메뉴 건너뛰기




Volumn 57, Issue 2, 2000, Pages 219-231

Mutational analysis of the highly conserved arginine within the Glu/Asp- Arg-Tyr motif of the α(1b)-adrenergic receptor: Effects on receptor isomerization and activation

Author keywords

[No Author keywords available]

Indexed keywords

ADRENALIN; ALPHA 1B ADRENERGIC RECEPTOR; CIRAZOLINE; COMPLEMENTARY DNA; DOPAMINE; METHOXAMINE; NORADRENALIN; OXYMETAZOLINE; PHENYLEPHRINE;

EID: 0033974265     PISSN: 0026895X     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (110)

References (37)
  • 2
    • 0031475025 scopus 로고    scopus 로고
    • Mutations of the conserved DRS motif in the second intracellular loop of the gonadotropin-releasing hormone receptor affect expression, activation and internalization
    • Arora KK, Cheng Z and Catt KJ (1997) Mutations of the conserved DRS motif in the second intracellular loop of the gonadotropin-releasing hormone receptor affect expression, activation and internalization. Mol Endocrinol 11:1203-1212.
    • (1997) Mol Endocrinol , vol.11 , pp. 1203-1212
    • Arora, K.K.1    Cheng, Z.2    Catt, K.J.3
  • 3
    • 0031565726 scopus 로고    scopus 로고
    • An alpha-carbon template for the transmembrane helices in the rhodopsin family of G protein-coupled receptors
    • Baldwin JM, Schertler GF and Unger VM (1997) An alpha-carbon template for the transmembrane helices in the rhodopsin family of G protein-coupled receptors. J Mol Biol 272:144-164.
    • (1997) J Mol Biol , vol.272 , pp. 144-164
    • Baldwin, J.M.1    Schertler, G.F.2    Unger, V.M.3
  • 5
    • 0027298812 scopus 로고
    • Constitutive activation of opsin: Influence of charge at position 134 and size at position 296
    • Cohen GB, Yang T, Robinson PR and Oprian DD (1993) Constitutive activation of opsin: Influence of charge at position 134 and size at position 296. Biochemistry 32: 6111-6115.
    • (1993) Biochemistry , vol.32 , pp. 6111-6115
    • Cohen, G.B.1    Yang, T.2    Robinson, P.R.3    Oprian, D.D.4
  • 6
    • 0026575003 scopus 로고
    • Discrete amino acid sequences of the α1-adrenergic receptor determine the selectivity of coupling to phosphatidylinositol hydrolysis
    • Cotecchia S, Ostrowski J, Kjelsberg MA, Caron MG and Lefkowitz RJ (1992) Discrete amino acid sequences of the α1-adrenergic receptor determine the selectivity of coupling to phosphatidylinositol hydrolysis. J Biol Chem 267:1633-1639.
    • (1992) J Biol Chem , vol.267 , pp. 1633-1639
    • Cotecchia, S.1    Ostrowski, J.2    Kjelsberg, M.A.3    Caron, M.G.4    Lefkowitz, R.J.5
  • 7
    • 0027374544 scopus 로고
    • Protonation states of membrane-embedded carboxylic acid groups in rhodopsin and metarhodospin II: A Fourier-transform infrared spectroscopy study of site-directed mutants
    • Fahmy K, Jager F, Beck M, Zvyaga TA, Sakmar TP and Siebert F (1993) Protonation states of membrane-embedded carboxylic acid groups in rhodopsin and metarhodospin II: A Fourier-transform infrared spectroscopy study of site-directed mutants. Proc Natl Acad Sci USA 90:10206-10210.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 10206-10210
    • Fahmy, K.1    Jager, F.2    Beck, M.3    Zvyaga, T.A.4    Sakmar, T.P.5    Siebert, F.6
  • 8
    • 0033033914 scopus 로고    scopus 로고
    • Activation mechanism of human oxytocin receptor: A combined study of experimental and computer-simulated mutagenesis
    • Fanelli F, Barbier P, Zanchetta D, De Benedetti PG and Chini B (1999a) Activation mechanism of human oxytocin receptor: A combined study of experimental and computer-simulated mutagenesis. Mol Pharmacol 56:214-225.
    • (1999) Mol Pharmacol , vol.56 , pp. 214-225
    • Fanelli, F.1    Barbier, P.2    Zanchetta, D.3    De Benedetti, P.G.4    Chini, B.5
  • 9
    • 0002843161 scopus 로고
    • Comparative molecular dynamics study of the seven-helix bundle arrangement of G-protein coupled receptors
    • Fanelli F, Menziani MC, Cocchi M and De Benedetti PG (1995) Comparative molecular dynamics study of the seven-helix bundle arrangement of G-protein coupled receptors. J Mol Struct (THEOCHEM) 333:49-69.
