메뉴 건너뛰기




Volumn 26, Issue 3, 2005, Pages 131-137

Emerging role of homo- and heterodimerization in G-protein-coupled receptor biosynthesis and maturation

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; DIMER; G PROTEIN COUPLED RECEPTOR;

EID: 14644387575     PISSN: 01656147     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tips.2005.01.004     Document Type: Review
Times cited : (402)

References (90)
  • 1
    • 0035318509 scopus 로고    scopus 로고
    • Oligomerization of G-protein-coupled transmitter receptors
    • M. Bouvier Oligomerization of G-protein-coupled transmitter receptors Nat. Rev. Neurosci. 2 2001 274 286
    • (2001) Nat. Rev. Neurosci. , vol.2 , pp. 274-286
    • Bouvier, M.1
  • 2
    • 0347320632 scopus 로고    scopus 로고
    • G-protein coupled receptor oligomerization in neuroendocrine pathways
    • K.M. Kroeger G-protein coupled receptor oligomerization in neuroendocrine pathways Front. Neuroendocrinol. 24 2003 254 278
    • (2003) Front. Neuroendocrinol. , vol.24 , pp. 254-278
    • Kroeger, K.M.1
  • 3
    • 0346059583 scopus 로고    scopus 로고
    • G protein-coupled receptor oligomerization: Implications for G protein activation and cell signaling
    • G.E. Breitwieser G protein-coupled receptor oligomerization: implications for G protein activation and cell signaling Circ. Res. 94 2004 17 27
    • (2004) Circ. Res. , vol.94 , pp. 17-27
    • Breitwieser, G.E.1
  • 4
    • 0242572132 scopus 로고    scopus 로고
    • Dimerization of G-protein-coupled receptors: Roles in signal transduction
    • M. Bai Dimerization of G-protein-coupled receptors: roles in signal transduction Cell. Signal. 16 2004 175 186
    • (2004) Cell. Signal. , vol.16 , pp. 175-186
    • Bai, M.1
  • 5
    • 0033201455 scopus 로고    scopus 로고
    • B receptors - The first 7TM heterodimers
    • B receptors - the first 7TM heterodimers Trends Pharmacol. Sci. 20 1999 396 399
    • (1999) Trends Pharmacol. Sci. , vol.20 , pp. 396-399
    • Marshall, F.H.1
  • 6
    • 0036174608 scopus 로고    scopus 로고
    • Dimerization: An emerging concept for G protein-coupled receptor ontogeny and function
    • S. Angers Dimerization: an emerging concept for G protein-coupled receptor ontogeny and function Annu. Rev. Pharmacol. Toxicol. 42 2002 409 435
    • (2002) Annu. Rev. Pharmacol. Toxicol. , vol.42 , pp. 409-435
    • Angers, S.1
  • 7
    • 0038170289 scopus 로고    scopus 로고
    • Applications of novel resonance energy transfer techniques to study dynamic hormone receptor interactions in living cells
    • K.A. Eidne Applications of novel resonance energy transfer techniques to study dynamic hormone receptor interactions in living cells Trends Endocrinol. Metab. 13 2002 415 421
    • (2002) Trends Endocrinol. Metab. , vol.13 , pp. 415-421
    • Eidne, K.A.1
  • 8
    • 0036780743 scopus 로고    scopus 로고
    • G-protein-coupled receptor oligomerization and its potential for drug discovery
    • S.R. George G-protein-coupled receptor oligomerization and its potential for drug discovery Nat. Rev. Drug Discov. 1 2002 808 820
    • (2002) Nat. Rev. Drug Discov. , vol.1 , pp. 808-820
    • George, S.R.1
  • 9
    • 0037426865 scopus 로고    scopus 로고
    • Atomic-force microscopy: Rhodopsin dimers in native disc membranes
    • D.L.Y. Fotiadis Atomic-force microscopy: rhodopsin dimers in native disc membranes Nature 421 2003 127 128
    • (2003) Nature , vol.421 , pp. 127-128
    • Fotiadis, D.L.Y.1
  • 10
    • 0034604451 scopus 로고    scopus 로고
    • Crystal structure of rhodopsin: A G protein-coupled receptor
    • K. Palczewski Crystal structure of rhodopsin: a G protein-coupled receptor Science 289 2000 739 745
    • (2000) Science , vol.289 , pp. 739-745
    • Palczewski, K.1
  • 11
    • 0030034646 scopus 로고    scopus 로고
    • Crystal structure of a G-protein beta gamma dimer at 2.1A resolution
    • J. Sondek Crystal structure of a G-protein beta gamma dimer at 2.1A resolution Nature 379 1996 369 374
    • (1996) Nature , vol.379 , pp. 369-374
    • Sondek, J.1
  • 12
    • 0029664589 scopus 로고    scopus 로고
    • The 2.0 a crystal structure of a heterotrimeric G protein
    • D.G. Lambright The 2.0 A crystal structure of a heterotrimeric G protein Nature 379 1996 311 319
    • (1996) Nature , vol.379 , pp. 311-319
    • Lambright, D.G.1
  • 13
    • 0035942220 scopus 로고    scopus 로고
