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Volumn 287, Issue 7, 2012, Pages 5008-5020

Cys-27 variant of human δ-opioid receptor modulates maturation and cell surface delivery of Phe-27 variant via heteromerization

Author keywords

[No Author keywords available]

Indexed keywords

BIOLUMINESCENCE RESONANCE ENERGY TRANSFER; CELL SURFACE EXPRESSION; CELL SURFACES; CO-IMMUNOPRECIPITATIONS; DOMINANT NEGATIVE; ENDOPLASMIC RETICULUM; G PROTEIN COUPLED RECEPTORS; HEK-293; LIVING CELL; METABOLIC LABELING; NALTREXONE; NEUROBLASTOMA CELLS; OPIOID RECEPTORS; SECRETORY PATHWAYS; WESTERN BLOTTING;

EID: 84856866923     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.305656     Document Type: Article
Times cited : (16)

References (52)
  • 2
    • 0033885478 scopus 로고    scopus 로고
    • Variant detection at the δ opioid receptor (OPRD1) locus and population genetics of a novel variant affecting protein sequence
    • DOI 10.1007/s004390050016
    • Gelernter, J., and Kranzler, H. R. (2000) Variant detection at the δ-opioid receptor (OPRD1) locus and population genetics of a novel variant affecting protein sequence. Hum. Genet 107, 86-88 (Pubitemid 30598953)
    • (2000) Human Genetics , vol.107 , Issue.1 , pp. 86-88
    • Gelernter, J.1    Kranzler, H.R.2
  • 4
    • 58149187864 scopus 로고    scopus 로고
    • Phe27Cys polymorphism alters the maturation and subcellular localization of the human δ-opioid receptor
    • Leskelä, T. T., Markkanen, P. M., Alahuhta, I. A., Tuusa, J. T., and Petäjä- Repo, U. E. (2009) Phe27Cys polymorphism alters the maturation and subcellular localization of the human δ-opioid receptor. Traffic 10, 116-129
    • (2009) Traffic , vol.10 , pp. 116-129
    • Leskelä, T.T.1    Markkanen, P.M.2    Alahuhta, I.A.3    Tuusa, J.T.4    Petäjä- Repo, U.E.5
  • 5
    • 0037007201 scopus 로고    scopus 로고
    • Ligands act as pharmacological chaperones and increase the efficiency of δ opioid receptor maturation
    • DOI 10.1093/emboj/21.7.1628
    • Petäjä-Repo, U. E., Hogue, M., Bhalla, S., Laperrière, A., Morello, J. P., and Bouvier, M. (2002) Ligands act as pharmacological chaperones and increase the efficiency of δ-opioid receptor maturation. EMBO J. 21, 1628-1637 (Pubitemid 34614619)
    • (2002) EMBO Journal , vol.21 , Issue.7 , pp. 1628-1637
    • Petaja-Repo, U.E.1    Hogue, M.2    Bhalla, S.3    Laperriere, A.4    Morello, J.-P.5    Bouvier, M.6
  • 6
    • 34548159460 scopus 로고    scopus 로고
    • Opioid receptor pharmacological chaperones act by binding and stabilizing newly synthesized receptors in the endoplasmic reticulum
    • Leskelä, T. T., Markkanen, P. M., Pietilä, E. M., Tuusa, J. T., and Petäjä- Repo, U. E. (2007) Opioid receptor pharmacological chaperones act by binding and stabilizing newly synthesized receptors in the endoplasmic reticulum. J. Biol. Chem. 282, 23171-23183
    • (2007) J. Biol. Chem. , vol.282 , pp. 23171-23183
    • Leskelä, T.T.1    Markkanen, P.M.2    Pietilä, E.M.3    Tuusa, J.T.4    Petäjä- Repo, U.E.5
  • 7
    • 0030760634 scopus 로고    scopus 로고
    • Dimerization of the δ opioid receptor: Implication for a role in receptor internalization
    • DOI 10.1074/jbc.272.43.26959