    • (1995) J Mol Struct (THEOCHEM) , vol.333 , pp. 49-69
    • Fanelli, F.1    Menziani, M.C.2    Cocchi, M.3    De Benedetti, P.G.4
  • 10
    • 0031712825 scopus 로고    scopus 로고
    • Ab initio modeling and molecular dynamics simulation of the α1b-adrenergic receptor activation
    • Fanelli F, Menziani MC, Scheer A, Cotecchia S and De Benedetti PG (1998) Ab initio modeling and molecular dynamics simulation of the α1b-adrenergic receptor activation. Methods 14:302-317.
    • (1998) Methods , vol.14 , pp. 302-317
    • Fanelli, F.1    Menziani, M.C.2    Scheer, A.3    Cotecchia, S.4    De Benedetti, P.G.5
  • 11
    • 0002047990 scopus 로고    scopus 로고
    • Theoretical study on receptor/G protein recognition: New insights into the mechanism of the α1b-adrenergic receptor activation
    • Fanelli F, Menziani C, Scheer A, Cotecchia S and De Benedetti PG (1999b) Theoretical study on receptor/G protein recognition: New insights into the mechanism of the α1b-adrenergic receptor activation. Int J Quantum Chem 73:71-83.
    • (1999) Int J Quantum Chem , vol.73 , pp. 71-83
    • Fanelli, F.1    Menziani, C.2    Scheer, A.3    Cotecchia, S.4    De Benedetti, P.G.5
  • 12
    • 0026780339 scopus 로고
    • Structure and function in rhodopsin. Studies of the interaction between the rhodospin cytoplasmic domain and transducin
    • Franke RR, Sakmar TP, Graham RM and Khorana HG (1992) Structure and function in rhodopsin. Studies of the interaction between the rhodospin cytoplasmic domain and transducin. J Biol Chem 267:14767-14774.
    • (1992) J Biol Chem , vol.267 , pp. 14767-14774
    • Franke, R.R.1    Sakmar, T.P.2    Graham, R.M.3    Khorana, H.G.4
  • 14
    • 0028981397 scopus 로고
    • The function of a highly conserved arginine residue in activation of the muscarinic M1 receptor
    • Jones PG. Curtis CAM and Hulme C (1995) The function of a highly conserved arginine residue in activation of the muscarinic M1 receptor. Eur J Pharmacol 288:251-257.
    • (1995) Eur J Pharmacol , vol.288 , pp. 251-257
    • Jones, P.G.1    Curtis, C.A.M.2    Hulme, C.3
  • 16
    • 0028059202 scopus 로고
    • Truncation of the receptor carboxyl terminus impairs agonist-dependent phosphorylation and desensitization of the α1B-adrenergic receptor
    • Lattion AL, Diviani D and Cotecchia S (1994) Truncation of the receptor carboxyl terminus impairs agonist-dependent phosphorylation and desensitization of the α1B-adrenergic receptor. J Biol Chem 269:22887-22893.
    • (1994) J Biol Chem , vol.269 , pp. 22887-22893
    • Lattion, A.L.1    Diviani, D.2    Cotecchia, S.3
  • 17
    • 0031037632 scopus 로고    scopus 로고
    • The role of the aspartate-arginine-tyrosine triad in the m1 muscarinic receptor: Mutations of aspartate 122 and tyrosine 124 decrease receptor expression but do not abolish signaling
    • Lu ZL, Curtis CA, Jones PG, Pavia J & Hulme EC (1997) The role of the aspartate-arginine-tyrosine triad in the m1 muscarinic receptor: Mutations of aspartate 122 and tyrosine 124 decrease receptor expression but do not abolish signaling. Mol Pharmacol 51:234-241.
    • (1997) Mol Pharmacol , vol.51 , pp. 234-241
    • Lu, Z.L.1    Curtis, C.A.2    Jones, P.G.3    Pavia, J.4    Hulme, E.C.5
  • 19
    • 0032217226 scopus 로고    scopus 로고
    • The D136A mutation of the V2 vasopressin receptor induces a constitutive activity which permits discrimination between antagonists with partial agonist and inverse agonist activities
    • Morin D, Cotte N, Balestre M-N, Mouillac B, Manning M, Breton C and Barberis C (1998) The D136A mutation of the V2 vasopressin receptor induces a constitutive activity which permits discrimination between antagonists with partial agonist and inverse agonist activities. FEBS Lett 441:470-475.
    • (1998) FEBS Lett , vol.441 , pp. 470-475
    • Morin, D.1    Cotte, N.2    Balestre, M.-N.3    Mouillac, B.4    Manning, M.5    Breton, C.6    Barberis, C.7
  • 20
    • 0030795114 scopus 로고    scopus 로고