    • How activated receptors couple to G proteins
    • H.E. Hamm How activated receptors couple to G proteins Proc. Natl. Acad. Sci. U. S. A. 98 2001 4819 4821
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 4819-4821
    • Hamm, H.E.1
  • 14
    • 0038392702 scopus 로고    scopus 로고
    • Structure-based analysis of GPCR function: Evidence for a novel pentameric assembly between the dimeric leukotriene B4 receptor BLT1 and the G-protein
    • J.L. Baneres, and J. Parello Structure-based analysis of GPCR function: evidence for a novel pentameric assembly between the dimeric leukotriene B4 receptor BLT1 and the G-protein J. Mol. Biol. 329 2003 815 829
    • (2003) J. Mol. Biol. , vol.329 , pp. 815-829
    • Baneres, J.L.1    Parello, J.2
  • 15
    • 3543036363 scopus 로고    scopus 로고
    • Closed state of both binding domains of homodimeric mGlu receptors is required for full activity
    • J. Kniazeff Closed state of both binding domains of homodimeric mGlu receptors is required for full activity Nat. Struct. Mol. Biol. 11 2004 706 713
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 706-713
    • Kniazeff, J.1
  • 16
    • 0038662595 scopus 로고    scopus 로고
    • Evolution, structure, and activation mechanism of family 3/C G-protein-coupled receptors
    • J.P. Pin Evolution, structure, and activation mechanism of family 3/C G-protein-coupled receptors Pharmacol. Ther. 98 2003 325 354
    • (2003) Pharmacol. Ther. , vol.98 , pp. 325-354
    • Pin, J.P.1
  • 17
    • 0033516576 scopus 로고    scopus 로고
    • Identification and molecular characterization of m3 muscarinic receptor dimers
    • F.Y. Zeng, and J. Wess Identification and molecular characterization of m3 muscarinic receptor dimers J. Biol. Chem. 274 1999 19487 19497
    • (1999) J. Biol. Chem. , vol.274 , pp. 19487-19497
    • Zeng, F.Y.1    Wess, J.2
  • 18
    • 0035958023 scopus 로고    scopus 로고
    • Monitoring receptor oligomerization using time-resolved fluorescence resonance energy transfer and bioluminescence resonance energy transfer. The human delta -opioid receptor displays constitutive oligomerization at the cell surface, which is not regulated by receptor occupancy
    • M. McVey Monitoring receptor oligomerization using time-resolved fluorescence resonance energy transfer and bioluminescence resonance energy transfer. The human delta -opioid receptor displays constitutive oligomerization at the cell surface, which is not regulated by receptor occupancy J. Biol. Chem. 276 2001 14092 14099
    • (2001) J. Biol. Chem. , vol.276 , pp. 14092-14099
    • McVey, M.1
  • 19
    • 0034704906 scopus 로고    scopus 로고
    • G-protein-coupled receptors function as oligomers in vivo
    • M.C. Overton, and K.J. Blumer G-protein-coupled receptors function as oligomers in vivo Curr. Biol. 10 2000 341 344
    • (2000) Curr. Biol. , vol.10 , pp. 341-344
    • Overton, M.C.1    Blumer, K.J.2
  • 20
    • 0037077208 scopus 로고    scopus 로고
    • Monitoring of ligand-independent dimerization and ligand-induced conformational changes of melatonin receptors in living cells by bioluminescence resonance energy transfer
    • M.A. Ayoub Monitoring of ligand-independent dimerization and ligand-induced conformational changes of melatonin receptors in living cells by bioluminescence resonance energy transfer J. Biol. Chem. 277 2002 21522 21528
    • (2002) J. Biol. Chem. , vol.277 , pp. 21522-21528
    • Ayoub, M.A.1
  • 21
    • 0037144581 scopus 로고    scopus 로고
    • Constitutive agonist-independent CCR5 oligomerization and antibody- mediated clustering occurring at physiological levels of receptors
    • H. Issafras Constitutive agonist-independent CCR5 oligomerization and antibody- mediated clustering occurring at physiological levels of receptors J. Biol. Chem. 277 2002 34666 34673
    • (2002) J. Biol. Chem. , vol.277 , pp. 34666-34673
    • Issafras, H.1
  • 22
    • 0036415131 scopus 로고    scopus 로고
    • Probing intermolecular protein-protein interactions in the calcium-sensing receptor homodimer using bioluminescence resonance energy transfer (BRET)
    • A.A. Jensen Probing intermolecular protein-protein interactions in the calcium-sensing receptor homodimer using bioluminescence resonance energy transfer (BRET) Eur. J. Biochem. 269 2002 5076 5087
    • (2002) Eur. J. Biochem. , vol.269 , pp. 5076-5087
