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Volumn 269, Issue 20, 2002, Pages 5076-5087

Probing intermolecular protein-protein interactions in the calcium-sensing receptor homodimer using bioluminescence resonance energy transfer (BRET)

Author keywords

BRET; CaR; Dimerization; Family C GPCR; Homodimerization

Indexed keywords

CALCIUM SENSING RECEPTOR; DIMER; GREEN FLUORESCENT PROTEIN; LUCIFERASE; MUTANT PROTEIN;

EID: 0036415131     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2002.03218.x     Document Type: Article
Times cited : (83)

References (62)
  • 2
    • 0027938848 scopus 로고
    • Metabotropic glutamate receptors: Synaptic transmission, modulation, and plasticity
    • Nakanishi, S. (1994) Metabotropic glutamate receptors: Synaptic transmission, modulation, and plasticity. Neuron 13, 1031-1037.
    • (1994) Neuron , vol.13 , pp. 1031-1037
    • Nakanishi, S.1
  • 3
    • 0032834028 scopus 로고    scopus 로고
    • Pharmacological agents acting at subtypes of metabotropic glutamate receptors
    • Schoepp, D.D., Jane, D.E. & Monn, J.A. (1999) Pharmacological agents acting at subtypes of metabotropic glutamate receptors. Neuropharmacology 38, 1431-1476.
    • (1999) Neuropharmacology , vol.38 , pp. 1431-1476
    • Schoepp, D.D.1    Jane, D.E.2    Monn, J.A.3
  • 4
    • 0033082906 scopus 로고    scopus 로고
    • Physiology and pathophysiology of the extracellular calcium-sensing receptor
    • Brown, E.M. (1999) Physiology and pathophysiology of the extracellular calcium-sensing receptor. Am. J. Med. 106, 238-253.
    • (1999) Am. J. Med. , vol.106 , pp. 238-253
    • Brown, E.M.1
  • 6
    • 0032212737 scopus 로고    scopus 로고
    • Molecular aspects of pheromonal communication via the vomeronasal organ of mammals
    • Tirindelli, R., Mucignat-Caretta, C. & Ryba, N.J. (1998) Molecular aspects of pheromonal communication via the vomeronasal organ of mammals. Trends Neurosci. 21, 482-486.
    • (1998) Trends Neurosci. , vol.21 , pp. 482-486
    • Tirindelli, R.1    Mucignat-Caretta, C.2    Ryba, N.J.3
  • 7
    • 0033582645 scopus 로고    scopus 로고
    • Putative mammalian taste receptors: A class of taste-specific GPCRs with distinct topographic selectivity
    • Hoon, M.A., Adler, E., Lindemeier, J., Battey, J.F., Ryba, N.J. & Zuker, C.S. (1999) Putative mammalian taste receptors: A class of taste-specific GPCRs with distinct topographic selectivity. Cell 96, 541-551.
    • (1999) Cell , vol.96 , pp. 541-551
    • Hoon, M.A.1    Adler, E.2    Lindemeier, J.3    Battey, J.F.4    Ryba, N.J.5    Zuker, C.S.6
  • 8
    • 0032567334 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel retinoic acid-inducible gene that encodes a putative G protein-coupled receptor
    • Cheng, V. & Lotan, R. (1998) Molecular cloning and characterization of a novel retinoic acid-inducible gene that encodes a putative G protein-coupled receptor. J. Biol. Chem. 273, 35008-35015.
    • (1998) J. Biol. Chem. , vol.273 , pp. 35008-35015
    • Cheng, V.1    Lotan, R.2
  • 9
    • 19244382287 scopus 로고    scopus 로고
    • Sequence and expression pattern of a novel human orphan G-protein-coupled receptor, GPRC5B, a family C receptor with a short amino-terminal domain
    • Bräuner-Osborne, H. & Krogsgaard-Larsen, P. (2000) Sequence and expression pattern of a novel human orphan G-protein-coupled receptor, GPRC5B, a family C receptor with a short amino-terminal domain. Genomics 65, 121-128.
