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Volumn 288, Issue 40, 2013, Pages 28831-28844

Recruitment of a cytoplasmic chaperone relay by the A2A adenosine receptor

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE RECEPTOR; CYTOSOLIC; ENDOPLASMIC RETICULUM; EXCHANGE MODELS; HEAT-SHOCK PROTEIN; MOLECULAR CHAPERONES;

EID: 84885107181     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.464776     Document Type: Article
Times cited : (37)

References (51)
  • 1
    • 0036142817 scopus 로고    scopus 로고
    • Adenosine receptors. G protein-mediated signalling and the role of accessory proteins
    • Klinger, M., Freissmuth, M., and Nanoff, C. (2002) Adenosine receptors.G protein-mediated signalling and the role of accessory proteins. Cell. Signal. 14, 99-108
    • (2002) Cell. Signal. , vol.14 , pp. 99-108
    • Klinger, M.1    Freissmuth, M.2    Nanoff, C.3
  • 2
    • 0028290280 scopus 로고
    • A carboxyl-terminally truncated mutant and nonglycosylated A2A adenosine receptors retain ligand-binding
    • Piersen, C. E., True, C. D., and Wells, J. N. (1994) A carboxyl-terminally truncated mutant and nonglycosylated A2A adenosine receptors retain ligand-binding. Mol. Pharmacol. 45, 861-870
    • (1994) Mol. Pharmacol. , vol.45 , pp. 861-870
    • Piersen, C.E.1    True, C.D.2    Wells, J.N.3
  • 3
    • 0036380649 scopus 로고    scopus 로고
    • Removal of the carboxyl terminus of the A2A-adenosine receptor blunts constitutive activity. Differential effect on cAMP accumulation and MAP kinase stimulation
    • Klinger, M., Kuhn, M., Just, H., Stefan, E., Palmer, T., Freissmuth, M., and Nanoff, C. (2002) Removal of the carboxyl terminus of the A2A-adenosine receptor blunts constitutive activity. Differential effect on cAMP accumulation and MAP kinase stimulation. Naunyn Schmiedebergs Arch. Pharmacol. 366, 287-298
    • (2002) Naunyn Schmiedebergs Arch. Pharmacol. , vol.366 , pp. 287-298
    • Klinger, M.1    Kuhn, M.2    Just, H.3    Stefan, E.4    Palmer, T.5    Freissmuth, M.6    Nanoff, C.7
  • 4
    • 79953194836 scopus 로고    scopus 로고
    • From cradle to twilight. The carboxyl terminus directs the fate of the A2A-adenosine receptor
    • Keuerleber, S., Gsandtner, I., and Freissmuth, M. (2011) From cradle to twilight. The carboxyl terminus directs the fate of the A2A-adenosine receptor. Biochim. Biophys. Acta 1808, 1350-1357
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 1350-1357
    • Keuerleber, S.1    Gsandtner, I.2    Freissmuth, M.3
  • 5
    • 84871341426 scopus 로고    scopus 로고
    • Reengineering the collision coupling and diffusion mode of the A2A-adenosine receptor. Palmitolyation in helix8 relieves confinement
    • Keuerleber, S., Thurner, P., Gruber, C.W., Zezula, J., and Freissmuth, M. (2012) Reengineering the collision coupling and diffusion mode of the A2A-adenosine receptor. Palmitolyation in helix 8 relieves confinement. J. Biol. Chem. 287, 42104-42118
    • (2012) J. Biol. Chem. , vol.287 , pp. 42104-42118
    • Keuerleber, S.1    Thurner, P.2    Gruber, C.W.3    Zezula, J.4    Freissmuth, M.5
  • 6
    • 33746256459 scopus 로고    scopus 로고
    • A tail of two signals. The C terminus of the A2A-adenosine receptor recruits alternative signaling pathways
    • Gsandtner, I., and Freissmuth, M. (2006) A tail of two signals. The C terminus of the A2A-adenosine receptor recruits alternative signaling pathways. Mol. Pharmacol. 70, 447-449
    • (2006) Mol. Pharmacol. , vol.70 , pp. 447-449
    • Gsandtner, I.1    Freissmuth, M.2
  • 7
    • 44049095443 scopus 로고    scopus 로고
    • Restricted collision coupling of theA2A-receptor revisited. Evidence for physical separation of two signaling cascades
