메뉴 건너뛰기




Volumn 19, Issue 8, 2005, Pages 2132-2144

The Δe13 isoform of the calcitonin receptor forms a six-transmembrane domain receptor with dominant-negative effects on receptor surface expression and signaling

Author keywords

[No Author keywords available]

Indexed keywords

CALCITONIN RECEPTOR; MITOGEN ACTIVATED PROTEIN KINASE;

EID: 23744461839     PISSN: 08888809     EISSN: None     Source Type: Journal    
DOI: 10.1210/me.2004-0472     Document Type: Article
Times cited : (29)

References (38)
  • 1
    • 0014452757 scopus 로고
    • Calcitonin and parathyroid hormone
    • Copp DH 1969 Calcitonin and parathyroid hormone. Annu Rev Pharmacol 9:327-344
    • (1969) Annu Rev Pharmacol , vol.9 , pp. 327-344
    • Copp, D.H.1
  • 3
    • 0025038279 scopus 로고
    • Evidence that the action of calcitonin on rat osteoclasts is mediated by two G proteins acting via separate post-receptor pathways
    • Zaidi M, Datta HK, Moonga BS, MacIntyre I 1990 Evidence that the action of calcitonin on rat osteoclasts is mediated by two G proteins acting via separate post-receptor pathways. J Endocrinol 126:473-481
    • (1990) J Endocrinol , vol.126 , pp. 473-481
    • Zaidi, M.1    Datta, H.K.2    Moonga, B.S.3    MacIntyre, I.4
  • 4
    • 0026808506 scopus 로고
    • Differential effects of the 3′,5′-cyclic adenosine monophosphate and protein kinase C pathways on the response of isolated rat osteoclasts to calcitonin
    • Su Y, Chakraborty M, Nathanson MH, Baron R 1992 Differential effects of the 3′,5′-cyclic adenosine monophosphate and protein kinase C pathways on the response of isolated rat osteoclasts to calcitonin. Endocrinology 131:1497-1502
    • (1992) Endocrinology , vol.131 , pp. 1497-1502
    • Su, Y.1    Chakraborty, M.2    Nathanson, M.H.3    Baron, R.4
  • 8
    • 0027286432 scopus 로고
    • Molecular cloning of two receptors from rat brain with high affinity for salmon calcitonin
    • Albrandt K, Mull E, Brady EMG, Herich J, Moore CX, Beaumont K 1993 Molecular cloning of two receptors from rat brain with high affinity for salmon calcitonin. FEBS Lett 325:225-232
    • (1993) FEBS Lett , vol.325 , pp. 225-232
    • Albrandt, K.1    Mull, E.2    Brady, E.M.G.3    Herich, J.4    Moore, C.X.5    Beaumont, K.6
  • 9
    • 0029958037 scopus 로고    scopus 로고
    • The deletion of 14 amino acids in the seventh transmembrane domain of a naturally occurring calcitonin receptor isoform alters ligand binding and selectively abolishes coupling to phospholipase C
    • Shyu J-F, Inoue D, Baron R, Horne WC 1996 The deletion of 14 amino acids in the seventh transmembrane domain of a naturally occurring calcitonin receptor isoform alters ligand binding and selectively abolishes coupling to phospholipase C. J Biol Chem 271:31127-31134
    • (1996) J Biol Chem , vol.271 , pp. 31127-31134
    • Shyu, J.-F.1    Inoue, D.2    Baron, R.3    Horne, W.C.4
  • 11
    • 0037663536 scopus 로고    scopus 로고
    • The alternatively spliced Δe13 transcript of the rabbit calcitonin receptor dimerizes with the C1a isoform and inhibits its surface expression
    • Seck T, Baron R, Horne WC 2003 The alternatively spliced Δe13 transcript of the rabbit calcitonin receptor dimerizes with the C1a isoform and inhibits its surface expression. J Biol Chem 278:23085-23093
    • (2003) J Biol Chem , vol.278 , pp. 23085-23093
    • Seck, T.1    Baron, R.2    Horne, W.C.3
  • 12
    • 0033310866 scopus 로고    scopus 로고
    • A novel spliced variant of the type 1 corticotropin-releasing hormone receptor with a deletion in the seventh transmembrane domain present in the human pregnant term myometrium and fetal membranes
    • Grammatopoulos DK, Dai Y, Randeva HS, Levine MA, Karteris E, Easton AJ, Hillhouse EW 1999 A novel spliced variant of the type 1 corticotropin-releasing hormone receptor with a deletion in the seventh transmembrane domain present in the human pregnant term myometrium and fetal membranes. Mol Endocrinol 13:2189-2202
    • (1999) Mol Endocrinol , vol.13 , pp. 2189-2202
    • Grammatopoulos, D.K.1    Dai, Y.2    Randeva, H.S.3    Levine, M.A.4    Karteris, E.5    Easton, A.J.6    Hillhouse, E.W.7
  • 13
    • 4644322846 scopus 로고    scopus 로고
    • A natural variant type II G protein-coupled receptor for vasoactive intestinal peptide with altered function
    • Grinninger C, Wang W, Oskoui KB, Voice JK, Goetzl EJ 2004 A natural variant type II G protein-coupled receptor for vasoactive intestinal peptide with altered function. J Biol Chem 279:40259-40262