    • (2000) Genomics , vol.65 , pp. 121-128
    • Bräuner-Osborne, H.1    Krogsgaard-Larsen, P.2
  • 12
    • 0027282265 scopus 로고
    • Role of the large extracellular domain of metabotropic glutamate receptors in agonist selectivity determination
    • Takahashi, K., Tsuchida, K., Tanabe, Y., Masayuki, M. & Nakanishi, S. (1993) Role of the large extracellular domain of metabotropic glutamate receptors in agonist selectivity determination. J. Biol. Chem. 268, 19341-19345.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19341-19345
    • Takahashi, K.1    Tsuchida, K.2    Tanabe, Y.3    Masayuki, M.4    Nakanishi, S.5
  • 14
    • 0029554137 scopus 로고
    • The agonist selectivity of a class III metabotropic glutamate receptor, human mGluR4a, is determined by the N-terminal extracellular domain
    • Tones, M.A., Bendali, N., Flor, P.J., Knöpfel, T. & Kuhn, R. (1995) The agonist selectivity of a class III metabotropic glutamate receptor, human mGluR4a, is determined by the N-terminal extracellular domain. Neuroreport 7, 117-120.
    • (1995) Neuroreport , vol.7 , pp. 117-120
    • Tones, M.A.1    Bendali, N.2    Flor, P.J.3    Knöpfel, T.4    Kuhn, R.5
  • 15
    • 0032557433 scopus 로고    scopus 로고
    • Expression and purification of the extracellular ligand binding region of metabotropic glutamate receptor subtype 1
    • Okamoto, T., Sekiyama, N., Otsu, M., Shimada, Y., Sato, A., Nakanishi, S. & Jingami, H. (1998) Expression and purification of the extracellular ligand binding region of metabotropic glutamate receptor subtype 1. J. Biol. Chem. 273, 13089-13096.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13089-13096
    • Okamoto, T.1    Sekiyama, N.2    Otsu, M.3    Shimada, Y.4    Sato, A.5    Nakanishi, S.6    Jingami, H.7
  • 16
    • 0033538058 scopus 로고    scopus 로고
    • Ligand binding to the amino-terminal domain of the mGluR4 subtype of metabotropic glutamate receptor
    • Han, G. & Hampson, D.R. (1999) Ligand binding to the amino-terminal domain of the mGluR4 subtype of metabotropic glutamate receptor. J. Biol. Chem. 274, 10008-10013.
    • (1999) J. Biol. Chem. , vol.274 , pp. 10008-10013
    • Han, G.1    Hampson, D.R.2
  • 17
    • 0037650260 scopus 로고    scopus 로고
    • The agonist-binding domain of the calcium-sensing receptor is located at the amino-terminal domain
    • Bräuner-Osborne, H., Jensen, A.A., Sheppard, P.O., O'Hara, P. & Krogsgaard-Larsen, P. (1999) The agonist-binding domain of the calcium-sensing receptor is located at the amino-terminal domain. J. Biol. Chem. 274, 18382-18386.
    • (1999) J. Biol. Chem. , vol.274 , pp. 18382-18386
    • Bräuner-Osborne, H.1    Jensen, A.A.2    Sheppard, P.O.3    O'Hara, P.4    Krogsgaard-Larsen, P.5
  • 24
    • 0029903640 scopus 로고    scopus 로고
    • Metabotropic glutamate receptor 5 is a disulfide-linked dimer
    • Romano, C., Yang, W.-L. & O'Malley, K.L. (1996) Metabotropic glutamate receptor 5 is a disulfide-linked dimer. J. Biol. Chem. 271, 28612-28616.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28612-28616
    • Romano, C.1    Yang, W.-L.2    O'Malley, K.L.3
  • 25
    • 0032483541 scopus 로고    scopus 로고
    • Dimerization of the extracellular Calcium-sensing Receptor (CaR) on the cell surface of CaR-transfected HEK 293 cells
    • Bai, M., Trivedi, S. & Brown, E.M. (1998) Dimerization of the extracellular Calcium-sensing Receptor (CaR) on the cell surface of CaR-transfected HEK 293 cells. J. Biol. Chem. 273, 23605-23610.
    • (1998) J. Biol. Chem. , vol.273 , pp. 23605-23610
    • Bai, M.1    Trivedi, S.2    Brown, E.M.3
  • 28
    • 0035895907 scopus 로고    scopus 로고
    • The extracellular calcium-sensing receptor dimerizes through multiple types of intermolecular interactions
    • Zhang, Z., Sun, S., Quinn, S.J., Brown, E.M. & Bai, M. (2001) The extracellular calcium-sensing receptor dimerizes through multiple types of intermolecular interactions. J. Biol. Chem. 276, 5316-5322.