    • Jensen, A.A.1
  • 23
    • 0037384043 scopus 로고    scopus 로고
    • Oxytocin and vasopressin V1a and V2 receptors form constitutive homo- and heterodimers during biosynthesis
    • S. Terrillon Oxytocin and vasopressin V1a and V2 receptors form constitutive homo- and heterodimers during biosynthesis Mol. Endocrinol. 17 2003 677 691
    • (2003) Mol. Endocrinol. , vol.17 , pp. 677-691
    • Terrillon, S.1
  • 24
    • 0037474238 scopus 로고    scopus 로고
    • Ligand-independent dimerization of CXCR4, a principal HIV-1 coreceptor
    • G.J. Babcock Ligand-independent dimerization of CXCR4, a principal HIV-1 coreceptor J. Biol. Chem. 278 2003 3378 3385
    • (2003) J. Biol. Chem. , vol.278 , pp. 3378-3385
    • Babcock, G.J.1
  • 25
    • 4043125390 scopus 로고    scopus 로고
    • Homodimerization of the {beta}2-Adrenergic Receptor as a Prerequisite for Cell Surface Targeting
    • A. Salahpour Homodimerization of the {beta}2-Adrenergic Receptor as a Prerequisite for Cell Surface Targeting J. Biol. Chem. 279 2004 33390 33397
    • (2004) J. Biol. Chem. , vol.279 , pp. 33390-33397
    • Salahpour, A.1
  • 26
    • 0042467972 scopus 로고    scopus 로고
    • Molecular mechanisms and therapeutical implications of intramembrane receptor/receptor interactions among heptahelical receptors with examples from the striatopallidal GABA neurons
    • L.F. Agnati Molecular mechanisms and therapeutical implications of intramembrane receptor/receptor interactions among heptahelical receptors with examples from the striatopallidal GABA neurons Pharmacol. Rev. 55 2003 509 550
    • (2003) Pharmacol. Rev. , vol.55 , pp. 509-550
    • Agnati, L.F.1
  • 27
    • 0033667466 scopus 로고    scopus 로고
    • (B) receptor heterodimerization
    • (B) receptor heterodimerization Neuron 27 2000 97 106
    • (2000) Neuron , vol.27 , pp. 97-106
    • Margeta-Mitrovic, M.1
  • 28
    • 0033118334 scopus 로고    scopus 로고
    • Molecular tinkering of G protein-coupled receptors: An evolutionary success
    • J. Bockaert, and J.P. Pin Molecular tinkering of G protein-coupled receptors: an evolutionary success EMBO J. 18 1999 1723 1729
    • (1999) EMBO J. , vol.18 , pp. 1723-1729
    • Bockaert, J.1    Pin, J.P.2
  • 29
    • 2442597256 scopus 로고    scopus 로고
    • Cell surface expression of alpha1D-adrenergic receptors is controlled by heterodimerization with alpha1B-adrenergic receptors
    • C. Hague Cell surface expression of alpha1D-adrenergic receptors is controlled by heterodimerization with alpha1B-adrenergic receptors J. Biol. Chem. 279 2004 15541 15549
    • (2004) J. Biol. Chem. , vol.279 , pp. 15541-15549
    • Hague, C.1
  • 30
    • 4544226342 scopus 로고    scopus 로고
    • Olfactory receptor surface expression is driven by association with the beta2-adrenergic receptor
    • C. Hague Olfactory receptor surface expression is driven by association with the beta2-adrenergic receptor Proc. Natl. Acad. Sci. U. S. A. 101 2004 13672 13676
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 13672-13676
    • Hague, C.1
  • 31
    • 0035839040 scopus 로고    scopus 로고
    • Mammalian sweet taste receptors
    • G. Nelson Mammalian sweet taste receptors Cell 106 2001 381 390
    • (2001) Cell , vol.106 , pp. 381-390
    • Nelson, G.1
  • 32
    • 0037075555 scopus 로고    scopus 로고
    • An amino-acid taste receptor
    • G. Nelson An amino-acid taste receptor Nature 416 2002 199 202
    • (2002) Nature , vol.416 , pp. 199-202
    • Nelson, G.1
  • 33
    • 0030712312 scopus 로고    scopus 로고
    • Mechanism of transdominant inhibition of CCR5-mediated HIV-1 infection by ccr5delta32
    • M. Benkirane Mechanism of transdominant inhibition of CCR5-mediated HIV-1 infection by ccr5delta32 J. Biol. Chem. 272 1997 30603 30606
    • (1997) J. Biol. Chem. , vol.272 , pp. 30603-30606
    • Benkirane, M.1
  • 34
    • 0035108034 scopus 로고    scopus 로고
    • Naturally occurring deletional mutation in the C-terminal cytoplasmic tail of CCR5 affects surface trafficking of CCR5
    • T. Shioda Naturally occurring deletional mutation in the C-terminal cytoplasmic tail of CCR5 affects surface trafficking of CCR5 J. Virol. 75 2001 3462 3468
    • (2001) J. Virol. , vol.75 , pp. 3462-3468
    • Shioda, T.1
  • 35
    • 1342332090 scopus 로고    scopus 로고
    • Mutant Frizzled 4 associated with vitreoretinopathy traps wild-type Frizzled in the endoplasmic reticulum by oligomerization
