Negishi, M. (1994) The C-terminus of the prostaglandin-E-receplor EP3 subtype is essential for activation of GTP-binding protein. Eur. J. Biochen. 224, 161-166
    • (1994) Eur. J. Biochen. , vol.224 , pp. 161-166
    • Irie, A.1    Sugimoto, Y.2    Namba, T.3    Asano, T.4    Ichikawa, A.5    Negishi, M.6
  • 20
    • 0032589203 scopus 로고    scopus 로고
    • Preservation of Gi coupling of a chimeric EP3/l-type prostaglandin (IP) receptor
    • Meyer-Kirchrath, J., Hasse. A. ard Schrör K. (1999) Preservation of Gi coupling of a chimeric EP3/l-type prostaglandin (IP) receptor. Biochem. Pharmacol. 58, 471-476
    • (1999) Biochem. Pharmacol. , vol.58 , pp. 471-476
    • Meyer-Kirchrath, J.1    Hasse, A.2    Schrör, K.3
  • 21
    • 0343742628 scopus 로고    scopus 로고
    • The C-terminal domain of the Gs-coupled EP4 receptor confers agonist-dependent coupling control to Gi but no coupling to Gs in a receptor hydrid with the Gi-coupled EP3 receptor
    • Neuschäfer-Rube, F., Hänecke, K., Biaschke, V., Jungermann, K. and Püschel, G. P. (1997) The C-terminal domain of the Gs-coupled EP4 receptor confers agonist-dependent coupling control to Gi but no coupling to Gs in a receptor hydrid with the Gi-coupled EP3 receptor. FEBS Lett. 401, 185-190
    • (1997) FEBS Lett. , vol.401 , pp. 185-190
    • Neuschäfer-Rube, F.1    Hänecke, K.2    Biaschke, V.3    Jungermann, K.4    Püschel, G.P.5
  • 22
    • 0036078874 scopus 로고    scopus 로고
    • Mutagenesis and peptide analysis of the DRY motif in the alpha2A adrenergic receptor: Evidence for alternate mechanisms in G-protein-coupled receptors
    • Chung, D. A., Wade, S. M., Fowler, C. B., Woods, D. D., Abada, P. B., Mosberg, H. I. and Neubig, R. R. (2002) Mutagenesis and peptide analysis of the DRY motif in the alpha2A adrenergic receptor: evidence for alternate mechanisms in G-protein-coupled receptors. Biochem. Biophys. Res. Commun. 293, 1233-1241
    • (2002) Biochem. Biophys. Res. Commun. , vol.293 , pp. 1233-1241
    • Chung, D.A.1    Wade, S.M.2    Fowler, C.B.3    Woods, D.D.4    Abada, P.B.5    Mosberg, H.I.6    Neubig, R.R.7
  • 23
    • 0033974265 scopus 로고    scopus 로고
    • Mutational analysis of the highly conserved arginine within the Glu/Asp-Arg-Tyr motif of the alpha(1b)-adrenergic receptor: Effects on receptor isomerization and activation
    • Scheer, A., Costa, T., Fanelli, F., De Benedetti, P. G., Mhaouty-Kodja, S., Abuin, L., Nenniger-Tosato, M. and Cotecchia, S. (2000) Mutational analysis of the highly conserved arginine within the Glu/Asp-Arg-Tyr motif of the alpha(1b)-adrenergic receptor: effects on receptor isomerization and activation. Mol. Pharmacol. 57, 219-231
    • (2000) Mol. Pharmacol. , vol.57 , pp. 219-231
    • Scheer, A.1    Costa, T.2    Fanelli, F.3    De Benedetti, P.G.4    Mhaouty-Kodja, S.5    Abuin, L.6    Nenniger-Tosato, M.7    Cotecchia, S.8
  • 24
    • 0030614337 scopus 로고    scopus 로고
    • The activation process of the alpha 1B-adrenergic receptor: Potential role of protonation and hydrophobicity of a highly conserved aspartate
    • Scheer, A., Fanelli, F., Costa, T., De Benedetti, P. G. and Cotecchia, S. (1997) The activation process of the alpha 1B-adrenergic receptor: potential role of protonation and hydrophobicity of a highly conserved aspartate. Proc. Natl. Acad. Sci. U.S.A. 94, 808-813
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 808-813
    • Scheer, A.1    Fanelli, F.2    Costa, T.3    De Benedetti, P.G.4    Cotecchia, S.5
  • 25
    • 0344348845 scopus 로고    scopus 로고
    • Agonist-induced phosphorylation by G-proleh-coupled receptor kinases of the EP4 receptor carboxyl-terminal domain in an EP3/EP4 prostaglandin E(2) receptor hybrid
    • Neuschäfer-Rube, F., Oppermann, M., Möller, U., Böer, U. and Püschel, G. P. (1999) Agonist-induced phosphorylation by G-proleh-coupled receptor kinases of the EP4 receptor carboxyl-terminal domain in an EP3/EP4 prostaglandin E(2) receptor hybrid. Mol. Pharmacol. 56, 419-428