    • (2001) J. Biol. Chem. , vol.276 , pp. 5316-5322
    • Zhang, Z.1    Sun, S.2    Quinn, S.J.3    Brown, E.M.4    Bai, M.5
  • 30
    • 0027297275 scopus 로고
    • Constitutive activity of receptors coupled to guanine nucleotide regulatory proteins
    • Lefkowitz, R.J., Cotecchia, S., Samama, P. & Costa, T. (1993) Constitutive activity of receptors coupled to guanine nucleotide regulatory proteins. Trends Pharmacol. Sci. 14, 303-307.
    • (1993) Trends Pharmacol. Sci. , vol.14 , pp. 303-307
    • Lefkowitz, R.J.1    Cotecchia, S.2    Samama, P.3    Costa, T.4
  • 31
    • 0028950255 scopus 로고
    • The two-state model of receptor activation
    • Leff, P. (1995) The two-state model of receptor activation. Trends Pharmacol. Sci. 16, 89-97.
    • (1995) Trends Pharmacol. Sci. , vol.16 , pp. 89-97
    • Leff, P.1
  • 32
    • 0033548048 scopus 로고    scopus 로고
    • Erythropoietin receptor activation by a ligand-induced conformation change
    • Remy, I., Wilson, I.A. & Michnick, S.W. (1999) Erythropoietin receptor activation by a ligand-induced conformation change. Science 283, 990-993.
    • (1999) Science , vol.283 , pp. 990-993
    • Remy, I.1    Wilson, I.A.2    Michnick, S.W.3
  • 33
    • 0034644539 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Schlessinger, J. (2000) Cell signaling by receptor tyrosine kinases. Cell 103, 211-225.
    • (2000) Cell , vol.103 , pp. 211-225
    • Schlessinger, J.1
  • 34
    • 0034724192 scopus 로고    scopus 로고
    • Detection of β2-adrenergic receptor dimerization in living cells using bioluminescence resonance energy transfer (BRET)
    • Angers, S., Salahpour, A., Joly, E., Hilairet, S., Chelsky, D., Dennis, M. & Bouvier, M. (2000) Detection of β2-adrenergic receptor dimerization in living cells using bioluminescence resonance energy transfer (BRET). Proc. Natl Acad. Sci. USA 97, 3684-3689.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 3684-3689
    • Angers, S.1    Salahpour, A.2    Joly, E.3    Hilairet, S.4    Chelsky, D.5    Dennis, M.6    Bouvier, M.7
  • 35
    • 0035918215 scopus 로고    scopus 로고
    • Constitutive and agonist-dependent homo-oligomerization of the thyrotropin-releasing hormone receptor
    • Kroeger, K.M., Hanyaloglu, A.C., Seeber, R.M., Miles, L.E.C. & Eidne, K.A. (2001) Constitutive and agonist-dependent homo-oligomerization of the thyrotropin-releasing hormone receptor. J. Biol. Chem. 276, 12736-12743.
    • (2001) J. Biol. Chem. , vol.276 , pp. 12736-12743
    • Kroeger, K.M.1    Hanyaloglu, A.C.2    Seeber, R.M.3    Miles, L.E.C.4    Eidne, K.A.5
  • 36
    • 0034616021 scopus 로고    scopus 로고
    • Receptors for dopamine and somatostatin: Formation of hetero-oligomers with enhanced functional activity
    • Rocheville, M., Lange, D.C., Kumar, U., Sasi, R., Patel, R.C. & Patel, Y.C. (2000) Receptors for dopamine and somatostatin: formation of hetero-oligomers with enhanced functional activity. Science 288, 154-157.
    • (2000) Science , vol.288 , pp. 154-157
    • Rocheville, M.1    Lange, D.C.2    Kumar, U.3    Sasi, R.4    Patel, R.C.5    Patel, Y.C.6
  • 37
    • 0035910464 scopus 로고    scopus 로고
    • Gonadotropin-releasing hormone receptor microaggregation
    • Cornea, A., Janovick, J.A., Maya-Núnez, G. & Conn, P.M. (2001) Gonadotropin-releasing hormone receptor microaggregation. J. Biol. Chem. 276, 2153-2158.