    • A. Kaykas Mutant Frizzled 4 associated with vitreoretinopathy traps wild-type Frizzled in the endoplasmic reticulum by oligomerization Nat. Cell Biol. 6 2004 52 58
    • (2004) Nat. Cell Biol. , vol.6 , pp. 52-58
    • Kaykas, A.1
  • 36
    • 1542467519 scopus 로고    scopus 로고
    • Oligomerization, biogenesis, and signaling is promoted by a glycophorin A-like dimerization motif in transmembrane domain 1 of a yeast G protein-coupled receptor
    • M.C. Overton Oligomerization, biogenesis, and signaling is promoted by a glycophorin A-like dimerization motif in transmembrane domain 1 of a yeast G protein-coupled receptor J. Biol. Chem. 278 2003 49369 49377
    • (2003) J. Biol. Chem. , vol.278 , pp. 49369-49377
    • Overton, M.C.1
  • 37
    • 0029666267 scopus 로고    scopus 로고
    • A peptide derived from a beta2-adrenergic receptor transmembrane domain inhibits both receptor dimerization and activation
    • T.E. Hebert A peptide derived from a beta2-adrenergic receptor transmembrane domain inhibits both receptor dimerization and activation J. Biol. Chem. 271 1996 16384 16392
    • (1996) J. Biol. Chem. , vol.271 , pp. 16384-16392
    • Hebert, T.E.1
  • 38
    • 0032482220 scopus 로고    scopus 로고
    • Folding of insulin receptor monomers is facilitated by the molecular chaperones calnexin and calreticulin and impaired by rapid dimerization
    • J. Bass Folding of insulin receptor monomers is facilitated by the molecular chaperones calnexin and calreticulin and impaired by rapid dimerization J. Cell Biol. 141 1998 637 646
    • (1998) J. Cell Biol. , vol.141 , pp. 637-646
    • Bass, J.1
  • 39
    • 2942623604 scopus 로고    scopus 로고
    • Proreceptor dimerization is required for insulin receptor post-translational processing
    • J.J. Wu, and G. Guidotti Proreceptor dimerization is required for insulin receptor post-translational processing J. Biol. Chem. 279 2004 25765 25773
    • (2004) J. Biol. Chem. , vol.279 , pp. 25765-25773
    • Wu, J.J.1    Guidotti, G.2
  • 40
    • 0037162458 scopus 로고    scopus 로고
    • Ligand-independent growth hormone receptor dimerization occurs in the endoplasmic reticulum and is required for ubiquitin system-dependent endocytosis
    • J. Gent Ligand-independent growth hormone receptor dimerization occurs in the endoplasmic reticulum and is required for ubiquitin system-dependent endocytosis Proc. Natl. Acad. Sci. U. S. A. 99 2002 9858 9863
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 9858-9863
    • Gent, J.1
  • 41
    • 0032559594 scopus 로고    scopus 로고
    • Oligomeric structure of type I and type II transforming growth factor beta receptors: Homodimers form in the ER and persist at the plasma membrane
    • L. Gilboa Oligomeric structure of type I and type II transforming growth factor beta receptors: homodimers form in the ER and persist at the plasma membrane J. Cell Biol. 140 1998 767 777
    • (1998) J. Cell Biol. , vol.140 , pp. 767-777
    • Gilboa, L.1
  • 42
    • 0033103174 scopus 로고    scopus 로고
    • A new ER trafficking signal regulates the subunit stoichiometry of plasma membrane K(ATP) channels
    • N. Zerangue A new ER trafficking signal regulates the subunit stoichiometry of plasma membrane K(ATP) channels Neuron 22 1999 537 548
    • (1999) Neuron , vol.22 , pp. 537-548
    • Zerangue, N.1
  • 43
    • 0033137035 scopus 로고    scopus 로고
    • Potassium channels: Some assembly required
    • D.M. Papazian Potassium channels: some assembly required Neuron 23 1999 7 10
    • (1999) Neuron , vol.23 , pp. 7-10
    • Papazian, D.M.1
  • 44
    • 0032128150 scopus 로고    scopus 로고
    • Assembly, sorting, and exit of oligomeric proteins from the endoplasmic reticulum
    • P.S. Reddy, and R.B. Corley Assembly, sorting, and exit of oligomeric proteins from the endoplasmic reticulum Bioessays 20 1998 546 554
    • (1998) Bioessays , vol.20 , pp. 546-554
    • Reddy, P.S.1    Corley, R.B.2
  • 45
    • 0037336295 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum
    • L. Ellgaard, and A. Helenius Quality control in the endoplasmic reticulum Nat. Rev. Mol. Cell Biol. 4 2003 181 191
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 181-191
    • Ellgaard, L.1    Helenius, A.2
  • 46
    • 0037447231 scopus 로고    scopus 로고
