메뉴 건너뛰기




Volumn 287, Issue 50, 2012, Pages 42104-42118

Reengineering the collision coupling and diffusion mode of the A 2A-adenosine receptor: Palmitoylation in helix 8 relieves confinement

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE RECEPTOR; C TERMINUS; DIFFUSION LIMITS; DIFFUSION MODES; EXPRESSION LEVELS; G PROTEIN; G PROTEIN COUPLED RECEPTORS; LIPID RAFT; LOCAL CONFINEMENT; MEAN SQUARE DISPLACEMENT; METABOLIC LABELING; PALMITOYLATION; RANDOM WALK; SINGLE PARTICLE TRACKING; WILD TYPES;

EID: 84871341426     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.393579     Document Type: Article
Times cited : (11)

References (51)
  • 1
    • 77952565720 scopus 로고    scopus 로고
    • Adenosine receptors as drug targets
    • Fredholm, B. B. (2010) Adenosine receptors as drug targets. Exp. Cell Res. 316, 1284-1288
    • (2010) Exp. Cell Res. , vol.316 , pp. 1284-1288
    • Fredholm, B.B.1
  • 3
  • 4
    • 41849131038 scopus 로고    scopus 로고
    • 2A receptor antagonist istradefylline (KW-6002) reduces off time in Parkinson's disease: A double-blind, randomized, multicenter clinical trial (6002-US-005)
    • DOI 10.1002/ana.21315
    • LeWitt, P. A., Guttman, M., Tetrud, J. W., Tuite, P. J., Mori, A., Chaikin, P., and Sussman, N. M. (2008) Adenosine A2A receptor antagonist istradefylline (KW-6002) reduces "off" time in Parkinson's disease. A double-blind, randomized, multicenter clinical trial (6002-US-005). Ann. Neurol. 63, 295-302 (Pubitemid 351499859)
    • (2008) Annals of Neurology , vol.63 , Issue.3 , pp. 295-302
    • LeWitt, P.A.1    Guttman, M.2    Tetrud, J.W.3    Tuite, P.J.4    Mori, A.5    Chaikin, P.6    Sussman, N.M.7
  • 6
    • 61449136722 scopus 로고    scopus 로고
    • Adenosine receptor agonists for promotion of dermal wound healing
    • Valls, M. D., Cronstein, B. N., and Montesinos, M. C. (2009) Adenosine receptor agonists for promotion of dermal wound healing. Biochem. Pharmacol. 77, 1117-1124
    • (2009) Biochem. Pharmacol. , vol.77 , pp. 1117-1124
    • Valls, M.D.1    Cronstein, B.N.2    Montesinos, M.C.3
  • 9
    • 40349110970 scopus 로고    scopus 로고
    • 2A adenosine receptor: An introduction
    • DOI 10.1038/sj.bjp.0707524, PII 0707524
    • Palmer, T. M., and Trevethick, M. A. (2008) Suppression of inflammatory and immune responses by the A(2A) adenosine receptor. An introduction. Br. J. Pharmacol. 153, S27-S34 (Pubitemid 351340988)
    • (2008) British Journal of Pharmacology , vol.153 , Issue.SUPPL. 1
    • Palmer, T.M.1    Trevethick, M.A.2
  • 11
    • 33746256459 scopus 로고    scopus 로고
    • 2A-adenosine receptor recruits alternative signaling pathways
    • 2A-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
  • 12
  • 15
    • 84865304129 scopus 로고    scopus 로고
    • Agonist-bound structures of G protein-coupled receptors
    • Lebon, G., Warne, T., and Tate, C. G. (2012) Agonist-bound structures of G protein-coupled receptors. Curr. Opin. Struct. Biol. 22, 482-490
    • (2012) Curr. Opin. Struct. Biol. , vol.22 , pp. 482-490
    • Lebon, G.1    Warne, T.2    Tate, C.G.3
  • 18
    • 0038757730 scopus 로고    scopus 로고
    • Role of palmitoylation/depalmitoylation reactions in G-protein-coupled receptor function