    • Mutational analysis of the mouse 5-HT7 receptor: Importance of the third intracellular loop for receptor-G protein interaction
    • Obosi LA, Hen R, Beadle DJ, Bermudez I and King LA (1997) Mutational analysis of the mouse 5-HT7 receptor: Importance of the third intracellular loop for receptor-G protein interaction. FEBS Lett 412:321-324.
    • (1997) FEBS Lett , vol.412 , pp. 321-324
    • Obosi, L.A.1    Hen, R.2    Beadle, D.J.3    Bermudez, I.4    King, L.A.5
  • 21
    • 0028276459 scopus 로고
    • A common step for signal transduction in G protein-coupled receptors
    • Oliveira L, Paiva ACM, Sander C and Vriend G (1994) A common step for signal transduction in G protein-coupled receptors. Trends Pharmacol Sci 15:170-172.
    • (1994) Trends Pharmacol Sci , vol.15 , pp. 170-172
    • Oliveira, L.1    Paiva, A.C.M.2    Sander, C.3    Vriend, G.4
  • 22
    • 0028331771 scopus 로고
    • A constitutively active mutant β2-adrenergic receptor is constitutively desensitized and phosphorylated
    • Pei G, Samama P, Lohse M, Wang M, Codina J and Lefkowitz RJ (1994) A constitutively active mutant β2-adrenergic receptor is constitutively desensitized and phosphorylated. Proc Natl Acad Sci USA 91:2699-2702.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 2699-2702
    • Pei, G.1    Samama, P.2    Lohse, M.3    Wang, M.4    Codina, J.5    Lefkowitz, R.J.6
  • 23
    • 0027364707 scopus 로고
    • Fourier transform infrared difference spectroscopy of rhodopsin mutants: Light activation of rhodopsin causes hydrogen bonding change in residue aspartic acid-83 during meta II formation
    • Rath P, DeCaluwé LLJ, Bovee-Geurts PHM, DeGrip WJ and Rotschil KJ (1993) Fourier transform infrared difference spectroscopy of rhodopsin mutants: Light activation of rhodopsin causes hydrogen bonding change in residue aspartic acid-83 during meta II formation. Biochemistry 32:10277-10282.
    • (1993) Biochemistry , vol.32 , pp. 10277-10282
    • Rath, P.1    DeCaluwé, L.L.J.2    Bovee-Geurts, P.H.M.3    DeGrip, W.J.4    Rotschil, K.J.5
  • 24
    • 0027296623 scopus 로고
    • Constitutively active mutants of the α2-adrenergic receptor
    • published erratum appears in J Biol Chem 1994; 269:1566
    • Ren Q, Kurose H, Lefkowitz RJ and Cotecchia S (1993) Constitutively active mutants of the α2-adrenergic receptor [published erratum appears in J Biol Chem 1994; 269:1566]. J Biol Chem 268:16483-16487.
    • (1993) J Biol Chem , vol.268 , pp. 16483-16487
    • Ren, Q.1    Kurose, H.2    Lefkowitz, R.J.3    Cotecchia, S.4
  • 25
    • 0027430336 scopus 로고
    • Nephrogenic diabetes insipidus. A V2 vasopressin receptor unable to stimulate adenylyl cyclase
    • Rosenthal W, Antaramian A, Gilbert S and Birnbaumer M (1993) Nephrogenic diabetes insipidus. A V2 vasopressin receptor unable to stimulate adenylyl cyclase. J Biol Chem 268:13030-13033.
    • (1993) J Biol Chem , vol.268 , pp. 13030-13033
    • Rosenthal, W.1    Antaramian, A.2    Gilbert, S.3    Birnbaumer, M.4
  • 26
    • 0027513982 scopus 로고
    • A mutation-induced activated state of the β2-adrenergic receptor. Extending the ternary complex model
    • Samama P, Cotecchia S, Costa T and Lefkowitz RJ (1993) A mutation-induced activated state of the β2-adrenergic receptor. Extending the ternary complex model. J Biol Chem 268:4625-4636.
    • (1993) J Biol Chem , vol.268 , pp. 4625-4636
    • Samama, P.1    Cotecchia, S.2    Costa, T.3    Lefkowitz, R.J.4
  • 27
    • 0029897495 scopus 로고    scopus 로고
    • Constitutively active mutants of the α1-adrenergic receptor: Role of highly conserved polar amino acids in receptor activation
    • Scheer A, Fanelli F, Costa T, De Benedetti PG and Cotecchia S (1996) Constitutively active mutants of the α1-adrenergic receptor: Role of highly conserved polar amino acids in receptor activation. EMBO (Eur Mol Biol Organ) J 15:3566-3578.
    • (1996) EMBO (Eur Mol Biol Organ) J , vol.15 , pp. 3566-3578
    • Scheer, A.1    Fanelli, F.2    Costa, T.3    De Benedetti, P.G.4    Cotecchia, S.5
  • 28
    • 0030614337 scopus 로고    scopus 로고
