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Volumn 70, Issue 1, 2006, Pages 249-258

Soluble mimics of the cytoplasmic face of the human V1-vascular vasopressin receptor bind arrestin2 and calmodulin

Author keywords

[No Author keywords available]

Indexed keywords

CALMODULIN; MALTOSE BINDING PROTEIN; RETINA S ANTIGEN; SCAFFOLD PROTEIN; UNCLASSIFIED DRUG; VASOPRESSIN RECEPTOR 1 ELEMENTS ON A SOLUBLE SCAFFOLD; VASOPRESSIN V1 RECEPTOR;

EID: 33745284999     PISSN: 0026895X     EISSN: 15210111     Source Type: Journal    
DOI: 10.1124/mol.105.018804     Document Type: Article
Times cited : (7)

References (41)
  • 1
    • 0034282469 scopus 로고    scopus 로고
    • Dynamic interaction of human vasopressin/oxytocin receptor subtypes with G protein-coupled receptor kinases and protein kinase C after agonist stimulation
    • Berrada K, Plesnicher CL, Luo X, and Thibonnier M (2000) Dynamic interaction of human vasopressin/oxytocin receptor subtypes with G protein-coupled receptor kinases and protein kinase C after agonist stimulation. J Biol Chem 275:27229-27237.
    • (2000) J Biol Chem , vol.275 , pp. 27229-27237
    • Berrada, K.1    Plesnicher, C.L.2    Luo, X.3    Thibonnier, M.4
  • 2
    • 0028242352 scopus 로고
    • + exchanger isoform 1 (NHE1) is a novel member of the calmodulin-binding proteins. Identification and characterization of calmodulin-binding sites
    • + exchanger isoform 1 (NHE1) is a novel member of the calmodulin-binding proteins. Identification and characterization of calmodulin-binding sites. J Biol Chem 269:13703-13709.
    • (1994) J Biol Chem , vol.269 , pp. 13703-13709
    • Bertrand, B.1    Wakabayashi, S.2    Ikeda, T.3    Pouyssegur, J.4    Shigekawa, M.5
  • 3
    • 0032101983 scopus 로고    scopus 로고
    • G-protein-coupled receptors: Turn-ons and turn-offs
    • Carman CV and Benovic JL (1998) G-protein-coupled receptors: turn-ons and turn-offs. Curr Opin Neurobiol 8:335-344.
    • (1998) Curr Opin Neurobiol , vol.8 , pp. 335-344
    • Carman, C.V.1    Benovic, J.L.2
  • 4
    • 0037088679 scopus 로고    scopus 로고
    • Conservation of the phosphate-sensitive elements in the arrestin family of proteins
    • Celver J, Vishnivetskiy SA, Chavkin C, and Gurevich VV (2002) Conservation of the phosphate-sensitive elements in the arrestin family of proteins. J Biol Chem 277:9043-9048.
    • (2002) J Biol Chem , vol.277 , pp. 9043-9048
    • Celver, J.1    Vishnivetskiy, S.A.2    Chavkin, C.3    Gurevich, V.V.4
  • 6
    • 0142179048 scopus 로고    scopus 로고
    • Soluble mimics of a chemokine receptor: Chemokine binding by receptor elements juxtaposed on a soluble scaffold
    • Datta A and Stone MJ (2003) Soluble mimics of a chemokine receptor: chemokine binding by receptor elements juxtaposed on a soluble scaffold. Protein Sci 12:2482-2491.
    • (2003) Protein Sci , vol.12 , pp. 2482-2491
    • Datta, A.1    Stone, M.J.2
  • 7
    • 10944253089 scopus 로고    scopus 로고
    • A cyclic peptide mimicking the third intracellular loop of the V2 vasopressin receptor inhibits signaling through its interaction with receptor dimer and G protein
    • Granier S, Terrillon S, Pascal R, Demene H, Bouvier M, Guillon G, and Mendre C (2004) A cyclic peptide mimicking the third intracellular loop of the V2 vasopressin receptor inhibits signaling through its interaction with receptor dimer and G protein. J Biol Chem 279:50904-50914.