    • DOI 10.1016/S0163-7258(02)00300-5, PII S0163725802003005
    • Qanbar, R., and Bouvier, M. (2003) Role of palmitoylation/ depalmitoylation reactions in G-protein-coupled receptor function. Pharmacol. Ther. 97, 1-33 (Pubitemid 35477802)
    • (2003) Pharmacology and Therapeutics , vol.97 , Issue.1 , pp. 1-33
    • Neve, K.A.1    Qanbar, R.2    Bouvier, M.3
  • 20
    • 0018126502 scopus 로고
    • Coupling of a single adenylate cyclase to two receptors: Adenosine and catecholamine
    • Tolkovsky, A. M., and Levitzki, A. (1978) Coupling of a single adenylate cyclase to two receptors. Adenosine and catecholamine. Biochemistry 17, 3811-3817 (Pubitemid 9022593)
    • (1978) Biochemistry , vol.17 , Issue.18 , pp. 3811-3817
    • Tolkovsky, A.M.1    Levitzki, A.2
  • 21
    • 0018791378 scopus 로고
    • Adenosine receptor permanently coupled to turkey erythrocyte adenylate cyclase
    • Braun, S., and Levitzki, A. (1979) Adenosine receptor permanently coupled to turkey erythrocyte adenylate cyclase. Biochemistry 18, 2134-2138
    • (1979) Biochemistry , vol.18 , pp. 2134-2138
    • Braun, S.1    Levitzki, A.2
  • 22
    • 0025921773 scopus 로고
    • 2 adenosine receptors. II. A restricted collision-coupling model of receptor-effector interaction
    • 2 adenosine receptors. II. A restricted collision-coupling model of receptor-effector interaction. Mol. Pharmacol. 39, 524-530
    • (1991) Mol. Pharmacol. , vol.39 , pp. 524-530
    • Gross, W.1    Lohse, M.J.2
  • 23
    • 0030049486 scopus 로고    scopus 로고
    • Thiophosphorylation of the G protein β subunit in human platelet membranes. Evidence against a direct phosphate transfer reaction to Gα subunits
    • Hohenegger, M., Mitterauer, T., Voss, T., Nanoff, C., and Freissmuth, M. (1996) Thiophosphorylation of the G protein β subunit in human platelet membranes. Evidence against a direct phosphate transfer reaction to Gα 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
  • 26
    • 0037031824 scopus 로고    scopus 로고
    • MAP kinase stimulation by cAMP does not require RAP1 but SRC family kinases
    • DOI 10.1074/jbc.M200556200
    • Klinger, M., Kudlacek, O., Seidel, M. G., Freissmuth, M., and Sexl, V. (2002) MAP kinase stimulation by cAMP does not require RAP1 but SRC family kinases. J. Biol. Chem. 277, 32490-32497 (Pubitemid 34984751)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.36 , pp. 32490-32497
    • Klinger, M.1    Kudlacek, O.2    Seidel, M.G.3    Freissmuth, M.4    Sexl, V.5
  • 27
    • 33748958810 scopus 로고    scopus 로고
    • Systematic screening for palmitoyl transferase activity of the DHHC protein family in mammalian cells
    • DOI 10.1016/j.ymeth.2006.05.015, PII S1046202306001538, Protein Palmitoylation
    • Fukata, Y., Iwanaga, T., and Fukata, M. (2006) Systematic screening for palmitoyl transferase activity of the DHHC protein family in mammalian cells. Methods 40, 177-182 (Pubitemid 44442975)
    • (2006) Methods , vol.40 , Issue.2 , pp. 177-182
    • Fukata, Y.1    Iwanaga, T.2    Fukata, M.3
  • 29
    • 34247857560 scopus 로고    scopus 로고
    • Multiple association states between glycine receptors and gephyrin identified by SPT analysis
    • DOI 10.1529/biophysj.106.095596