    • (2004) J Biol Chem , vol.279 , pp. 40259-40262
    • Grinninger, C.1    Wang, W.2    Oskoui, K.B.3    Voice, J.K.4    Goetzl, E.J.5
  • 15
    • 0032530692 scopus 로고    scopus 로고
    • Binding domain of human parathyroid hormone receptor: From conformation to function
    • Pellegrini M, Bisello A, Rosenblatt M, Chorev M, Mierke DF 1998 Binding domain of human parathyroid hormone receptor: from conformation to function. Biochemistry 37:12737-12743
    • (1998) Biochemistry , vol.37 , pp. 12737-12743
    • Pellegrini, M.1    Bisello, A.2    Rosenblatt, M.3    Chorev, M.4    Mierke, D.F.5
  • 16
    • 0038532256 scopus 로고    scopus 로고
    • Binding of filamin to the C-terminal tail of the calcitonin receptor controls recycling
    • Seck T, Baron R, Horne WC 2003 Binding of filamin to the C-terminal tail of the calcitonin receptor controls recycling. J Biol Chem 278:10408-10416
    • (2003) J Biol Chem , vol.278 , pp. 10408-10416
    • Seck, T.1    Baron, R.2    Horne, W.C.3
  • 19
    • 0032496280 scopus 로고    scopus 로고
    • Gonadotropin-releasing hormone receptors with intracellular carboxyl-terminal tails undergo acute desensitization of total inositol phosphate production and exhibit accelerated internalization kinetics
    • Heding A, Vrecl M, Bogerd J, McGregor A, Sellar R, Taylor PL, Eidne KA 1998 Gonadotropin-releasing hormone receptors with intracellular carboxyl-terminal tails undergo acute desensitization of total inositol phosphate production and exhibit accelerated internalization kinetics. J Biol Chem 273:11472-11477
    • (1998) J Biol Chem , vol.273 , pp. 11472-11477
    • Heding, A.1    Vrecl, M.2    Bogerd, J.3    McGregor, A.4    Sellar, R.5    Taylor, P.L.6    Eidne, K.A.7
  • 20
    • 0028840145 scopus 로고
    • The cytoplasmic tail of the G-protein-coupled receptor for parathyroid hormone and parathyroid hormone-related protein contains positive and negative signals for endocytosis
    • Huang Z, Chen Y, Nissenson RA 1995 The cytoplasmic tail of the G-protein-coupled receptor for parathyroid hormone and parathyroid hormone-related protein contains positive and negative signals for endocytosis. J Biol Chem 270:151-156
    • (1995) J Biol Chem , vol.270 , pp. 151-156
    • Huang, Z.1    Chen, Y.2    Nissenson, R.A.3
  • 21
    • 0030875776 scopus 로고    scopus 로고
    • Structural and functional requirements for agonist-induced internalization of the human platelet-activating factor receptor
    • Le Gouill C, Parent J-L, Rola-Pleszczynski M, Stankova J 1997 Structural and functional requirements for agonist-induced internalization of the human platelet-activating factor receptor. J Biol Chem 272:21289-21295
    • (1997) J Biol Chem , vol.272 , pp. 21289-21295
    • Le Gouill, C.1    Parent, J.-L.2    Rola-Pleszczynski, M.3    Stankova, J.4
  • 22
    • 0030054664 scopus 로고    scopus 로고
    • Truncated, desensitization-defective neurokinin receptors mediate sustained MAP kinase activation, cell growth and transformation by a Ras-independent mechanism
    • Alblas J, van Etten I, Moolenaar WH 1996 Truncated, desensitization- defective neurokinin receptors mediate sustained MAP kinase activation, cell growth and transformation by a Ras-independent mechanism. EMBO J 15:3351-3360
    • (1996) EMBO J , vol.15 , pp. 3351-3360
    • Alblas, J.1    Van Etten, I.2    Moolenaar, W.H.3
  • 23
    • 0027171693 scopus 로고
    • Identification of specific intracellular domains of the human ETA receptor required for ligand binding and signal transduction
    • Hashido K, Adachi M, Gamou T, Watanabe T, Furuichi Y, Miyamoto C 1993 Identification of specific intracellular domains of the human ETA receptor required for ligand binding and signal transduction. Cell Mol Biol Res 39:3-12
    • (1993) Cell Mol Biol Res , vol.39 , pp. 3-12
    • Hashido, K.1    Adachi, M.2    Gamou, T.3    Watanabe, T.4    Furuichi, Y.5    Miyamoto, C.6
  • 24
    • 0028785484 scopus 로고
    • Truncation of the C-terminal tail of the follitropin receptor does not impair the agonist- or phorbol ester-induced receptor phosphorylation and uncoupling
    • Hipkin RW, Liu X, Ascoli M 1995 Truncation of the C-terminal tail of the follitropin receptor does not impair the agonist- or phorbol ester-induced receptor phosphorylation and uncoupling. J Biol Chem 270: 26683-26689
    • (1995) J Biol Chem , vol.270 , pp. 26683-26689