    • (2004) J Biol Chem , vol.279 , pp. 50904-50914
    • Granier, S.1    Terrillon, S.2    Pascal, R.3    Demene, H.4    Bouvier, M.5    Guillon, G.6    Mendre, C.7
  • 8
    • 0027241013 scopus 로고
    • Visual arrestin interaction with rhodopsin: Sequential multisite binding ensures strict selectivity towards light-activated phosphorylated rhodopsin
    • Gurevich VV and Benovic JL (1993) Visual arrestin interaction with rhodopsin: sequential multisite binding ensures strict selectivity towards light-activated phosphorylated rhodopsin. J Biol Chem 268:11628-11638.
    • (1993) J Biol Chem , vol.268 , pp. 11628-11638
    • Gurevich, V.V.1    Benovic, J.L.2
  • 9
    • 0028924619 scopus 로고
    • Visual arrestin binding to rhodopsin: Diverse functional roles of positively charged residues within the phosphorylation-recognition region of arrestin
    • Gurevich VV and Benovic JL (1995) Visual arrestin binding to rhodopsin: diverse functional roles of positively charged residues within the phosphorylation-recognition region of arrestin. J Biol Chem 270:6010-6016.
    • (1995) J Biol Chem , vol.270 , pp. 6010-6016
    • Gurevich, V.V.1    Benovic, J.L.2
  • 10
    • 0031015458 scopus 로고    scopus 로고
    • Mechanism of phosphorylation-recognition by visual arrestin and the transition of arrestin into a high affinity binding state
    • Gurevich VV and Benovic JL (1997) Mechanism of phosphorylation- recognition by visual arrestin and the transition of arrestin into a high affinity binding state. Mol Pharmacol 51:161-169.
    • (1997) Mol Pharmacol , vol.51 , pp. 161-169
    • Gurevich, V.V.1    Benovic, J.L.2
  • 11
    • 0034006773 scopus 로고    scopus 로고
    • Arrestin: Mutagenesis, expression, purification and functional characterization
    • Gurevich VV and Benovic JL (2000) Arrestin: mutagenesis, expression, purification and functional characterization. Methods Enzymol 315:422-437.
    • (2000) Methods Enzymol , vol.315 , pp. 422-437
    • Gurevich, V.V.1    Benovic, J.L.2
  • 12
    • 10644254689 scopus 로고    scopus 로고
    • Arrestin2 expression selectively increases during neural differentiation
    • Gurevich EV, Benovic JL, and Gurevich VV (2004) Arrestin2 expression selectively increases during neural differentiation. J Neurochem 91:1404-1416.
    • (2004) J Neurochem , vol.91 , pp. 1404-1416
    • Gurevich, E.V.1    Benovic, J.L.2    Gurevich, V.V.3
  • 13
    • 0028924953 scopus 로고
    • Arrestin interactions with G protein-coupled receptors: Direct binding studies with rhodopsin, β2-adrenergic and m2 muscarinic cholinergic receptors
    • Gurevich VV, Dion SB, Onorato JJ, Ptasienski J, Kim CM, Sterne-Marr R, Hosey MM, and Benovic JL (1995) Arrestin interactions with G protein-coupled receptors: direct binding studies with rhodopsin, β2-adrenergic and m2 muscarinic cholinergic receptors. J Biol Chem 270:720-731.
    • (1995) J Biol Chem , vol.270 , pp. 720-731
    • Gurevich, V.V.1    Dion, S.B.2    Onorato, J.J.3    Ptasienski, J.4    Kim, C.M.5    Sterne-Marr, R.6    Hosey, M.M.7    Benovic, J.L.8
  • 14
    • 0842331059 scopus 로고    scopus 로고
    • The molecular acrobatics of arrestin activation
    • Gurevich VV and Gurevich EV (2004) The molecular acrobatics of arrestin activation. Trends Pharmacol Sci 25:59-112.
    • (2004) Trends Pharmacol Sci , vol.25 , pp. 59-112
    • Gurevich, V.V.1    Gurevich, E.V.2
  • 15
    • 33646414189 scopus 로고    scopus 로고
    • The structural basis of arrestin-mediated regulation of G protein-coupled receptors
    • in press
    • Gurevich VV and Gurevich EV (2006) The structural basis of arrestin-mediated regulation of G protein-coupled receptors. Pharmacol Ther, in press.