    • Ehrensperger, M. V., Hanus, C., Vannier, C., Triller, A., and Dahan, M. (2007) Multiple association states between glycine receptors and gephyrin identified by SPT analysis. Biophys. J. 92, 3706-3718 (Pubitemid 46698659)
    • (2007) Biophysical Journal , vol.92 , Issue.10 , pp. 3706-3718
    • Ehrensperger, M.-V.1    Hanus, C.2    Vannier, C.3    Triller, A.4    Dahan, M.5
  • 30
    • 77952215650 scopus 로고    scopus 로고
    • Optimized localization analysis for single-molecule tracking and superresolution microscopy
    • Mortensen, K. I., Churchman, L. S., Spudich, J. A., and Flyvbjerg, H. (2010) Optimized localization analysis for single-molecule tracking and superresolution microscopy. Nat. Methods 7, 377-381
    • (2010) Nat. Methods , vol.7 , pp. 377-381
    • Mortensen, K.I.1    Churchman, L.S.2    Spudich, J.A.3    Flyvbjerg, H.4
  • 31
    • 0027504198 scopus 로고
    • Confined lateral diffusion of membrane receptors as studied by single particle tracking (nanovid microscopy). Effects of calcium-induced differentiation in cultured epithelial cells
    • Kusumi, A., Sako, Y., and Yamamoto, M. (1993) Confined lateral diffusion of membrane receptors as studied by single particle tracking (nanovid microscopy). Effects of calcium-induced differentiation in cultured epithelial cells. Biophys. J. 65, 2021-2040 (Pubitemid 23334870)
    • (1993) Biophysical Journal , vol.65 , Issue.5 , pp. 2021-2040
    • Kusumi, A.1    Sako, Y.2    Yamamoto, M.3
  • 32
    • 0036787587 scopus 로고    scopus 로고
    • Apparent subdiffusion inherent to single particle tracking
    • Martin, D. S., Forstner, M. B., and Käs, J. A. (2002) Apparent subdiffusion inherent to single particle tracking. Biophys. J. 83, 2109-2117
    • (2002) Biophys. J. , vol.83 , pp. 2109-2117
    • Martin, D.S.1    Forstner, M.B.2    Käs, J.A.3
  • 34
    • 0027197103 scopus 로고
    • Lateral diffusion in an archipelago. Single-particle diffusion
    • Saxton, M. J. (1993) Lateral diffusion in an archipelago. Single-particle diffusion. Biophys. J. 64, 1766-1780
    • (1993) Biophys. J. , vol.64 , pp. 1766-1780
    • Saxton, M.J.1
  • 35
    • 0033198917 scopus 로고    scopus 로고
    • 1 adenosine receptor: Enhanced proteolysis of palmitoylation-deficient mutant receptors
    • DOI 10.1042/0264-6021:3420387
    • Gao, Z., Ni, Y., Szabo, G., and Linden, J. (1999) Palmitoylation of the recombinant human A1 adenosine receptor. Enhanced proteolysis of palmitoylation-deficient mutant receptors. Biochem. J. 342, 387-395 (Pubitemid 29425361)
    • (1999) Biochemical Journal , vol.342 , Issue.2 , pp. 387-395
    • Gao, Z.1    Ni, Y.2    Szabo, G.3    Linden, J.4
  • 36
    • 0043031408 scopus 로고    scopus 로고
    • 1 adenosine receptor reveals distinct roles of the membrane-proximal carboxyl terminus in receptor folding and G protein coupling
    • DOI 10.1074/jbc.M212918200
    • 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 (Pubitemid 36962422)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.32 , pp. 30283-30293
    • Pankevych, H.1    Korkhov, V.2    Freissmuth, M.3    Nanoff, C.4
  • 37
    • 0025924670 scopus 로고
    • 2 adenosine receptor. Guanine nucleotide modulation of agonist binding is enhanced by proteolysis