    • (1999) Mol. Pharmacol. , vol.56 , pp. 419-428
    • Neuschäfer-Rube, F.1    Oppermann, M.2    Möller, U.3    Böer, U.4    Püschel, G.P.5
  • 26
    • 0028071341 scopus 로고
    • Molecular cloning and expression of a prostaglandin E2 receptor of the EP3 beta subtype from rat hepatocytes
    • Neuschäfer-Rube, F., DeVries, C., Hänecke, K., Jungermann, K. and Püschel, G. P. (1994) Molecular cloning and expression of a prostaglandin E2 receptor of the EP3 beta subtype from rat hepatocytes. FEBS Lett. 351, 119-122
    • (1994) FEBS Lett. , vol.351 , pp. 119-122
    • Neuschäfer-Rube, F.1    DeVries, C.2    Hänecke, K.3    Jungermann, K.4    Püschel, G.P.5
  • 27
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 28
    • 0019061918 scopus 로고
    • Ligand: A versatile computelzed approach for characterization of ligand-binding systems
    • Munson, P. J. and Rodbard, D. (1980) Ligand: a versatile computelzed approach for characterization of ligand-binding systems. Anal. Biochem. 107, 220-239
    • (1980) Anal. Biochem. , vol.107 , pp. 220-239
    • Munson, P.J.1    Rodbard, D.2
  • 29
    • 0035918222 scopus 로고    scopus 로고
    • FP prostanoid receptor activation of a T-cell factor/beta-catenin signaling pathway
    • Fujino, H. and Regan, J. W. (2001) FP prostanoid receptor activation of a T-cell factor/beta-catenin signaling pathway. J. Biol. Chem. 276, 12489-12492
    • (2001) J. Biol. Chem. , vol.276 , pp. 12489-12492
    • Fujino, H.1    Regan, J.W.2
  • 30
    • 0035895142 scopus 로고    scopus 로고
    • Interaction of Galpha 12 and Galpha 13 with the cytoplasmic domain of cadherin provides a mechanism for beta-catenin release
    • Meigs, T. E. Fields, T. A., McKee, D. D. and Casey, P. J. (2001) Interaction of Galpha 12 and Galpha 13 with the cytoplasmic domain of cadherin provides a mechanism for beta-catenin release. Proc. Natl. Acad. Sci. U.S.A. 98, 519-524
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 519-524
    • Meigs, T.E.1    Fields, T.A.2    McKee, D.D.3    Casey, P.J.4
  • 31
    • 0037073807 scopus 로고    scopus 로고
    • Cellular conditioning and activation of beta-catenin signaling by the FPB prostanoid receptor
    • Fujino, H., Srinivasan, D. and Regan, J. W. (2002) Cellular conditioning and activation of beta-catenin signaling by the FPB prostanoid receptor. J. Biol. Chem. 277, 48786-48795
    • (2002) J. Biol. Chem. , vol.277 , pp. 48786-48795
    • Fujino, H.1    Srinivasan, D.2    Regan, J.W.3
  • 32
    • 0027443488 scopus 로고
    • Inhibition by the protein kinase C activator 4 beta-phorbol 12-myristate 13-acetate of the prostaglandin F2 alpha-mediated and noradrenaline-nediated but not glucagon-mediated activation of glycogenolysis in rat liver
    • Püschel, G. P., Miura, H., Neuschäfer-Rube, F. and Jungermann, K. (1993) Inhibition by the protein kinase C activator 4 beta-phorbol 12-myristate 13-acetate of the prostaglandin F2 alpha-mediated and noradrenaline-nediated but not glucagon-mediated activation of glycogenolysis in rat liver. Eur. J. Biochem. 217, 305-311
    • (1993) Eur. J. Biochem. , vol.217 , pp. 305-311
    • Püschel, G.P.1    Miura, H.2    Neuschäfer-Rube, F.3    Jungermann, K.4
  • 33
    • 0033975106 scopus 로고    scopus 로고
    • Differential regulation of prostaglandin F(2alpha) receptor isoforms by protein kinase
    • Fujino, H., Srinivasan, D., Pierce, K. L. and Regan, J. W. (2000) Differential regulation of prostaglandin F(2alpha) receptor isoforms by protein kinase C. Mot Pharmacol. 57, 353-358
    • (2000) C. Mot Pharmacol. , vol.57 , pp. 353-358
    • Fujino, H.1    Srinivasan, D.2    Pierce, K.L.3    Regan, J.W.4
  • 34
    • 0036082357 scopus 로고    scopus 로고
    • Differential internalization of the prostaglandin f(2alpha) receptor isoforms: Role of protein kinase C and clathrin
    • Srinivasan, D., Fujino, H. and Regan, J. W. (2002) Differential internalization of the prostaglandin f(2alpha) receptor isoforms: role of protein kinase C and clathrin. J. Pharmaccl. Exp. Ther. 302, 219-224