    • Cvejic, S., and Devi, L. A. (1997) Dimerization of the δ-opioid receptor. Implication for a role in receptor internalization. J. Biol. Chem. 272, 26959-26964 (Pubitemid 27452648)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.43 , pp. 26959-26964
    • Cvejic, S.1    Devi, L.A.2
  • 8
    • 0033578005 scopus 로고    scopus 로고
    • G-protein-coupled receptor heterodimerization modulates receptor function
    • DOI 10.1038/21441
    • Jordan, B. A., and Devi, L. A. (1999) G protein-coupled receptor heterodimerization modulates receptor function. Nature 399, 697-700 (Pubitemid 29289066)
    • (1999) Nature , vol.399 , Issue.6737 , pp. 697-700
    • Jordan, B.A.1    Devi, L.A.2
  • 9
    • 0035958023 scopus 로고    scopus 로고
    • Monitoring receptor oligomerization using time-resolved fluorescence resonance energy transfer and bioluminescence resonance energy transfer. The human δ-opioid receptor displays constitutive oligomerization at the cell surface, which is not regulated by receptor occupancy
    • McVey, M., Ramsay, D., Kellett, E., Rees, S., Wilson, S., Pope, A. J., and Milligan, G. (2001) Monitoring receptor oligomerization using time-resolved fluorescence resonance energy transfer and bioluminescence resonance energy transfer. The human δ-opioid receptor displays constitutive oligomerization at the cell surface, which is not regulated by receptor occupancy. 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
  • 10
    • 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
    • DOI 10.1042/BJ20020251
    • Ramsay, D., Kellett, E., McVey, M., Rees, S., and 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 (BRET). Hetero-oligomers between receptor subtypes form more efficiently than between less closely related sequences. Biochem. J. 365, 429-440 (Pubitemid 36135314)
    • (2002) Biochemical Journal , vol.365 , Issue.2 , pp. 429-440
    • Ramsay, D.1    Kellett, E.2    McVey, M.3    Rees, S.4    Milligan, G.5
  • 11
    • 21144439867 scopus 로고    scopus 로고
    • Opioid receptor homo- and heterodimerization in living cells by quantitative bioluminescence resonance energy transfer
    • DOI 10.1124/mol.104.010272
    • Wang, D., Sun, X., Bohn, L. M., and Sadée, W. (2005) Opioid receptor homo- and heterodimerization in living cells by quantitative bioluminescence resonance energy transfer. Mol. Pharmacol. 67, 2173-2184 (Pubitemid 41007796)
    • (2005) Molecular Pharmacology , vol.67 , Issue.6 , pp. 2173-2184
    • Wang, D.1    Sun, X.2    Bohn, L.M.3    Sadee, W.4
  • 12
    • 25144488303 scopus 로고    scopus 로고
    • Interaction of bivalent ligand KDN21 with heterodimeric δ-κ-opioid receptors in human embryonic kidney 293 cells
    • Xie, Z., Bhushan, R. G., Daniels, D. J., and Portoghese, P. S. (2005) Interaction of bivalent ligand KDN21 with heterodimeric δ-κ-opioid receptors in human embryonic kidney 293 cells. Mol. Pharmacol. 68, 1079 -1086
    • (2005) Mol. Pharmacol. , vol.68 , pp. 1079-1086
    • Xie, Z.1    Bhushan, R.G.2    Daniels, D.J.3    Portoghese, P.S.4
  • 14
    • 33746256433 scopus 로고    scopus 로고