    • Hipkin, R.W.1    Liu, X.2    Ascoli, M.3
  • 26
    • 0035011489 scopus 로고    scopus 로고
    • Regulation of transport of the dopamine D1 receptor by a new membrane-associated ER protein
    • Bermak JC, Li M, Bullock C, Zhou Q-Y 2001 Regulation of transport of the dopamine D1 receptor by a new membrane-associated ER protein. Nat Cell Biol 3:492-498
    • (2001) Nat Cell Biol , vol.3 , pp. 492-498
    • Bermak, J.C.1    Li, M.2    Bullock, C.3    Zhou, Q.-Y.4
  • 29
    • 0028587202 scopus 로고
    • Truncation of the porcine calcitonin receptor cytoplasmic tail inhibits internalization and signal transduction but increases receptor affinity
    • Findlay DM, Houssami S, Lin HY, Myers DE, Brady CL, Darcy PK, Ikeda K, Martin TJ, Sexton PM 1994 Truncation of the porcine calcitonin receptor cytoplasmic tail inhibits internalization and signal transduction but increases receptor affinity. Mol Endocrinol 8:1691-1700
    • (1994) Mol Endocrinol , vol.8 , pp. 1691-1700
    • Findlay, D.M.1    Houssami, S.2    Lin, H.Y.3    Myers, D.E.4    Brady, C.L.5    Darcy, P.K.6    Ikeda, K.7    Martin, T.J.8    Sexton, P.M.9
  • 30
    • 0028126645 scopus 로고
    • Inhibition of inositol phosphate second messenger formation by intracellular loop one of a human calcitonin receptor. Expression and mutational analysis of synthetic receptor genes
    • Nussenzveig DR, Thaw CN, Gershengorn MC 1994 Inhibition of inositol phosphate second messenger formation by intracellular loop one of a human calcitonin receptor. Expression and mutational analysis of synthetic receptor genes. J Biol Chem 269:28123-28129
    • (1994) J Biol Chem , vol.269 , pp. 28123-28129
    • Nussenzveig, D.R.1    Thaw, C.N.2    Gershengorn, M.C.3
  • 31
    • 0031776122 scopus 로고    scopus 로고
    • Effects of C-terminal truncation of the recombinant δ-opioid receptor on phospholipase C and adenylyl cyclase coupling
    • Hirst RA, Smart D, Devi LA, Lambert DG 1998 Effects of C-terminal truncation of the recombinant δ-opioid receptor on phospholipase C and adenylyl cyclase coupling. J Neurochem 70:2273-2278
    • (1998) J Neurochem , vol.70 , pp. 2273-2278
    • Hirst, R.A.1    Smart, D.2    Devi, L.A.3    Lambert, D.G.4
  • 33
    • 0036839745 scopus 로고    scopus 로고
    • Dancing with different partners: Protein kinase A phosphorylation of seven membrane-spanning receptors regulates their G protein-coupling specificity
    • Lefkowitz RJ, Pierce KL, Luttrell LM 2002 Dancing with different partners: protein kinase A phosphorylation of seven membrane-spanning receptors regulates their G protein-coupling specificity. Mol Pharmacol 62:971-974
    • (2002) Mol Pharmacol , vol.62 , pp. 971-974
    • Lefkowitz, R.J.1    Pierce, K.L.2    Luttrell, L.M.3
  • 35
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto M, Saudek V, Sklenar V 1992 Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J Biomol NMR 2:661-665
    • (1992) J Biomol NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 36
    • 0025932859 scopus 로고
    • An evaluation of computational strategies for use in determination of protein structure from distance geometry constraints obtained by nuclear magnetic resonance
    • Havel TF 1991 An evaluation of computational strategies for use in determination of protein structure from distance geometry constraints obtained by nuclear magnetic resonance. Prog Biophys Mol Biol 56:43-78
    • (1991) Prog Biophys Mol Biol , vol.56 , pp. 43-78
    • Havel, T.F.1
  • 37
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: A package for molecular simulation and trajectory analysis
    • Lindahl E, Hess B, Van der Spoel D 2001 GROMACS 3.0: A package for molecular simulation and trajectory analysis. J Mol Mod 7:306-317
    • (2001) J Mol Mod , vol.7 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    Van Der Spoel, D.3
  • 38
    • 0033609896 scopus 로고    scopus 로고
    • Cas family member HEF1 downstream of the G protein-coupled calcitonin receptor. Calcitonin induces the association of HEF1, paxillin, and focal adhesion kinase
    • Cas family member HEF1 downstream of the G protein-coupled calcitonin receptor. Calcitonin induces the association of HEF1, paxillin, and focal adhesion kinase. J Biol Chem 274:25093-250938
    • (1999) J Biol Chem , vol.274 , pp. 25093-250938
    • Zhang, Z.1    Hernandez-Lagunas, L.2    Horne, W.C.3    Baron, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.