    • (2006) Pharmacol Ther
    • Gurevich, V.V.1    Gurevich, E.V.2
  • 16
    • 0030664060 scopus 로고    scopus 로고
    • Agonist-receptor-arrestin, an alternative ternary complex with high agonist affinity
    • Gurevich VV, Pals-Rylaarsdam R, Benovic JL, Hosey MM, and Onorato JJ (1997) Agonist-receptor-arrestin, an alternative ternary complex with high agonist affinity. J Biol Chem 272:28849-28852.
    • (1997) J Biol Chem , vol.272 , pp. 28849-28852
    • Gurevich, V.V.1    Pals-Rylaarsdam, R.2    Benovic, J.L.3    Hosey, M.M.4    Onorato, J.J.5
  • 17
    • 33645524290 scopus 로고    scopus 로고
    • The differential engagement of arrestin surface charges by the various functional forms of the receptor
    • Hanson SM and Gurevich VV (2006) The differential engagement of arrestin surface charges by the various functional forms of the receptor. J Biol Chem 281:3458-3462.
    • (2006) J Biol Chem , vol.281 , pp. 3458-3462
    • Hanson, S.M.1    Gurevich, V.V.2
  • 18
    • 17144384733 scopus 로고    scopus 로고
    • Calmodulin is required for vasopressin-stimulated increase in cyclic AMP production in inner medullary collecting duct
    • Hoffert JD, Chou CL, Fenton RA, and Knepper MA (2005) Calmodulin is required for vasopressin-stimulated increase in cyclic AMP production in inner medullary collecting duct. J Biol Chem 280:13624-13630.
    • (2005) J Biol Chem , vol.280 , pp. 13624-13630
    • Hoffert, J.D.1    Chou, C.L.2    Fenton, R.A.3    Knepper, M.A.4
  • 19
    • 0037305746 scopus 로고    scopus 로고
    • Insights into binding cooperativity of MATa1/MATalpha2 from the crystal structure of a MATa1 homeodomain-maltose binding protein chimera
    • Ke A and Wolberger C (2003) Insights into binding cooperativity of MATa1/MATalpha2 from the crystal structure of a MATa1 homeodomain-maltose binding protein chimera. Protein Sci 12:306-312.
    • (2003) Protein Sci , vol.12 , pp. 306-312
    • Ke, A.1    Wolberger, C.2
  • 20
    • 0028017950 scopus 로고
    • Arrestin-rhodopsin interaction. Multi-site binding delineated by peptide inhibition
    • Krupnick JG, Gurevich VV, Schepers T, Hamm HE, and Benovic JL (1994) Arrestin-rhodopsin interaction. Multi-site binding delineated by peptide inhibition. J Biol Chem 269:3226-3232.
    • (1994) J Biol Chem , vol.269 , pp. 3226-3232
    • Krupnick, J.G.1    Gurevich, V.V.2    Schepers, T.3    Hamm, H.E.4    Benovic, J.L.5
  • 21
    • 17644402459 scopus 로고    scopus 로고
    • Transduction of receptor signals by beta-arrestins
    • Lefkowitz RJ and Shenoy SK (2005) Transduction of receptor signals by beta-arrestins. Science (Wash DC) 308:512-517.
    • (2005) Science (Wash DC) , vol.308 , pp. 512-517
    • Lefkowitz, R.J.1    Shenoy, S.K.2
  • 23
    • 0029991991 scopus 로고    scopus 로고
    • Different single receptor domains determine the distinct G protein coupling profiles of members of the vasopressin receptor family
    • Liu J and Wess J (1996) Different single receptor domains determine the distinct G protein coupling profiles of members of the vasopressin receptor family. J Biol Chem 271:8772-8778.