    • Simultaneous activation of the δ opioid receptor (δOR)/sensory neuron-specific receptor-4 (SNSR-4) hetero-oligomer by the mixed bivalent agonist bovine adrenal medulla peptide 22 activates SNSR-4 but inhibits δOR signaling
    • DOI 10.1124/mol.106.022897
    • Breit, A., Gagnidze, K., Devi, L. A., Lagacé, M., and Bouvier, M. (2006) Simultaneous activation of the δ-opioid receptor (δ-OR)/sensory neuron-specific receptor-4 (SNSR-4) hetero-oligomer by the mixed bivalent agonist bovine adrenal medulla peptide 22 activates SNSR-4 but inhibits δOR signaling. Mol. Pharmacol. 70, 686-696 (Pubitemid 44092329)
    • (2006) Molecular Pharmacology , vol.70 , Issue.2 , pp. 686-696
    • Breit, A.1    Gagnidze, K.2    Devi, L.A.3    Lagace, M.4    Bouvier, M.5
  • 15
    • 36048947671 scopus 로고    scopus 로고
    • Trafficking of preassembled opioid μ-δ heterooligomer-Gz signaling complexes to the plasma membrane: Coregulation by agonists
    • DOI 10.1021/bi701436w
    • Hasbi, A., Nguyen, T., Fan, T., Cheng, R., Rashid, A., Alijaniaram, M., Rasenick, M. M., O'Dowd, B. F., and George, S. R. (2007) Trafficking of preassembled opioid μ-δ heterooligomer-Gz signaling complexes to the plasma membrane. Coregulation by agonists. Biochemistry 46, 12997-13009 (Pubitemid 350086219)
    • (2007) Biochemistry , vol.46 , Issue.45 , pp. 12997-13009
    • Hasbi, A.1    Nguyen, T.2    Fan, T.3    Cheng, R.4    Rashid, A.5    Alijaniaram, M.6    Rasenick, M.M.7    O'Dowd, B.F.8    George, S.R.9
  • 16
    • 44449175613 scopus 로고    scopus 로고
    • CXCR2 chemokine receptor antagonism enhances DOP opioid receptor function via allosteric regulation of the CXCR2-DOP receptor heterodimer
    • DOI 10.1042/BJ20071689
    • Parenty, G., Appelbe, S., and Milligan, G. (2008) CXCR2 chemokine receptor antagonism enhances DOP opioid receptor function via allosteric regulation of the CXCR2-DOP receptor heterodimer. Biochem. J. 412, 245-256 (Pubitemid 351758230)
    • (2008) Biochemical Journal , vol.412 , Issue.2 , pp. 245-256
    • Parenty, G.1    Appelbe, S.2    Milligan, G.3
  • 18
    • 72449123327 scopus 로고    scopus 로고
    • Opioid receptor heteromer-specific trafficking and pharmacology
    • van Rijn, R. M., Whistler, J. L., and Waldhoer, M. (2010) Opioid receptor heteromer-specific trafficking and pharmacology. Curr. Opin. Pharmacol. 10, 73-79
    • (2010) Curr. Opin. Pharmacol. , vol.10 , pp. 73-79
    • Van Rijn, R.M.1    Whistler, J.L.2    Waldhoer, M.3
  • 19
    • 79551485761 scopus 로고    scopus 로고
    • Exploring a role for heteromerization in GPCR signalling specificity
    • Rozenfeld, R., and Devi, L. A. (2011) Exploring a role for heteromerization in GPCR signalling specificity. Biochem. J. 433, 11-18
    • (2011) Biochem. J. , vol.433 , pp. 11-18
    • Rozenfeld, R.1    Devi, L.A.2
  • 21
    • 14644387575 scopus 로고    scopus 로고
    • Emerging role of homo- and heterodimerization in G-protein-coupled receptor biosynthesis and maturation
    • DOI 10.1016/j.tips.2005.01.004
    • Bulenger, S., Marullo, S., and Bouvier, M. (2005) Emerging role of homo- and heterodimerization in G protein-coupled receptor biosynthesis and maturation. Trends Pharmacol. Sci. 26, 131-137 (Pubitemid 40313592)
    • (2005) Trends in Pharmacological Sciences , vol.26 , Issue.3 , pp. 131-137