    • 2 adenosine receptor. Guanine nucleotide modulation of agonist binding is enhanced by proteolysis. Mol. Pharmacol. 39, 130-135
    • (1991) Mol. Pharmacol. , vol.39 , pp. 130-135
    • Nanoff, C.1    Jacobson, K.A.2    Stiles, G.L.3
  • 41
    • 67649306770 scopus 로고    scopus 로고
    • G-protein-coupled receptors, cholesterol and palmitoylation. Facts about fats
    • Chini, B., and Parenti, M. (2009) G-protein-coupled receptors, cholesterol and palmitoylation. Facts about fats. J. Mol. Endocrinol. 42, 371-379
    • (2009) J. Mol. Endocrinol. , vol.42 , pp. 371-379
    • Chini, B.1    Parenti, M.2
  • 43
    • 0026666760 scopus 로고
    • Functional expression of the human serotonin 5-HT1A receptor in Escherichia coli. Ligand binding properties and interaction with recombinant G protein α-subunits
    • Bertin, B., Freissmuth, M., Breyer, R. M., Schütz, W., 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 α-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
  • 46
    • 17644390240 scopus 로고    scopus 로고
    • Mass spectrometric analysis of agonist effects on posttranslational modifications of the β-2 adrenoceptor in mammalian cells
    • DOI 10.1021/bi0475469
    • Trester-Zedlitz, M., Burlingame, A., Kobilka, B., and von Zastrow, M. (2005) Mass spectrometric analysis of agonist effects on posttranslational modifications of the β2 adrenoceptor in mammalian cells. Biochemistry 44, 6133-6143 (Pubitemid 40570706)
    • (2005) Biochemistry , vol.44 , Issue.16 , pp. 6133-6143
    • Trester-Zedlitz, M.1    Burlingame, A.2    Kobilka, B.3    Von Zastrow, M.4
  • 47
    • 10844293498 scopus 로고    scopus 로고
    • 1A receptor tagged to yellow fluorescent protein
    • DOI 10.1021/bi0480887
    • Pucadyil, T. J., Kalipatnapu, S., Harikumar, K. G., Rangaraj, N., Karnik, S. S., and Chattopadhyay, A. (2004) G-protein-dependent cell surface dynamics of the human serotonin 1A receptor tagged to yellow fluorescent protein. Biochemistry 43, 15852-15862 (Pubitemid 39665084)
    • (2004) Biochemistry , vol.43 , Issue.50 , pp. 15852-15862
    • Pucadyil, T.J.1    Kalipatnapu, S.2    Harikumar, K.G.3    Rangaraj, N.4    Karnik, S.S.5    Chattopadhyay, A.6
  • 50
    • 76649102423 scopus 로고    scopus 로고
    • Proteome scale characterization of human S-acylated proteins in lipid raft-enriched and non-raft membranes
    • Yang, W., Di Vizio, D., Kirchner, M., Steen, H., and Freeman, M. R. (2010) Proteome scale characterization of human S-acylated proteins in lipid raft-enriched and non-raft membranes. Mol. Cell. Proteomics 9, 54-70
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 54-70
    • Yang, W.1    Di Vizio, D.2    Kirchner, M.3    Steen, H.4    Freeman, M.R.5
  • 51
    • 30944443590 scopus 로고    scopus 로고
    • Receptor palmitoylation and ubiquitination regulate anthrax toxin endocytosis
    • DOI 10.1083/jcb.200507067
    • Abrami, L., Leppla, S. H., and van der Goot, F. G. (2006) Receptor palmitoylation and ubiquitination regulate anthrax toxin endocytosis. J. Cell Biol. 172, 309-320 (Pubitemid 43112976)
    • (2006) Journal of Cell Biology , vol.172 , Issue.2 , pp. 309-320
    • Abrami, L.1    Leppla, S.H.2    Gisou, V.D.G.F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.