    • Charalambous, C., Gsandtner, I., Keuerleber, S., Milan-Lobo, L., Kudlacek, O., Freissmuth, M., and Zezula, J. (2008) Restricted collision coupling of theA2A-receptor revisited. Evidence for physical separation of two signaling cascades. J. Biol. Chem. 283, 9276-9288
    • (2008) J. Biol. Chem. , vol.283 , pp. 9276-9288
    • Charalambous, C.1    Gsandtner, I.2    Keuerleber, S.3    Milan-Lobo, L.4    Kudlacek, O.5    Freissmuth, M.6    Zezula, J.7
  • 10
    • 33746256457 scopus 로고    scopus 로고
    • Rescue of p53 blockage by the A2A adenosine receptor via a novel interacting protein, translin-associated protein X
    • Sun, C. N., Cheng, H. C., Chou, J. L., Lee, S. Y., Lin, Y. W., Lai, H. L., Chen, H. M., and Chern, Y. (2006) Rescue of p53 blockage by the A2A adenosine receptor via a novel interacting protein, translin-associated protein X. Mol. Pharmacol. 70, 454-466
    • (2006) Mol. Pharmacol. , vol.70 , pp. 454-466
    • Sun, C.N.1    Cheng, H.C.2    Chou, J.L.3    Lee, S.Y.4    Lin, Y.W.5    Lai, H.L.6    Chen, H.M.7    Chern, Y.8
  • 13
    • 0035853065 scopus 로고    scopus 로고
    • Activation of Trk neurotrophin receptors in the absence of neurotrophins
    • Lee, F. S., and Chao, M. V. (2001) Activation of Trk neurotrophin receptors in the absence of neurotrophins. Proc. Natl. Acad. Sci. U.S.A. 98, 3555-3560
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 3555-3560
    • Lee, F.S.1    Chao, M.V.2
  • 14
    • 0036204336 scopus 로고    scopus 로고
    • Anoxia redistributes adenosineA2A receptors in PC12 cells and increases receptor-mediated formation of cAMP
    • Arslan, G., Kull, B., and Fredholm, B. B. (2002) Anoxia redistributes adenosineA2A receptors in PC12 cells and increases receptor-mediated formation of cAMP. Naunyn Schmiedebergs Arch. Pharmacol. 365, 150-157
    • (2002) Naunyn Schmiedebergs Arch. Pharmacol. , vol.365 , pp. 150-157
    • Arslan, G.1    Kull, B.2    Fredholm, B.B.3
  • 15
    • 41249102584 scopus 로고    scopus 로고
    • Peptide-based interactions with calnexin target misassembled membrane proteins into endoplasmic reticulum-derived multilamellar bodies
    • Korkhov, V. M., Milan-Lobo, L., Zuber, B., Farhan, H., Schmid, J. A., Freissmuth, M., and Sitte, H. H. (2008) Peptide-based interactions with calnexin target misassembled membrane proteins into endoplasmic reticulum-derived multilamellar bodies. J. Mol. Biol. 378, 337-352
    • (2008) J. Mol. Biol. , vol.378 , pp. 337-352
    • Korkhov, V.M.1    Milan-Lobo, L.2    Zuber, B.3    Farhan, H.4    Schmid, J.A.5    Freissmuth, M.6    Sitte, H.H.7
  • 16
    • 37048999786 scopus 로고    scopus 로고
    • A novel tandem affinity purification strategy for the efficient isolation and characterisation of native protein complexes
    • Gloeckner, C. J., Boldt, K., Schumacher, A., Roepman, R., and Ueffing, M. (2007) A novel tandem affinity purification strategy for the efficient isolation and characterisation of native protein complexes. Proteomics 7, 4228-4234
    • (2007) Proteomics , vol.7 , pp. 4228-4234
    • Gloeckner, C.J.1    Boldt, K.2    Schumacher, A.3    Roepman, R.4    Ueffing, M.5
  • 19
    • 0030049486 scopus 로고    scopus 로고
    • Thiophosphorylation of the G protein-subunit in human platelet membranes. Evidence against a direct phosphate transfer reaction to G-subunits
    • Hohenegger M., Mitterauer T., Voss T., Nanoff C., Freissmuth M. (1996) Thiophosphorylation of the G protein-subunit in human platelet membranes. Evidence against a direct phosphate transfer reaction to G-subunits. Mol. Pharmacol. 49, 73-80
    • (1996) Mol. Pharmacol. , vol.49 , pp. 73-80
    • Hohenegger, M.1    Mitterauer, T.2    Voss, T.3    Nanoff, C.4    Freissmuth, M.5
  • 20
    • 8744236215 scopus 로고    scopus 로고
    • Pharmacochaperones post-translationally enhance cell surface expression by increasing conformational stability of wild-type and mutant vasopressin V2 receptors