    • Bulenger, S.1    Marullo, S.2    Bouvier, M.3
  • 22
    • 12544250742 scopus 로고    scopus 로고
    • Suppression of wild-type rhodopsin maturation by mutants linked to autosomal dominant retinitis pigmentosa
    • Rajan, R. S., and Kopito, R. R. (2005) Suppression of wild-type rhodopsin maturation by mutants linked to autosomal dominant retinitis pigmentosa. J. Biol. Chem. 280, 1284-1291
    • (2005) J. Biol. Chem. , vol.280 , pp. 1284-1291
    • Rajan, R.S.1    Kopito, R.R.2
  • 23
    • 0033798153 scopus 로고    scopus 로고
    • The dopamine D3 receptor interacts with itself and the truncated D3 splice variant d3nf. D3-D3nf interaction causes mislocalization of D3 receptors
    • Karpa, K. D., Lin, R., Kabbani, N., and Levenson, R. (2000) The dopamine D3 receptor interacts with itself and the truncated D3 splice variant d3nf. D3-D3nf interaction causes mislocalization of D3 receptors. Mol. Pharmacol. 58, 677-683
    • (2000) Mol. Pharmacol. , vol.58 , pp. 677-683
    • Karpa, K.D.1    Lin, R.2    Kabbani, N.3    Levenson, R.4
  • 24
    • 0033924207 scopus 로고    scopus 로고
    • Inhibition of cell surface expression by mutant receptors demonstrates that D2 dopamine receptors exist as oligomers in the cell
    • Lee, S. P., O'Dowd, B. F., Ng, G. Y., Varghese, G., Akil, H., Mansour, A., Nguyen, T., and George, S. R. (2000) Inhibition of cell surface expression by mutant receptors demonstrates that D2 dopamine receptors exist as oligomers in the cell. Mol. Pharmacol. 58, 120-128 (Pubitemid 30452534)
    • (2000) Molecular Pharmacology , vol.58 , Issue.1 , pp. 120-128
    • Lee, S.P.1    O'Dowd, B.F.2    Ng, G.Y.K.3    Varghese, G.4    Akil, H.5    Mansour, A.6    Nguyen, T.7    George, S.R.8
  • 25
    • 0031446639 scopus 로고    scopus 로고
    • Inhibition of gonadotropin releasing hormone receptor signaling by expression of a splice variant of the human receptor
    • DOI 10.1210/me.11.9.1305
    • Grosse, R., Schöneberg, T., Schultz, G., and Gudermann, T. (1997) Inhibition of gonadotropin-releasing hormone receptor signaling by expression of a splice variant of the human receptor. Mol. Endocrinol. 11, 1305-1318 (Pubitemid 28041337)
    • (1997) Molecular Endocrinology , vol.11 , Issue.9 , pp. 1305-1318
    • Grosse, R.1    Schoneberg, T.2    Schultz, G.3    Gudermann, T.4
  • 26
    • 3042800569 scopus 로고    scopus 로고
    • Human loss-of-function gonadotropin-releasing hormone receptor mutants retain wild-type receptors in the endoplasmic reticulum: Molecular basis of the dominant-negative effect
    • DOI 10.1210/me.2004-0091
    • Brothers, S. P., Cornea, A., Janovick, J. A., and Conn, P. M. (2004) Human loss-of-function gonadotropin-releasing hormone receptor mutants retain wild-type receptors in the endoplasmic reticulum. Molecular basis of the dominant-negative effect. Mol. Endocrinol. 18, 1787-1797 (Pubitemid 38859584)
    • (2004) Molecular Endocrinology , vol.18 , Issue.7 , pp. 1787-1797
    • Brothers, S.P.1    Cornea, A.2    Janovick, J.A.3    Conn, P.M.4
  • 28
    • 34548385653 scopus 로고    scopus 로고
    • Receptor function, dominant negative activity and phenotype correlations for MC1R variant alleles