    • The activation process of the α1B-adrenergic receptor: Potential role of protonation and hydrophobicity of a highly conserved aspartate
    • Scheer A, Fanelli F, Costa T, De Benedetti PG and Cotecchia S (1997) The activation process of the α1B-adrenergic receptor: Potential role of protonation and hydrophobicity of a highly conserved aspartate. Proc Natl Acad Sci USA 94:808-813.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 808-813
    • Scheer, A.1    Fanelli, F.2    Costa, T.3    De Benedetti, P.G.4    Cotecchia, S.5
  • 29
    • 0031740230 scopus 로고    scopus 로고
    • Mutations of the DRY motif preserve β2-adrenoceptor coupling
    • Seibold A, Dagarag M and Birnbaumer M (1998) Mutations of the DRY motif preserve β2-adrenoceptor coupling Receptors Channels 5:375-385.
    • (1998) Receptors Channels , vol.5 , pp. 375-385
    • Seibold, A.1    Dagarag, M.2    Birnbaumer, M.3
  • 30
    • 0032492650 scopus 로고    scopus 로고
    • Rhodopsin arginine-135 mutants are phosphorylated by rhodopsin kinase and bind arrestin in the absence of 11-cis-retinal
    • Shi W, Sports CD, Raman D, Shirakawa S, Osawa S and Weiss ER (1998) Rhodopsin arginine-135 mutants are phosphorylated by rhodopsin kinase and bind arrestin in the absence of 11-cis-retinal. Biochemistry 37:4869-4874.
    • (1998) Biochemistry , vol.37 , pp. 4869-4874
    • Shi, W.1    Sports, C.D.2    Raman, D.3    Shirakawa, S.4    Osawa, S.5    Weiss, E.R.6
  • 31
    • 0029829504 scopus 로고    scopus 로고
    • Coupling efficiency of human α1-adrenergic receptor subtypes: Titration of receptor density and responsiveness with inducible and repressible expression vectors
    • Theroux TL, Esbenshade TA, Peavy RD and Minneman KP (1996) Coupling efficiency of human α1-adrenergic receptor subtypes: Titration of receptor density and responsiveness with inducible and repressible expression vectors. Mol Pharmacol 50:1376-1387.
    • (1996) Mol Pharmacol , vol.50 , pp. 1376-1387
    • Theroux, T.L.1    Esbenshade, T.A.2    Peavy, R.D.3    Minneman, K.P.4
  • 33
    • 0015528157 scopus 로고
    • Ligand binding and internal equilibria in proteins
    • Weber G (1972) Ligand binding and internal equilibria in proteins. Biochemistry 11:864-878.
    • (1972) Biochemistry , vol.11 , pp. 864-878
    • Weber, G.1
  • 34
    • 0029935383 scopus 로고    scopus 로고
    • The cubic ternary complex receptor-occupancy model. I. Model decsription
    • Weiss JM, Morgan PH, Lutz MW and Kenakin TP (1996a) The cubic ternary complex receptor-occupancy model. I. Model decsription. J Theor Biol 178:151-167.
    • (1996) J Theor Biol , vol.178 , pp. 151-167
    • Weiss, J.M.1    Morgan, P.H.2    Lutz, M.W.3    Kenakin, T.P.4
  • 35
    • 0030596736 scopus 로고    scopus 로고
    • The cubic ternary complex receptor-occupancy model. III. Resurrecting efficacy
    • Weiss JM, Morgan PH, Lutz MW and Kenakin TP (1996b) The cubic ternary complex receptor-occupancy model. III. Resurrecting efficacy. J Theor Biol 181:381-397.
    • (1996) J Theor Biol , vol.181 , pp. 381-397
    • Weiss, J.M.1    Morgan, P.H.2    Lutz, M.W.3    Kenakin, T.P.4
  • 36
    • 0030938936 scopus 로고    scopus 로고
    • G-protein-coupled receptors: Molecular mechanisms involved in receptor activation and selectivity of G-protein recognition
    • Wess J (1997) G-protein-coupled receptors: Molecular mechanisms involved in receptor activation and selectivity of G-protein recognition. FASEB J 11:346-354.
    • (1997) FASEB J , vol.11 , pp. 346-354
    • Wess, J.1
  • 37
    • 0009603660 scopus 로고
    • An arginine conserved in most G protein-coupled receptors is essential for the function of the m1 muscarinic receptor
    • Zhu SZ. Wang SZ, Hu J and El-Fakahany E (1994) An arginine conserved in most G protein-coupled receptors is essential for the function of the m1 muscarinic receptor. Mol Pharmacol 45:517-523.
    • (1994) Mol Pharmacol , vol.45 , pp. 517-523
    • Zhu, S.Z.1    Wang, S.Z.2    Hu, J.3    El-Fakahany, E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.