    • (2001) J. Biol. Chem. , vol.276 , pp. 2153-2158
    • Cornea, A.1    Janovick, J.A.2    Maya-Núnez, G.3    Conn, P.M.4
  • 38
    • 0034677745 scopus 로고    scopus 로고
    • Subtypes of somatostatin receptor assemble as functional homo- and heterodimers
    • Rocheville, M., Lange, D.C., Kumar, U., Sasi, R., Patel, R.C. & Patel, Y.C. (2000) Subtypes of somatostatin receptor assemble as functional homo- and heterodimers. J. Biol. Chem. 275, 7862-7869.
    • (2000) J. Biol. Chem. , vol.275 , pp. 7862-7869
    • Rocheville, M.1    Lange, D.C.2    Kumar, U.3    Sasi, R.4    Patel, R.C.5    Patel, Y.C.6
  • 39
    • 0035958023 scopus 로고    scopus 로고
    • Monitoring receptor oligomerization using time-resolved fluorescence resonance energy transfer and bioluminescence resonance energy transfer
    • McVey, M., Ramsay, D., Kellett, E., Rees, S., Wilson, S., Pope, A.J. & Milligan, G. (2001) Monitoring receptor oligomerization using time-resolved fluorescence resonance energy transfer and bioluminescence resonance energy transfer. J. Biol. Chem. 276, 14092-14099.
    • (2001) J. Biol. Chem. , vol.276 , pp. 14092-14099
    • McVey, M.1    Ramsay, D.2    Kellett, E.3    Rees, S.4    Wilson, S.5    Pope, A.J.6    Milligan, G.7
  • 40
    • 0033524455 scopus 로고    scopus 로고
    • A bioluminescence resonance energy transfer (BRET) system: Application to interacting circadian clock proteins
    • Xu, Y., Piston, D.W. & Johnson, C.H. (1999) A bioluminescence resonance energy transfer (BRET) system: Application to interacting circadian clock proteins. Proc. Natl Acad. Sci. USA 96, 151-156.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 151-156
    • Xu, Y.1    Piston, D.W.2    Johnson, C.H.3
  • 41
    • 0037101774 scopus 로고    scopus 로고
    • Homo- and hetero-oligomeric interactions between G protein-coupled receptors in living cells monitored by two variants of bioluminescence resonance energy transfer
    • Ramsay, D., Kellett, E., McVey, M., Rees, S. & Milligan, G. (2002) Homo- and hetero-oligomeric interactions between G protein-coupled receptors in living cells monitored by two variants of bioluminescence resonance energy transfer. Biochem. J. 15, 429-440.
    • (2002) Biochem. J. , vol.15 , pp. 429-440
    • Ramsay, D.1    Kellett, E.2    McVey, M.3    Rees, S.4    Milligan, G.5
  • 42
    • 0028955536 scopus 로고
    • Calcium sensing receptor: Molecular cloning in rat and localization to nerve terminals
    • Ruat, M., Molliver, M.E., Snowman, A.M. & Snyder, S.H. (1995) Calcium sensing receptor: Molecular cloning in rat and localization to nerve terminals. Proc. Natl Acad. Sci. USA 92, 3161-3165.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 3161-3165
    • Ruat, M.1    Molliver, M.E.2    Snowman, A.M.3    Snyder, S.H.4
  • 43
    • 0026093312 scopus 로고
    • Sequence and expression of a metabotropic glutamate receptor
    • Masu, M., Tanabe, Y., Tsuchida, K., Shigemoto, R. & Nakanishi, S. (1991) Sequence and expression of a metabotropic glutamate receptor. Nature 349, 760-765.
    • (1991) Nature , vol.349 , pp. 760-765
    • Masu, M.1    Tanabe, Y.2    Tsuchida, K.3    Shigemoto, R.4    Nakanishi, S.5
  • 44
    • 0028288443 scopus 로고
    • Functional expression and properties of the human skeletal muscle sodium channel
    • Chahine, M., Bennett, P.B., George, A.L.Jr & Horn, R. (1994) Functional expression and properties of the human skeletal muscle sodium channel. Pflügers Arch. 427, 136-142.