    • DOI 10.1093/hmg/ddm177
    • Beaumont, K. A., Shekar, S. N., Shekar, S. L., Newton, R. A., James, M. R., Stow, J. L., Duffy, D. L., and Sturm, R. A. (2007) Receptor function, dominant negative activity, and phenotype correlations for MC1R variant alleles. Hum. Mol. Genet 16, 2249-2260 (Pubitemid 47354907)
    • (2007) Human Molecular Genetics , vol.16 , Issue.18 , pp. 2249-2260
    • Beaumont, K.A.1    Shekar, S.L.2    Newton, R.A.3    James, M.R.4    Stow, J.L.5    Duffy, D.L.6    Sturm, R.A.7
  • 29
    • 27544481186 scopus 로고    scopus 로고
    • Intracellular entrapment of wild-type TSH receptor by oligomerization with mutants linked to dominant TSH resistance
    • DOI 10.1093/hmg/ddi329
    • Calebiro, D., de Filippis, T., Lucchi, S., Covino, C., Panigone, S., Beck-Peccoz, P., Dunlap, D., and Persani, L. (2005) Intracellular entrapment of wild-type TSH receptor by oligomerization with mutants linked to dominant TSH resistance. Hum. Mol. Genet 14, 2991-3002 (Pubitemid 41535464)
    • (2005) Human Molecular Genetics , vol.14 , Issue.20 , pp. 2991-3002
    • Calebiro, D.1    De Filippis, T.2    Lucchi, S.3    Covino, C.4    Panigone, S.5    Beck-Peccoz, P.6    Dunlap, D.7    Persani, L.8
  • 30
    • 33744923745 scopus 로고    scopus 로고
    • Luteinizing hormone receptor ectodomain splice variant misroutes the full-length receptor into a subcompartment of the endoplasmic reticulum
    • DOI 10.1091/mbc.E05-09-0875
    • Apaja, P. M., Tuusa, J. T., Pietilä, E. M., Rajaniemi, H. J., and Petäjä-Repo, U. E. (2006) Luteinizing hormone receptor ectodomain splice variant misroutes the full-length receptor into a subcompartment of the endoplasmic reticulum. Mol. Biol. Cell 17, 2243-2255 (Pubitemid 44011740)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.5 , pp. 2243-2255
    • Apaja, P.M.1    Tuusa, J.T.2    Pietila, E.M.3    Rajaniemi, H.J.4    Petaja-Repo, U.E.5
  • 31
    • 0030712312 scopus 로고    scopus 로고
    • Mechanism of transdominant inhibition of CCR5-mediated HIV-1 infection by ccr5delta32
    • DOI 10.1074/jbc.272.49.30603
    • Benkirane, M., Jin, D. Y., Chun, R. F., Koup, R. A., and Jeang, K. T. (1997) Mechanism of transdominant inhibition of CCR5-mediated HIV-1 infection by ccr5delta32. J. Biol. Chem. 272, 30603-30606 (Pubitemid 27527488)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.49 , pp. 30603-30606
    • Benkirane, M.1    Jin, D.-Y.2    Chun, R.F.3    Koup, R.A.4    Jeang, K.-T.5
  • 32
    • 0035108034 scopus 로고    scopus 로고
    • Naturally occurring deletional mutation in the C-terminal cytoplasmic tail of CCR5 affects surface trafficking of CCR5
    • DOI 10.1128/JVI.75.7.3462-3468.2001
    • Shioda, T., Nakayama, E. E., Tanaka, Y., Xin, X., Liu, H., Kawana-Tachikawa, A., Kato, A., Sakai, Y., Nagai, Y., and Iwamoto, A. (2001) Naturally occurring deletional mutation in the C-terminal cytoplasmic tail of CCR5 affects surface trafficking of CCR5. J. Virol. 75, 3462-3468 (Pubitemid 32225909)
    • (2001) Journal of Virology , vol.75 , Issue.7 , pp. 3462-3468
    • Shioda, T.1    Nakayama, E.E.2    Tanaka, Y.3    Xin, X.4    Liu, H.5    Kawana-Tachikawa, A.6    Kato, A.7    Sakai, Y.8    Nagai, Y.9    Iwamoto, A.10