    • 14-3-3 Dimers probe the assembly status of multimeric membrane proteins
    • H. Yuan 14-3-3 dimers probe the assembly status of multimeric membrane proteins Curr. Biol. 13 2003 638 646
    • (2003) Curr. Biol. , vol.13 , pp. 638-646
    • Yuan, H.1
  • 47
    • 0033531936 scopus 로고    scopus 로고
    • The zeta isoform of 14-3-3 proteins interacts with the third intracellular loop of different alpha2-adrenergic receptor subtypes
    • L. Prezeau The zeta isoform of 14-3-3 proteins interacts with the third intracellular loop of different alpha2-adrenergic receptor subtypes J. Biol. Chem. 274 1999 13462 13469
    • (1999) J. Biol. Chem. , vol.274 , pp. 13462-13469
    • Prezeau, L.1
  • 48
    • 0035117587 scopus 로고    scopus 로고
    • (B) receptors and members of the 14-3-3 family of signaling proteins
    • (B) receptors and members of the 14-3-3 family of signaling proteins Mol. Cell. Neurosci. 17 2001 317 328
    • (2001) Mol. Cell. Neurosci. , vol.17 , pp. 317-328
    • Couve, A.1
  • 49
    • 0037451701 scopus 로고    scopus 로고
    • Interaction of the parathyroid hormone receptor with the 14-3-3 protein
    • H. Tazawa Interaction of the parathyroid hormone receptor with the 14-3-3 protein Biochim. Biophys. Acta 1620 2003 32 38
    • (2003) Biochim. Biophys. Acta , vol.1620 , pp. 32-38
    • Tazawa, H.1
  • 50
    • 0028143610 scopus 로고
    • The cyclophilin homolog NinaA functions as a chaperone, forming a stable complex in vivo with its protein target rhodopsin
    • E.K. Baker The cyclophilin homolog NinaA functions as a chaperone, forming a stable complex in vivo with its protein target rhodopsin EMBO J. 13 1994 4886 4895
    • (1994) EMBO J. , vol.13 , pp. 4886-4895
    • Baker, E.K.1
  • 51
    • 0038819926 scopus 로고    scopus 로고
    • The chaperone environment at the cytoplasmic face of the endoplasmic reticulum can modulate rhodopsin processing and inclusion formation
    • J.P. Chapple, and M.E. Cheetham The chaperone environment at the cytoplasmic face of the endoplasmic reticulum can modulate rhodopsin processing and inclusion formation J. Biol. Chem. 278 2003 19087 19094
    • (2003) J. Biol. Chem. , vol.278 , pp. 19087-19094
    • Chapple, J.P.1    Cheetham, M.E.2
  • 52
    • 0035011489 scopus 로고    scopus 로고
    • Regulation of transport of the dopamine D1 receptor by a new membrane- associated ER protein
    • J.C. Bermak Regulation of transport of the dopamine D1 receptor by a new membrane- associated ER protein Nat. Cell Biol. 3 2001 492 498
    • (2001) Nat. Cell Biol. , vol.3 , pp. 492-498
    • Bermak, J.C.1
  • 53
    • 0032574982 scopus 로고    scopus 로고
    • RAMPs regulate the transport and ligand specificity of the calcitonin- receptor-like receptor
    • L.M. McLatchie RAMPs regulate the transport and ligand specificity of the calcitonin- receptor-like receptor Nature 393 1998 333 339
    • (1998) Nature , vol.393 , pp. 333-339
    • McLatchie, L.M.1
  • 54
    • 0035100661 scopus 로고    scopus 로고
    • Receptor activity modifying proteins
    • P.M. Sexton Receptor activity modifying proteins Cell. Signal. 13 2001 73 83
    • (2001) Cell. Signal. , vol.13 , pp. 73-83
    • Sexton, P.M.1
  • 55
    • 0037423953 scopus 로고    scopus 로고
    • Functional expression of murine V2R pheromone receptors involves selective association with the M10 and M1 families of MHC class Ib molecules
    • J. Loconto Functional expression of murine V2R pheromone receptors involves selective association with the M10 and M1 families of MHC class Ib molecules Cell 112 2003 607 618
    • (2003) Cell , vol.112 , pp. 607-618
    • Loconto, J.1
  • 56
    • 0035831477 scopus 로고    scopus 로고
    • Olfactory receptor trafficking involves conserved regulatory steps
    • A.A. Gimelbrant Olfactory receptor trafficking involves conserved regulatory steps J. Biol. Chem. 276 2001 7285 7290
    • (2001) J. Biol. Chem. , vol.276 , pp. 7285-7290
    • Gimelbrant, A.A.1
  • 57
    • 0032076851 scopus 로고    scopus 로고
    • Odorant receptor localization to olfactory cilia is mediated by ODR-4, a novel membrane-associated protein
    • N.D. Dwyer Odorant receptor localization to olfactory cilia is mediated by ODR-4, a novel membrane-associated protein Cell 93 1998 455 466
    • (1998) Cell , vol.93 , pp. 455-466
    • Dwyer, N.D.1
  • 58
    • 0033543572 scopus 로고    scopus 로고