    • (1994) Pflügers Arch. , vol.427 , pp. 136-142
    • Chahine, M.1    Bennett, P.B.2    George A.L., Jr.3    Horn, R.4
  • 45
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • Tsien, R.Y. (1998) The green fluorescent protein. Annu. Rev. Biochem. 67, 509-544.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 509-544
    • Tsien, R.Y.1
  • 48
    • 0032491497 scopus 로고    scopus 로고
    • 2+ activation of the human calcium sensing receptor
    • 2+ activation of the human calcium sensing receptor. J. Biol. Chem. 45, 29712-29718.
    • (1998) J. Biol. Chem. , vol.45 , pp. 29712-29718
    • Gama, L.1    Breitwieser, G.E.2
  • 49
    • 0031450210 scopus 로고    scopus 로고
    • The carboxyl terminus of the human calcium receptor. Requirements for cell-surface expression and signal transduction
    • Ray, K., Fan, G.F., Goldsmith, P.K. & Spiegel, A.M. (1997) The carboxyl terminus of the human calcium receptor. Requirements for cell-surface expression and signal transduction. J. Biol. Chem. 272, 31355-31361.
    • (1997) J. Biol. Chem. , vol.272 , pp. 31355-31361
    • Ray, K.1    Fan, G.F.2    Goldsmith, P.K.3    Spiegel, A.M.4
  • 53
    • 84981779372 scopus 로고
    • Zwischenmolekulare energiewanderung und fluoreszenz
    • Förster, V.T. (1948) Zwischenmolekulare energiewanderung und fluoreszenz. Ann. Phys. 6, 54-75.
    • (1948) Ann. Phys. , vol.6 , pp. 54-75
    • Förster, V.T.1
  • 54
    • 0028913136 scopus 로고
    • Fluorescence resonance energy transfer
    • Selvin, P.R. (1995) Fluorescence resonance energy transfer. Meth. Enzymol. 246, 300-334.
    • (1995) Meth. Enzymol. , vol.246 , pp. 300-334
    • Selvin, P.R.1
  • 55
    • 0035914405 scopus 로고    scopus 로고
    • Heterodimerization of calcium sensing receptors with metabotropic glutamate receptors in neurons
    • Gama, L., Wilt, S.G. & Breitwieser, G.E. (2001) Heterodimerization of calcium sensing receptors with metabotropic glutamate receptors in neurons. J. Biol. Chem. 276, 39053-39059.
    • (2001) J. Biol. Chem. , vol.276 , pp. 39053-39059
    • Gama, L.1    Wilt, S.G.2    Breitwieser, G.E.3
  • 57
    • 0034801960 scopus 로고    scopus 로고
    • Monitoring the activation state of the insulin receptor using bioluminescence resonance energy transfer
    • Boute, N., Pernet, K. & Issad, T. (2001) Monitoring the activation state of the insulin receptor using bioluminescence resonance energy transfer. Mol. Pharmacol. 60, 640-645.
    • (2001) Mol. Pharmacol. , vol.60 , pp. 640-645
    • Boute, N.1    Pernet, K.2    Issad, T.3
  • 58
    • 0032545265 scopus 로고    scopus 로고
    • Identification of the sites of N-linked glycosylation on the human calcium receptor and assessment of their role in cell surface expression and signal transduction
    • Ray, K., Clapp, P., Goldsmith, P.K. & Spiegel, A.M. (1998) Identification of the sites of N-linked glycosylation on the human calcium receptor and assessment of their role in cell surface expression and signal transduction. J. Biol. Chem. 273, 34558-34567.
    • (1998) J. Biol. Chem. , vol.273 , pp. 34558-34567
    • Ray, K.1    Clapp, P.2    Goldsmith, P.K.3    Spiegel, A.M.4
  • 60
    • 0029963929 scopus 로고    scopus 로고
    • Changes in the carboxyl-terminal of metabotropic glutamate receptor 1 by alternative splicing generate receptors with differing agonist-independent activity
    • Prézeau, L., Gomeza, J., Ahern, S., Mary, S., Galvez, T., Bockaert, J. & Pin, J.-P. (1996) Changes in the carboxyl-terminal of metabotropic glutamate receptor 1 by alternative splicing generate receptors with differing agonist-independent activity. Mol. Pharmacol. 49, 422-429.
    • (1996) Mol. Pharmacol. , vol.49 , pp. 422-429
    • Prézeau, L.1    Gomeza, J.2    Ahern, S.3    Mary, S.4    Galvez, T.5    Bockaert, J.6    Pin, J.-P.7


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