  • 33
    • 0032506160 scopus 로고    scopus 로고
    • Truncated V2 vasopressin receptors as negative regulators of wild-type V2 receptor function
    • DOI 10.1021/bi981162z
    • Zhu, X., and Wess, J. (1998) Truncated V2 vasopressin receptors as negative regulators of wild-type V2 receptor function. Biochemistry 37, 15773-15784 (Pubitemid 28524748)
    • (1998) Biochemistry , vol.37 , Issue.45 , pp. 15773-15784
    • Zhu, X.1    Wess, J.2
  • 34
    • 2442597256 scopus 로고    scopus 로고
    • 1D-Adrenergic Receptors
    • DOI 10.1074/jbc.M314014200
    • Hague, C., Uberti, M. A., Chen, Z., Hall, R. A., and Minneman, K. P. (2004) Cell surface expression of α1D-adrenergic receptors is controlled by heterodimerization with α1B-adrenergic receptors. J. Biol. Chem. 279, 15541-15549 (Pubitemid 38618955)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.15 , pp. 15541-15549
    • Hague, C.1    Uberti, M.A.2    Chen, Z.3    Hall, R.A.4    Minneman, K.P.5
  • 35
    • 58249090329 scopus 로고    scopus 로고
    • Cell surface delivery and structural reorganization by pharmacological chaperones of an oligomerization-defective α (1b)-adrenoceptor mutant demonstrates membrane targeting of GPCR oligomers
    • Canals, M., Lopez-Gimenez, J. F., and Milligan, G. (2009) Cell surface delivery and structural reorganization by pharmacological chaperones of an oligomerization-defective α (1b)-adrenoceptor mutant demonstrates membrane targeting of GPCR oligomers. Biochem. J. 417, 161-172
    • (2009) Biochem. J. , vol.417 , pp. 161-172
    • Canals, M.1    Lopez-Gimenez, J.F.2    Milligan, G.3
  • 36
    • 67649951498 scopus 로고    scopus 로고
    • Functional rescue of β-adrenoceptor dimerization and trafficking by pharmacological chaperones
    • Kobayashi, H., Ogawa, K., Yao, R., Lichtarge, O., and Bouvier, M. (2009) Functional rescue of β-adrenoceptor dimerization and trafficking by pharmacological chaperones. Traffic 10, 1019-1033
    • (2009) Traffic , vol.10 , pp. 1019-1033
    • Kobayashi, H.1    Ogawa, K.2    Yao, R.3    Lichtarge, O.4    Bouvier, M.5
  • 37
    • 15744401602 scopus 로고    scopus 로고
    • Heterodimerization of μ- and δ-opioid receptors occurs at the cell surface only and requires receptor-G protein interactions
    • DOI 10.1074/jbc.M500171200
    • Law, P. Y., Erickson-Herbrandson, L. J., Zha, Q. Q., Solberg, J., Chu, J., Sarre, A., and Loh, H. H. (2005) Heterodimerization of μ- and δ-opioid receptors occurs at the cell surface only and requires receptor-G protein interactions. J. Biol. Chem. 280, 11152-11164 (Pubitemid 40418422)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.12 , pp. 11152-11164
    • Law, P.-Y.1    Erickson-Herbrandson, L.J.2    Zha, Q.Q.3    Solberg, J.4    Chu, J.5    Sarre, A.6    Loh, H.H.7
  • 38
    • 22544435246 scopus 로고    scopus 로고
    • Inefficient maturation of the rat luteinizing hormone receptor. A putative way to regulate receptor numbers at the cell surface
    • Pietilä, E. M., Tuusa, J. T., Apaja, P. M., Aatsinki, J. T., Hakalahti, A. E., Rajaniemi, H. J., and Petäjä-Repo, U. E. (2005) Inefficient maturation of the rat luteinizing hormone receptor. A putative way to regulate receptor numbers at the cell surface. J. Biol. Chem. 280, 26622-26629