    • (1996) J Biol Chem , vol.271 , pp. 8772-8778
    • Liu, J.1    Wess, J.2
  • 24
    • 0033582296 scopus 로고    scopus 로고
    • A direct role for arrestins in desensitization of luteinizing hormone/choriogonatropin receptor in porcine ovarian follicular membranes
    • Mukherjee S, Palczewski K, Gurevich VV, Benovic JL, Banga JP, and Hunzicker-Dunn M (1999a) A direct role for arrestins in desensitization of luteinizing hormone/choriogonatropin receptor in porcine ovarian follicular membranes. Proc Natl Acad Sci USA 96:493-498.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 493-498
    • Mukherjee, S.1    Palczewski, K.2    Gurevich, V.V.3    Benovic, J.L.4    Banga, J.P.5    Hunzicker-Dunn, M.6
  • 25
    • 0033532195 scopus 로고    scopus 로고
    • β-Arrestin dependent desensitization of luteinizing hormone/choriogonadotropin receptor is prevented by a synthetic peptide corresponding to the third intracellular loop of the receptor
    • Mukherjee S, Palczewski K, Gurevich VV, and Hunzicker-Dunn M (1999b) β-Arrestin dependent desensitization of luteinizing hormone/ choriogonadotropin receptor is prevented by a synthetic peptide corresponding to the third intracellular loop of the receptor. J Biol Chem 274:12984-12989.
    • (1999) J Biol Chem , vol.274 , pp. 12984-12989
    • Mukherjee, S.1    Palczewski, K.2    Gurevich, V.V.3    Hunzicker-Dunn, M.4
  • 26
    • 0034614524 scopus 로고    scopus 로고
    • Seven non-contiguous intracellular residues of the lutropin/ choriogonadotropin receptor dictate the rate of agonist-induced internalization and its sensitivity to non-visual arrestins
    • Nakamura K, Liu X, and Ascoli M (2000) Seven non-contiguous intracellular residues of the lutropin/choriogonadotropin receptor dictate the rate of agonist-induced internalization and its sensitivity to non-visual arrestins. J Biol Chem 275:241-247.
    • (2000) J Biol Chem , vol.275 , pp. 241-247
    • Nakamura, K.1    Liu, X.2    Ascoli, M.3
  • 27
    • 8744296089 scopus 로고    scopus 로고
    • Calmodulin interacts with the V2 vasopressin receptor: Elimination of binding to the C terminus also eliminates arginine vasopressin-stimulated elevation of intracellular calcium
    • Nickols HH, Shah VN, Chazin WJ, and Limbird LE (2004) Calmodulin interacts with the V2 vasopressin receptor: elimination of binding to the C terminus also eliminates arginine vasopressin-stimulated elevation of intracellular calcium. J Biol Chem 279:46969-46980.
    • (2004) J Biol Chem , vol.279 , pp. 46969-46980
    • Nickols, H.H.1    Shah, V.N.2    Chazin, W.J.3    Limbird, L.E.4
  • 30
    • 0037088654 scopus 로고    scopus 로고
    • Arrestin variants display differential binding characteristics for the phosphorylated N-formyl peptide receptor carboxyl terminus
    • Potter RM, Key TA, Gurevich VV, Sklar LA, and Prossnitz ER (2002) Arrestin variants display differential binding characteristics for the phosphorylated N-formyl peptide receptor carboxyl terminus. J Biol Chem 277:8970-8978.
    • (2002) J Biol Chem , vol.277 , pp. 8970-8978
    • Potter, R.M.1    Key, T.A.2    Gurevich, V.V.3    Sklar, L.A.4    Prossnitz, E.R.5
  • 31
    • 0037340792 scopus 로고    scopus 로고
    • The interaction with the cytoplasmic loops of rhodopsin plays a crucial role in arrestin activation and binding
    • Raman D, Osawa S, Gurevich VV, and Weiss ER (2003) The interaction with the cytoplasmic loops of rhodopsin plays a crucial role in arrestin activation and binding. J Neurochem 84:1040-1050.
    • (2003) J Neurochem , vol.84 , pp. 1040-1050
    • Raman, D.1    Osawa, S.2    Gurevich, V.V.3    Weiss, E.R.4
  • 32
    • 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
  • 33
    • 0031922116 scopus 로고    scopus 로고
    • Development and therapeutic indications of orally-active nonpeptide vasopressin receptor antagonists
    • Thibonnier M (1998) Development and therapeutic indications of orally-active nonpeptide vasopressin receptor antagonists. Expert Opin Investig Drugs 7:729-740.