    • Involvement of the amino terminus of the B(2) receptor in agonist- induced receptor dimerization
    • S. AbdAlla Involvement of the amino terminus of the B(2) receptor in agonist- induced receptor dimerization J. Biol. Chem. 274 1999 26079 26084
    • (1999) J. Biol. Chem. , vol.274 , pp. 26079-26084
    • Abdalla, S.1
  • 59
    • 0033616765 scopus 로고    scopus 로고
    • The chemokine monocyte chemoattractant protein-1 induces functional responses through dimerization of its receptor CCR2
    • J.M. Rodriguez-Frade The chemokine monocyte chemoattractant protein-1 induces functional responses through dimerization of its receptor CCR2 Proc. Natl. Acad. Sci. U. S. A. 96 1999 3628 3633
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 3628-3633
    • Rodriguez-Frade, J.M.1
  • 60
    • 0034677745 scopus 로고    scopus 로고
    • Subtypes of the somatostatin receptor assemble as functional homo- and heterodimers
    • M. Rocheville Subtypes of the somatostatin receptor assemble as functional homo- and heterodimers J. Biol. Chem. 275 2000 7862 7869
    • (2000) J. Biol. Chem. , vol.275 , pp. 7862-7869
    • Rocheville, M.1
  • 61
    • 0034724420 scopus 로고    scopus 로고
    • HIV-1 infection through the CCR5 receptor is blocked by receptor dimerization
    • A.J. Vila-Coro HIV-1 infection through the CCR5 receptor is blocked by receptor dimerization Proc. Natl. Acad. Sci. U. S. A. 97 2000 3388 3393
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 3388-3393
    • Vila-Coro, A.J.1
  • 62
    • 0035002343 scopus 로고    scopus 로고
    • Binding of agonist but not antagonist leads to fluorescence resonance energy transfer between intrinsically fluorescent gonadotropin-releasing hormone receptors
    • R.D. Horvat Binding of agonist but not antagonist leads to fluorescence resonance energy transfer between intrinsically fluorescent gonadotropin- releasing hormone receptors Mol. Endocrinol. 15 2001 695 703
    • (2001) Mol. Endocrinol. , vol.15 , pp. 695-703
    • Horvat, R.D.1
  • 63
    • 1242276192 scopus 로고    scopus 로고
    • Roles of G-protein-coupled receptor dimerization
    • S. Terrillon, and M. Bouvier Roles of G-protein-coupled receptor dimerization EMBO Rep. 5 2004 30 34
    • (2004) EMBO Rep. , vol.5 , pp. 30-34
    • Terrillon, S.1    Bouvier, M.2
  • 64
    • 0038729670 scopus 로고    scopus 로고
    • Measurement of the millisecond activation switch of G protein-coupled receptors in living cells
    • J.P. Vilardaga Measurement of the millisecond activation switch of G protein-coupled receptors in living cells Nat. Biotechnol. 21 2003 807 812
    • (2003) Nat. Biotechnol. , vol.21 , pp. 807-812
    • Vilardaga, J.P.1
  • 65
    • 0034616021 scopus 로고    scopus 로고
    • Receptors for dopamine and somatostatin: Formation of hetero-oligomers with enhanced functional activity
    • M. Rocheville Receptors for dopamine and somatostatin: formation of hetero-oligomers with enhanced functional activity Science 288 2000 154 157
    • (2000) Science , vol.288 , pp. 154-157
    • Rocheville, M.1
  • 66
    • 0035918215 scopus 로고    scopus 로고
    • Constitutive and agonist-dependent homo-oligomerization of the thyrotropin-releasing hormone receptor. Detection in living cells using bioluminescence resonance energy transfer
    • K.M. Kroeger Constitutive and agonist-dependent homo-oligomerization of the thyrotropin-releasing hormone receptor. Detection in living cells using bioluminescence resonance energy transfer J. Biol. Chem. 276 2001 12736 12743
    • (2001) J. Biol. Chem. , vol.276 , pp. 12736-12743
    • Kroeger, K.M.1
  • 67
    • 0037022641 scopus 로고    scopus 로고
    • Ligand binding to somatostatin receptors induces receptor-specific oligomer formation in live cells
    • R.C. Patel Ligand binding to somatostatin receptors induces receptor-specific oligomer formation in live cells Proc. Natl. Acad. Sci. U. S. A. 99 2002 3294 3299
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 3294-3299
    • Patel, R.C.1
  • 68
    • 3342965731 scopus 로고    scopus 로고
    • Preferential formation of MT1/MT2 melatonin receptor heterodimers with distinct ligand interaction properties compared to MT2 homodimers
    • M.A. Ayoub Preferential formation of MT1/MT2 melatonin receptor heterodimers with distinct ligand interaction properties compared to MT2 homodimers Mol. Pharmacol. 66 2004 312 321