    • (2005) J. Biol. Chem. , vol.280 , pp. 26622-26629
    • Pietilä, E.M.1    Tuusa, J.T.2    Apaja, P.M.3    Aatsinki, J.T.4    Hakalahti, A.E.5    Rajaniemi, H.J.6    Petäjä-Repo, U.E.7
  • 39
    • 77953548554 scopus 로고    scopus 로고
    • Human δ-opioid receptor biogenesis is regulated via interactions with SERCA2b and calnexin
    • Tuusa, J. T., Leskelä, T. T., and Petäjä-Repo, U. E. (2010) Human δ-opioid receptor biogenesis is regulated via interactions with SERCA2b and calnexin. FEBS J. 277, 2815-2829
    • (2010) FEBS J. , vol.277 , pp. 2815-2829
    • Tuusa, J.T.1    Leskelä, T.T.2    Petäjä-Repo, U.E.3
  • 40
    • 0036138908 scopus 로고    scopus 로고
    • A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications
    • DOI 10.1038/nbt0102-87
    • Nagai, T., Ibata, K., Park, E. S., Kubota, M., Mikoshiba, K., and Miyawaki, A. (2002) A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications. Nat. Biotechnol. 20, 87-90 (Pubitemid 34044921)
    • (2002) Nature Biotechnology , vol.20 , Issue.1 , pp. 87-90
    • Nagai, T.1    Ibata, K.2    Park, E.S.3    Kubota, M.4    Mikoshiba, K.5    Miyawaki, A.6
  • 42
    • 0035830863 scopus 로고    scopus 로고
    • Newly synthesized human δ-opioid receptors retained in the endoplasmic reticulum are retrotranslocated to the cytosol, deglycosylated, ubiquitinated, and degraded by the proteasome
    • Petaja-Repo, U. E., Hogue, M., Laperriere, A., Bhalla, S., Walker, P., and Bouvier, M. (2001) Newly synthesized human δ-opioid receptors retained in the endoplasmic reticulum are retrotranslocated to the cytosol, deglycosylated, ubiquitinated, and degraded by the proteasome. J. Biol. Chem. 276, 4416-4423
    • (2001) J. Biol. Chem. , vol.276 , pp. 4416-4423
    • Petaja-Repo, U.E.1    Hogue, M.2    Laperriere, A.3    Bhalla, S.4    Walker, P.5    Bouvier, M.6
  • 43
    • 33744943821 scopus 로고    scopus 로고
    • Distinct subcellular localization for constitutive and agonist-modulated palmitoylation of the human δ opioid receptor
    • DOI 10.1074/jbc.M602267200
    • Petäjä-Repo, U. E., Hogue, M., Leskelä, T. T., Markkanen, P. M., Tuusa, J. T., and Bouvier, M. (2006) Distinct subcellular localization for constitutive and agonist-modulated palmitoylation of the human δ-opioid receptor. J. Biol. Chem. 281, 15780-15789 (Pubitemid 43848468)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.23 , pp. 15780-15789
    • Petaja-Repo, U.E.1    Hogue, M.2    Leskela, T.T.3    Markkanen, P.M.H.4    Tuusa, J.T.5    Bouvier, M.6
  • 44
    • 57649139756 scopus 로고    scopus 로고
    • N-Glycan-mediated quality control in the endoplasmic reticulum is required for the expression of correctly folded δ-opioid receptors at the cell surface
    • Markkanen, P. M., and Petäjä-Repo, U. E. (2008) N-Glycan-mediated quality control in the endoplasmic reticulum is required for the expression of correctly folded δ-opioid receptors at the cell surface. J. Biol. Chem. 283, 29086-29098
    • (2008) J. Biol. Chem. , vol.283 , pp. 29086-29098
    • Markkanen, P.M.1    Petäjä-Repo, U.E.2
  • 45
    • 0027512245 scopus 로고