    • (1998) Expert Opin Investig Drugs , vol.7 , pp. 729-740
    • Thibonnier, M.1
  • 34
    • 0344013488 scopus 로고    scopus 로고
    • Vasopressin receptor antagonists in heart failure
    • Thibonnier M (2003) Vasopressin receptor antagonists in heart failure. Curr Opin Pharmacol 3:683-687.
    • (2003) Curr Opin Pharmacol , vol.3 , pp. 683-687
    • Thibonnier, M.1
  • 35
    • 0032452027 scopus 로고    scopus 로고
    • Signal transduction pathways of the human V1-vascular, V2-renal, V3-pituitary vasopressin and oxytocin receptors
    • Thibonnier M, Berti-Mattera LN, Dulin N, Conarty DM, and Mattera R (1998a) Signal transduction pathways of the human V1-vascular, V2-renal, V3-pituitary vasopressin and oxytocin receptors. Prog Brain Res 119:147-161.
    • (1998) Prog Brain Res , vol.119 , pp. 147-161
    • Thibonnier, M.1    Berti-Mattera, L.N.2    Dulin, N.3    Conarty, D.M.4    Mattera, R.5
  • 36
    • 0035029158 scopus 로고    scopus 로고
    • The basic and clinical pharmacology of nonpeptide vasopressin receptor antagonists
    • Thibonnier M, Coles P, Thibonnier A, and Shoham M (2001a) The basic and clinical pharmacology of nonpeptide vasopressin receptor antagonists. Annu Rev Pharmacol Toxicol 41:175-202.
    • (2001) Annu Rev Pharmacol Toxicol , vol.41 , pp. 175-202
    • Thibonnier, M.1    Coles, P.2    Thibonnier, A.3    Shoham, M.4
  • 38
    • 0034803137 scopus 로고    scopus 로고
    • Role of the human V1 vasopressin receptor COOH terminus in internalization and mitogenic signal transduction
    • Thibonnier M, Plesnicher CL, Berrada K, and Berti-Mattera L (2001b) Role of the human V1 vasopressin receptor COOH terminus in internalization and mitogenic signal transduction. Am J Physiol 281:E81-E92.
    • (2001) Am J Physiol , vol.281
    • Thibonnier, M.1    Plesnicher, C.L.2    Berrada, K.3    Berti-Mattera, L.4
  • 39
    • 2342425115 scopus 로고    scopus 로고
    • Calmodulin interacts with the third intracellular loop of the serotonin 5-hydroxytryptamine1A receptor at two distinct sites: Putative role in receptor phosphorylation by protein kinase C
    • Turner JH, Gelasco AK, and Raymond JR (2004) Calmodulin interacts with the third intracellular loop of the serotonin 5-hydroxytryptamine1A receptor at two distinct sites: putative role in receptor phosphorylation by protein kinase C. J Biol Chem 279:17027-17037.
    • (2004) J Biol Chem , vol.279 , pp. 17027-17037
    • Turner, J.H.1    Gelasco, A.K.2    Raymond, J.R.3
  • 40
    • 0347723912 scopus 로고    scopus 로고
    • Mapping the arrestin-receptor interface. Structural elements responsible for receptor specificity of arrestin proteins
    • Vishnivetskiy SA, Hosey MM, Benovic JL, and Gurevich VV (2004) Mapping the arrestin-receptor interface. Structural elements responsible for receptor specificity of arrestin proteins. J Biol Chem 279:1262-1268.
    • (2004) J Biol Chem , vol.279 , pp. 1262-1268
    • Vishnivetskiy, S.A.1    Hosey, M.M.2    Benovic, J.L.3    Gurevich, V.V.4
  • 41
    • 0034731304 scopus 로고    scopus 로고
    • An additional phosphate-binding element in arrestin molecule: Implications for the mechanism of arrestin activation
    • Vishnivetskiy SA, Schubert C, Climaco GC, Gurevich YV, Velez M-G, and Gurevich VV (2000) An additional phosphate-binding element in arrestin molecule: implications for the mechanism of arrestin activation. J Biol Chem 275:41049-41057.
    • (2000) J Biol Chem , vol.275 , pp. 41049-41057
    • Vishnivetskiy, S.A.1    Schubert, C.2    Climaco, G.C.3    Gurevich, Y.V.4    Velez, M.-G.5    Gurevich, V.V.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.