    • (2004) Mol. Pharmacol. , vol.66 , pp. 312-321
    • Ayoub, M.A.1
  • 69
    • 3142617997 scopus 로고    scopus 로고
    • Heterodimerization between beta 2- and beta 3-adrenergic receptors generates a beta -adrenergic signalling unit with distinct functional properties
    • A. Breit Heterodimerization between beta 2- and beta 3-adrenergic receptors generates a beta -adrenergic signalling unit with distinct functional properties J. Biol. Chem. 279 2004 28756 28765
    • (2004) J. Biol. Chem. , vol.279 , pp. 28756-28765
    • Breit, A.1
  • 70
    • 0034618268 scopus 로고    scopus 로고
    • AT1-receptor heterodimers show enhanced G-protein activation and altered receptor sequestration
    • S. AbdAlla AT1-receptor heterodimers show enhanced G-protein activation and altered receptor sequestration Nature 407 2000 94 98
    • (2000) Nature , vol.407 , pp. 94-98
    • Abdalla, S.1
  • 71
    • 0242460494 scopus 로고    scopus 로고
    • Metabotropic glutamate 1alpha and adenosine A1 receptors assemble into functionally interacting complexes
    • F. Ciruela Metabotropic glutamate 1alpha and adenosine A1 receptors assemble into functionally interacting complexes J. Biol. Chem. 276 2001 18345 18351
    • (2001) J. Biol. Chem. , vol.276 , pp. 18345-18351
    • Ciruela, F.1
  • 72
    • 0034785580 scopus 로고    scopus 로고
    • Increased AT(1) receptor heterodimers in preeclampsia mediate enhanced angiotensin II responsiveness
    • S. AbdAlla Increased AT(1) receptor heterodimers in preeclampsia mediate enhanced angiotensin II responsiveness Nat. Med. 7 2001 1003 1009
    • (2001) Nat. Med. , vol.7 , pp. 1003-1009
    • Abdalla, S.1
  • 73
    • 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 (BRET): Hetero-oligomers between receptor subtypes form more efficiently than between less closely related sequences
    • D. Ramsay Homo- and hetero-oligomeric interactions between G-protein-coupled receptors in living cells monitored by two variants of bioluminescence resonance energy transfer (BRET): hetero-oligomers between receptor subtypes form more efficiently than between less closely related sequences Biochem. J. 365 2002 429 440
    • (2002) Biochem. J. , vol.365 , pp. 429-440
    • Ramsay, D.1
  • 74
    • 0037160105 scopus 로고    scopus 로고
    • Quantitative assessment of beta 1 and beta 2-adrenergic receptor homo and hetero-dimerization by bioluminescence resonance energy transfer
    • J.F. Mercier Quantitative assessment of beta 1 and beta 2-adrenergic receptor homo and hetero-dimerization by bioluminescence resonance energy transfer J. Biol. Chem. 277 2002 44925 44931
    • (2002) J. Biol. Chem. , vol.277 , pp. 44925-44931
    • Mercier, J.F.1
  • 75
    • 0033600911 scopus 로고    scopus 로고
    • Identification of the cysteine residues in the amino-terminal extracellular domain of the human Ca(2+) receptor critical for dimerization. Implications for function of monomeric Ca(2+) receptor
    • K. Ray Identification of the cysteine residues in the amino-terminal extracellular domain of the human Ca(2+) receptor critical for dimerization. Implications for function of monomeric Ca(2+) receptor J. Biol. Chem. 274 1999 27642 27650
    • (1999) J. Biol. Chem. , vol.274 , pp. 27642-27650
    • Ray, K.1
  • 76
    • 0034718925 scopus 로고    scopus 로고
    • Structural basis of glutamate recognition by a dimeric metabotropic glutamate receptor
    • N. Kunishima Structural basis of glutamate recognition by a dimeric metabotropic glutamate receptor Nature 407 2000 971 977
    • (2000) Nature , vol.407 , pp. 971-977
    • Kunishima, N.1
  • 77
    • 0035895907 scopus 로고    scopus 로고
    • The extracellular calcium-sensing receptor dimerizes through multiple types of intermolecular interactions
    • Z. Zhang The extracellular calcium-sensing receptor dimerizes through multiple types of intermolecular interactions J. Biol. Chem. 276 2001 5316 5322
    • (2001) J. Biol. Chem. , vol.276 , pp. 5316-5322
    • Zhang, Z.1
  • 78
    • 0035866088 scopus 로고    scopus 로고
    • (B) receptors
    • (B) receptors J. Neurosci. 21 2001 1189 1202
    • (2001) J. Neurosci. , vol.21 , pp. 1189-1202
    • Pagano, A.1
  • 79
    • 0030760634 scopus 로고    scopus 로고
    • Dimerization of the delta opioid receptor: Implication for a role in receptor internalization