    • Role of oligosaccharides in the processing and function of human transferrin receptors. Effect of the loss of the three N-glycosyl oligosaccharides individually or together
    • Yang, B., Hoe, M. H., Black, P., and Hunt, R. C. (1993) Role of oligosaccharides in the processing and function of human transferrin receptors. Effect of the loss of the three N-glycosyl oligosaccharides individually or together. J. Biol. Chem. 268, 7435-7441 (Pubitemid 23105639)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.10 , pp. 7435-7441
    • Yang, B.1    Hoe, M.H.2    Black, P.3    Hunt, R.C.4
  • 46
    • 0026732917 scopus 로고
    • Presence of O-linked oligosaccharide on a threonine residue in the human transferrin receptor
    • Do, S. I., and Cummings, R. D. (1992) Presence of O-linked oligosaccharide on a threonine residue in the human transferrin receptor. Glycobiology 2, 345-353
    • (1992) Glycobiology , vol.2 , pp. 345-353
    • Do, S.I.1    Cummings, R.D.2
  • 47
    • 79952001514 scopus 로고    scopus 로고
    • i/o-coupled receptors compete for signaling to adenylyl cyclase in SH-SY5Y cells and reduce opioid-mediated cAMP overshoot
    • i/o-coupled receptors compete for signaling to adenylyl cyclase in SH-SY5Y cells and reduce opioid-mediated cAMP overshoot. Mol. Pharmacol. 79, 461-471
    • (2011) Mol. Pharmacol. , vol.79 , pp. 461-471
    • Levitt, E.S.1    Purington, L.C.2    Traynor, J.R.3
  • 48
    • 0037160105 scopus 로고    scopus 로고
    • 2- adrenergic receptor homo- and heterodimerization by bioluminescence resonance energy transfer
    • DOI 10.1074/jbc.M205767200
    • Mercier, J. F., Salahpour, A., Angers, S., Breit, A., and Bouvier, M. (2002) Quantitative assessment of β1- and β2-adrenergic receptor homo- and heterodimerization by bioluminescence resonance energy transfer. J. Biol. Chem. 277, 44925-44931 (Pubitemid 36159089)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.47 , pp. 44925-44931
    • Mercier, J.-F.1    Salahpour, A.2    Angers, S.3    Breit, A.4    Bouvier, M.5
  • 49
    • 0034714335 scopus 로고    scopus 로고
    • Oligomerization of μ- And δ-opioid receptors. Generation of novel functional properties
    • George, S. R., Fan, T., Xie, Z., Tse, R., Tam, V., Varghese, G., and O'Dowd, B. F. (2000) Oligomerization of μ- and δ-opioid receptors. Generation of novel functional properties. J. Biol. Chem. 275, 26128-26135
    • (2000) J. Biol. Chem. , vol.275 , pp. 26128-26135
    • George, S.R.1    Fan, T.2    Xie, Z.3    Tse, R.4    Tam, V.5    Varghese, G.6    O'Dowd, B.F.7
  • 50
    • 4043125390 scopus 로고    scopus 로고
    • Homodimerization of the β2-adrenergic receptor as a prerequisite for cell surface targeting
    • DOI 10.1074/jbc.M403363200
    • Salahpour, A., Angers, S., Mercier, J. F., Lagacé, M., Marullo, S., and Bouvier, M. (2004) Homodimerization of the δ2-adrenergic receptor as a prerequisite for cell surface targeting. J. Biol. Chem. 279, 33390-33397 (Pubitemid 39062987)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.32 , pp. 33390-33397
    • Salahpour, A.1    Angers, S.2    Mercier, J.-F.3    Lagace, M.4    Marullo, S.5    Bouvier, M.6


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