    • (2002) J. Pharmaccl. Exp. Ther. , vol.302 , pp. 219-224
    • Srinivasan, D.1    Fujino, H.2    Regan, J.W.3
  • 35
    • 0032504208 scopus 로고    scopus 로고
    • Endocytosis of the glucose transporter GLUT4 is mediated by the GTPase dynamin
    • Al-Hasani, H., Hinck, C. S. and Cushman, S. W. (1998) Endocytosis of the glucose transporter GLUT4 is mediated by the GTPase dynamin. J. Biol. Chem. 273, 17504-17510
    • (1998) J. Biol. Chem. , vol.273 , pp. 17504-17510
    • Al-Hasani, H.1    Hinck, C.S.2    Cushman, S.W.3
  • 37
    • 0034691035 scopus 로고    scopus 로고
    • Systematic identification of mutations that constitutively activate the angiotensin II type 1A receptor by screening a randomly mutated cDNA library with an original pharmacological bioassay
    • Parnot, C., Bardin, S., Miserey-Lenkei, S., Guedin, D., Corvol, P. and Clauser, E. (2000) Systematic identification of mutations that constitutively activate the angiotensin II type 1A receptor by screening a randomly mutated cDNA library with an original pharmacological bioassay. Proc. Natl. Acad. Sci. U.S.A. 97, 7615-7620
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 7615-7620
    • Parnot, C.1    Bardin, S.2    Miserey-Lenkei, S.3    Guedin, D.4    Corvol, P.5    Clauser, E.6
  • 38
    • 0031559932 scopus 로고    scopus 로고
    • Functional role of carboxyl-terminal tail of prostaglandin EPS receptor in Gi ccupling
    • Hizaki, H., Hasegawa, H., Katoh, H., Negishi, M. and Ichikawa, A. (1997) Functional role of carboxyl-terminal tail of prostaglandin EPS receptor in Gi ccupling. FEBS Lett 414, 323-326
    • (1997) FEBS Lett , vol.414 , pp. 323-326
    • Hizaki, H.1    Hasegawa, H.2    Katoh, H.3    Negishi, M.4    Ichikawa, A.5
  • 39
    • 0029963929 scopus 로고    scopus 로고
    • Changes in the carboxyl-terminal domain of metabotropic glutamate receptor 1 by alternative saucing generate receptors with differing agonist-independent activity
    • Prezeau, L., Gomeza, J., Anern, S., Mary, S., Galvez, T., Bockaert, J. and Pin, J. P. (1996) Changes in the carboxyl-terminal domain of metabotropic glutamate receptor 1 by alternative saucing generate receptors with differing agonist-independent activity. Mot. Pharmacol. 49, 422-429
    • (1996) Mot. Pharmacol. , vol.49 , pp. 422-429
    • Prezeau, L.1    Gomeza, J.2    Anern, S.3    Mary, S.4    Galvez, T.5    Bockaert, J.6    Pin, J.P.7
  • 40
    • 0027205165 scopus 로고
    • Two isoforms of prostaglandin e receptor EP3 subtype. Different COOH-terminal domains determine sensitivity to agonist-induced desensitization
    • Negishi, M., Sugimolo, Y., Irie, A., Narumiya, S. and Ichikawa, A. (1993) Two isoforms of prostaglandin E receptor EP3 subtype. Different COOH-terminal domains determine sensitivity to agonist-induced desensitization. J. Biol. Chem. 268, 9517-9521
    • (1993) J. Biol. Chem. , vol.268 , pp. 9517-9521
    • Negishi, M.1    Sugimolo, Y.2    Irie, A.3    Narumiya, S.4    Ichikawa, A.5
  • 41
    • 2542565698 scopus 로고    scopus 로고
    • Identification of a Ser/Thr cluster in the C-terminal domain of the human prostaglandin receptor EP4 that is essential for agonisl-inducec beta-arrestin1 recruitment but differs from the apparent principal phosphorylatior site
    • Neuschäfer-Rube, F., Hermosilla, R., Rehwald, M., Rönnstrand, L., Schülein, R., Wernsted:, C. and Püschel, G. P. (2004) Identification of a Ser/Thr cluster in the C-terminal domain of the human prostaglandin receptor EP4 that is essential for agonisl-inducec beta-arrestin1 recruitment but differs from the apparent principal phosphorylatior site. Biochem. J. 379, 573-585
    • (2004) Biochem. J. , vol.379 , pp. 573-585
    • Neuschäfer-Rube, F.1    Hermosilla, R.2    Rehwald, M.3    Rönnstrand, L.4    Schülein, R.5    Wernsted, C.6    Püschel, G.P.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.