    • Wüller, S., Wiesner, B., Löffler, A., Furkert, J., Krause, G., Hermosilla, R., Schaefer, M., Schülein, R., Rosenthal, W., and Oksche, A. (2004) Pharmacochaperones post-translationally enhance cell surface expression by increasing conformational stability of wild-type and mutant vasopressin V2 receptors. J. Biol. Chem. 279, 47254-47263
    • (2004) J. Biol. Chem. , vol.279 , pp. 47254-47263
    • Wüller, S.1    Wiesner, B.2    Löffler, A.3    Furkert, J.4    Krause, G.5    Hermosilla, R.6    Schaefer, M.7    Schülein, R.8    Rosenthal, W.9    Oksche, A.10
  • 22
    • 0032942443 scopus 로고    scopus 로고
    • Distinction between surmountable and insurmountable selective AT1 receptor antagonists by use of CHO-K1 cells expressing human angiotensin II AT1 receptors
    • Vanderheyden, P. M., Fierens, F. L., De Backer, J. P., Fraeyman, N., and Vauquelin, G. (1999) Distinction between surmountable and insurmountable selective AT1 receptor antagonists by use of CHO-K1 cells expressing human angiotensin II AT1 receptors. Br. J. Pharmacol. 126, 1057-1065
    • (1999) Br. J. Pharmacol. , vol.126 , pp. 1057-1065
    • Vanderheyden, P.M.1    Fierens, F.L.2    De Backer, J.P.3    Fraeyman, N.4    Vauquelin, G.5
  • 23
    • 0029887140 scopus 로고    scopus 로고
    • The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding
    • Freeman, B. C., and Morimoto, R. I. (1996) The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding. EMBO J. 15, 2969-2979
    • (1996) EMBO J. , vol.15 , pp. 2969-2979
    • Freeman, B.C.1    Morimoto, R.I.2
  • 24
    • 0034708485 scopus 로고    scopus 로고
    • A critical role for the proteasome activator PA28 in the Hsp90-dependent protein refolding
    • Minami, Y., Kawasaki, H., Minami, M., Tanahashi, N., Tanaka, K., and Yahara, I. (2000) A critical role for the proteasome activator PA28 in the Hsp90-dependent protein refolding. J. Biol. Chem. 275, 9055-9061
    • (2000) J. Biol. Chem. , vol.275 , pp. 9055-9061
    • Minami, Y.1    Kawasaki, H.2    Minami, M.3    Tanahashi, N.4    Tanaka, K.5    Yahara, I.6
  • 28
    • 0031844350 scopus 로고    scopus 로고
    • Antibiotic radicicol binds to the N-terminal domain of Hsp90 and shares important biologic activities with geldanamycin
    • Schulte, T. W., Akinaga, S., Soga, S., Sullivan, W., Stensgard, B., Toft, D., and Neckers, L. M. (1998) Antibiotic radicicol binds to the N-terminal domain of Hsp90 and shares important biologic activities with geldanamycin. Cell Stress Chaperones. 3, 100-108
    • (1998) Cell Stress Chaperones. , vol.3 , pp. 100-108
    • Schulte, T.W.1    Akinaga, S.2    Soga, S.3    Sullivan, W.4    Stensgard, B.5    Toft, D.6    Neckers, L.M.7
  • 29
    • 77951907072 scopus 로고    scopus 로고
    • Phase i pharmacokinetic and pharmacodynamic study of 17- dimethylaminoethylamino-17-demethoxygeldanamycin, an inhibitor of heatshock protein 90, in patients with advanced solid tumors
    • Ramanathan, R. K., Egorin, M. J., Erlichman, C., Remick, S. C., Ramalingam, S. S., Naret, C., Holleran, J. L., TenEyck, C. J., Ivy, S. P., Belani, C. P. (2010) Phase I pharmacokinetic and pharmacodynamic study of 17-dimethylaminoethylamino-17-demethoxygeldanamycin, an inhibitor of heatshock protein 90, in patients with advanced solid tumors. J. Clin. Oncol. 28, 1520-1526
    • (2010) J. Clin. Oncol. , vol.28 , pp. 1520-1526
    • Ramanathan, R.K.1    Egorin, M.J.2    Erlichman, C.3    Remick, S.C.4    Ramalingam, S.S.5    Naret, C.6    Holleran, J.L.7    Teneyck, C.J.8    Ivy, S.P.9    Belani, C.P.10
  • 30
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • Hartl, F. U., Bracher, A., and Hayer-Hartl, M. (2011) Molecular chaperones in protein folding and proteostasis. Nature 475, 324-332
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 31
    • 77954947810 scopus 로고    scopus 로고
    • The HSP70 chaperone machinery. J proteins as drivers of functional specificity