    • S. Cvejic, and L.A. Devi Dimerization of the delta opioid receptor: implication for a role in receptor internalization J. Biol. Chem. 272 1997 26959 26964
    • (1997) J. Biol. Chem. , vol.272 , pp. 26959-26964
    • Cvejic, S.1    Devi, L.A.2
  • 80
    • 10744223537 scopus 로고    scopus 로고
    • Identification of amino acid residues crucial for chemokine receptor dimerization
    • P. Hernanz-Falcon Identification of amino acid residues crucial for chemokine receptor dimerization Nat. Immunol. 5 2004 216 223
    • (2004) Nat. Immunol. , vol.5 , pp. 216-223
    • Hernanz-Falcon, P.1
  • 81
    • 0141431029 scopus 로고    scopus 로고
    • D2 dopamine receptor homodimerization is mediated by multiple sites of interaction, including an intermolecular interaction involving transmembrane domain 4
    • S.P. Lee D2 dopamine receptor homodimerization is mediated by multiple sites of interaction, including an intermolecular interaction involving transmembrane domain 4 Biochemistry 42 2003 11023 11031
    • (2003) Biochemistry , vol.42 , pp. 11023-11031
    • Lee, S.P.1
  • 82
    • 6944234943 scopus 로고    scopus 로고
    • Multiple interactions between transmembrane helices generate the oligomeric {alpha}1b-adrenoceptor
    • J.J. Carrillo Multiple interactions between transmembrane helices generate the oligomeric {alpha}1b-adrenoceptor Mol. Pharmacol. 66 2004 1123 1137
    • (2004) Mol. Pharmacol. , vol.66 , pp. 1123-1137
    • Carrillo, J.J.1
  • 83
    • 0038576278 scopus 로고    scopus 로고
    • The fourth transmembrane segment forms the interface of the dopamine D2 receptor homodimer
    • W. Guo The fourth transmembrane segment forms the interface of the dopamine D2 receptor homodimer J. Biol. Chem. 278 2003 4385 4388
    • (2003) J. Biol. Chem. , vol.278 , pp. 4385-4388
    • Guo, W.1
  • 84
    • 0035664761 scopus 로고    scopus 로고
    • Lipid-facing correlated mutations and dimerization in G-protein coupled receptors
    • P.R. Gouldson Lipid-facing correlated mutations and dimerization in G-protein coupled receptors Protein Eng. 14 2001 759 767
    • (2001) Protein Eng. , vol.14 , pp. 759-767
    • Gouldson, P.R.1
  • 85
    • 0035924184 scopus 로고    scopus 로고
    • Dimerization of G-protein-coupled receptors
    • M.K. Dean Dimerization of G-protein-coupled receptors J. Med. Chem. 44 2001 4595 4614
    • (2001) J. Med. Chem. , vol.44 , pp. 4595-4614
    • Dean, M.K.1
  • 86
    • 0036878162 scopus 로고    scopus 로고
    • Prediction of heterodimerization interfaces of G-protein coupled receptors with a new subtractive correlated mutation method
    • M. Filizola Prediction of heterodimerization interfaces of G-protein coupled receptors with a new subtractive correlated mutation method Protein Eng. 15 2002 881 885
    • (2002) Protein Eng. , vol.15 , pp. 881-885
    • Filizola, M.1
  • 87
    • 0033578005 scopus 로고    scopus 로고
    • G-protein-coupled receptor heterodimerization modulates receptor function
    • B.A. Jordan, and L.A. Devi G-protein-coupled receptor heterodimerization modulates receptor function Nature 399 1999 697 700
    • (1999) Nature , vol.399 , pp. 697-700
    • Jordan, B.A.1    Devi, L.A.2
  • 88
    • 0036732940 scopus 로고    scopus 로고
    • Membrane trafficking of heterotrimeric G proteins via the endoplasmic reticulum and Golgi
    • D. Michaelson Membrane trafficking of heterotrimeric G proteins via the endoplasmic reticulum and Golgi Mol. Biol. Cell 13 2002 3294 3302
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3294-3302
    • Michaelson, D.1
  • 89
    • 0038607927 scopus 로고    scopus 로고
    • Heterotrimer formation, together with isoprenylation, is required for plasma membrane targeting of Gbetagamma
    • S. Takida, and P.B. Wedegaertner Heterotrimer formation, together with isoprenylation, is required for plasma membrane targeting of Gbetagamma J. Biol. Chem. 278 2003 17284 17290
    • (2003) J. Biol. Chem. , vol.278 , pp. 17284-17290
    • Takida, S.1    Wedegaertner, P.B.2
  • 90
    • 2942617262 scopus 로고    scopus 로고
    • Exocytic pathway-independent plasma membrane targeting of heterotrimeric G proteins
    • S. Takida, and P.B. Wedegaertner Exocytic pathway-independent plasma membrane targeting of heterotrimeric G proteins FEBS Lett. 567 2004 209 213
    • (2004) FEBS Lett. , vol.567 , pp. 209-213
    • Takida, S.1    Wedegaertner, P.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.