    • Kampinga, H. H., and Craig, E. A. (2010) The HSP70 chaperone machinery. J proteins as drivers of functional specificity. Nat. Rev. Mol. Cell Biol. 11, 579-592
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 579-592
    • Kampinga, H.H.1    Craig, E.A.2
  • 32
    • 83355169702 scopus 로고    scopus 로고
    • Inhibition of endoplasmic reticulum-associated degradation rescues native folding in loss of function protein misfolding diseases
    • Wang, F., Song, W., Brancati, G., and Segatori, L. (2011) Inhibition of endoplasmic reticulum-associated degradation rescues native folding in loss of function protein misfolding diseases. J. Biol. Chem. 286, 43454-43464
    • (2011) J. Biol. Chem. , vol.286 , pp. 43454-43464
    • Wang, F.1    Song, W.2    Brancati, G.3    Segatori, L.4
  • 33
    • 0032541344 scopus 로고    scopus 로고
    • ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo
    • Panaretou, B., Prodromou, C., Roe, S. M., O'Brien, R., Ladbury, J. E., Piper, P. W., and Pearl, L. H. (1998) ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo. EMBO J. 17, 4829-4836
    • (1998) EMBO J. , vol.17 , pp. 4829-4836
    • Panaretou, B.1    Prodromou, C.2    Roe, S.M.3    O'Brien, R.4    Ladbury, J.E.5    Piper, P.W.6    Pearl, L.H.7
  • 35
    • 0037336295 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum
    • Ellgaard, L., and Helenius, A. (2003) Quality control in the endoplasmic reticulum. Nat. Rev. Mol. Cell Biol. 4, 181-191
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 181-191
    • Ellgaard, L.1    Helenius, A.2
  • 36
    • 33751508817 scopus 로고    scopus 로고
    • N-Glycan processing in ER quality control
    • Ruddock, L. W., and Molinari, M. (2006) N-Glycan processing in ER quality control. J. Cell Sci. 119, 4373-4380
    • (2006) J. Cell Sci. , vol.119 , pp. 4373-4380
    • Ruddock, L.W.1    Molinari, M.2
  • 37
    • 85029310052 scopus 로고    scopus 로고
    • ER-bound steps in the biosynthesis of G protein-coupled receptors
    • Nanoff, C., and Freissmuth, M. (2012) ER-bound steps in the biosynthesis of G protein-coupled receptors. Subcell. Biochem. 63, 1-21
    • (2012) Subcell. Biochem. , vol.63 , pp. 1-21
    • Nanoff, C.1    Freissmuth, M.2
  • 39
    • 0033863883 scopus 로고    scopus 로고
    • The heat shock protein 90 antagonist geldanamycin alters chaperone association with p210bcr-abl and v-src proteins before their degradation by the proteasome
    • An, W. G., Schulte, T. W., and Neckers, L. M. (2000) The heat shock protein 90 antagonist geldanamycin alters chaperone association with p210bcr-abl and v-src proteins before their degradation by the proteasome. Cell Growth Differ. 11, 355-360
    • (2000) Cell Growth Differ. , vol.11 , pp. 355-360
    • An, W.G.1    Schulte, T.W.2    Neckers, L.M.3
  • 40
    • 0035011489 scopus 로고    scopus 로고
    • Regulation of transport of the dopamineD1 receptor by a new membrane-associated ER protein
    • Bermak, J. C., Li, M., Bullock, C., and Zhou, Q. Y. (2001) Regulation of transport of the dopamineD1 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
  • 41
  • 42
    • 63849177196 scopus 로고    scopus 로고
    • Anterograde trafficking of G protein-coupled receptors. Function of the C-terminal F(X) 6LL motif in export from the endoplasmic reticulum
    • Duvernay, M. T., Dong, C., Zhang, X., Zhou, F., Nichols, C. D., and Wu, G. (2009) Anterograde trafficking of G protein-coupled receptors. Function of the C-terminal F(X)6LL motif in export from the endoplasmic reticulum. Mol. Pharmacol. 75, 751-761
    • (2009) Mol. Pharmacol. , vol.75 , pp. 751-761
    • Duvernay, M.T.1    Dong, C.2    Zhang, X.3    Zhou, F.4    Nichols, C.D.5    Wu, G.6
  • 43
    • 12544254491 scopus 로고    scopus 로고
    • A novel C-terminal motif is necessary for the export of the vasopressin V1b/V3 receptor to the plasma membrane
    • Robert, J., Clauser, E., Petit, P. X., and Ventura, M. A. (2005) A novel C-terminal motif is necessary for the export of the vasopressin V1b/V3 receptor to the plasma membrane. J. Biol. Chem. 280, 2300-2308
    • (2005) J. Biol. Chem. , vol.280 , pp. 2300-2308
    • Robert, J.1    Clauser, E.2    Petit, P.X.3    Ventura, M.A.4
  • 44
    • 0043031408 scopus 로고    scopus 로고
    • Truncation of the A1 adenosine receptor reveals distinct roles of the membrane-proximal carboxyl terminus in receptor folding and G protein coupling
    • Pankevych, H., Korkhov, V., Freissmuth, M., and Nanoff, C. (2003) Truncation of the A1 adenosine receptor reveals distinct roles of the membrane-proximal carboxyl terminus in receptor folding and G protein coupling. J. Biol. Chem. 278, 30283-30293
    • (2003) J. Biol. Chem. , vol.278 , pp. 30283-30293
    • Pankevych, H.1    Korkhov, V.2    Freissmuth, M.3    Nanoff, C.4
  • 46
    • 84866180204 scopus 로고    scopus 로고
    • Molecular chaperones as targets to circumvent the CFTR defect in cystic fibrosis
    • Chanoux, R. A, Rubenstein, R. C. (2012) Molecular chaperones as targets to circumvent the CFTR defect in cystic fibrosis. Front. Pharmacol. 3, 137
    • (2012) Front. Pharmacol. , vol.3 , pp. 137
    • Chanoux, R.A.1    Rubenstein, R.C.2
  • 47
    • 83755181547 scopus 로고    scopus 로고
    • The thiazide-sensitive NaCl cotransporter is targeted for chaperone-dependent endoplasmic reticulum-associated degradation
    • Needham, P. G., Mikoluk, K., Dhakarwal, P., Khadem, S., Snyder, A. C., Subramanya, A. R., and Brodsky, J. L. (2011) The thiazide-sensitive NaCl cotransporter is targeted for chaperone-dependent endoplasmic reticulum-associated degradation. J. Biol. Chem. 286, 43611-43621
    • (2011) J. Biol. Chem. , vol.286 , pp. 43611-43621
    • Needham, P.G.1    Mikoluk, K.2    Dhakarwal, P.3    Khadem, S.4    Snyder, A.C.5    Subramanya, A.R.6    Brodsky, J.L.7
  • 48
    • 34748871331 scopus 로고    scopus 로고
    • G proteincoupled receptor trafficking in health and disease. Lessons learned to prepare for therapeutic mutant rescue in vivo
    • Conn, P. M., Ulloa-Aguirre, A., Ito, J., and Janovick, J. A. (2007) G proteincoupled receptor trafficking in health and disease. Lessons learned to prepare for therapeutic mutant rescue in vivo. Pharmacol. Rev. 59, 225-250
    • (2007) Pharmacol. Rev. , vol.59 , pp. 225-250
    • Conn, P.M.1    Ulloa-Aguirre, A.2    Ito, J.3    Janovick, J.A.4
  • 49
    • 0025987006 scopus 로고
    • Expression of two human-adrenergic receptors in Escherichia coli. Functional interaction with two forms of the stimulatory G protein
    • Freissmuth, M., Selzer, E., Marullo, S., Schütz, W., and Strosberg, A. D. (1991) Expression of two human-adrenergic receptors in Escherichia coli. Functional interaction with two forms of the stimulatory G protein. Proc. Natl. Acad. Sci. U.S.A. 88, 8548-8552
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 8548-8552
    • Freissmuth, M.1    Selzer, E.2    Marullo, S.3    Schütz, W.4    Strosberg, A.D.5
  • 50
    • 0026666760 scopus 로고
    • Functional expression of the human serotonin 5-HT1A receptor in Escherichia coli. Ligand binding properties and interaction with recombinant G protein-subunits
    • Bertin, B., Freissmuth, M., Breyer, R. M., Schütz, W., and Strosberg, A. D., and Marullo, S. (1992) Functional expression of the human serotonin 5-HT1A receptor in Escherichia coli. Ligand binding properties and interaction with recombinant G protein-subunits. J. Biol. Chem. 267, 8200-8206
    • (1992) J. Biol. Chem. , vol.267 , pp. 8200-8206
    • Bertin, B.1    Freissmuth, M.2    Breyer, R.M.3    Schütz, W.4    Strosberg, A.D.5    Marullo, S.6


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