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Volumn 28, Issue 5, 2003, Pages 238-243

Regulation of heptaspanning-membrane-receptor function by dimerization and clustering

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE A1 RECEPTOR; CAVEOLIN; G PROTEIN COUPLED RECEPTOR; MEMBRANE RECEPTOR;

EID: 0037727707     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0968-0004(03)00065-3     Document Type: Review
Times cited : (75)

References (40)
  • 1
    • 0026793456 scopus 로고
    • Growth factor signalling by receptor tyrosine kinases
    • Schlessinger J., Ullrich A. Growth factor signalling by receptor tyrosine kinases. Neuron. 9:1992;383-391.
    • (1992) Neuron , vol.9 , pp. 383-391
    • Schlessinger, J.1    Ullrich, A.2
  • 2
    • 0025343230 scopus 로고
    • Signal transduction by receptors with tyrosine kinase activity
    • Ullrich A., Schlessinger J. Signal transduction by receptors with tyrosine kinase activity. Cell. 20:1990;203-212.
    • (1990) Cell , vol.20 , pp. 203-212
    • Ullrich, A.1    Schlessinger, J.2
  • 3
    • 0019291065 scopus 로고
    • Aspects on receptor regulation and isoreceptor identification
    • Agnati L.F., et al. Aspects on receptor regulation and isoreceptor identification. Med. Biol. 58:1980;182-187.
    • (1980) Med. Biol. , vol.58 , pp. 182-187
    • Agnati, L.F.1
  • 4
    • 0020668303 scopus 로고
    • Evidence for the existence of receptor-receptor interactions in the central nervous system. Studies on the regulation of monoamine receptors by neuropeptides
    • Fuxe K., et al. Evidence for the existence of receptor-receptor interactions in the central nervous system. Studies on the regulation of monoamine receptors by neuropeptides. J. Neural Transm. Suppl. 18:1983;165-179.
    • (1983) J. Neural Transm. Suppl. , vol.18 , pp. 165-179
    • Fuxe, K.1
  • 5
    • 85031169619 scopus 로고    scopus 로고
    • Molecular mechanisms and therapeutical implications of intramembrane receptor-receptor interactions among heptahelical receptors with examples from the striato-pallidal GABA neurons
    • in press
    • Agnati, L.F. et al. Molecular mechanisms and therapeutical implications of intramembrane receptor-receptor interactions among heptahelical receptors with examples from the striato-pallidal GABA neurons. Pharmacol. Rev. (in press).
    • Pharmacol. Rev.
    • Agnati, L.F.1
  • 6
    • 0033771402 scopus 로고    scopus 로고
    • The superfamily of heptahelical receptors
    • Lefkowitz R.J. The superfamily of heptahelical receptors. Nat. Cell Biol. 2:2000;E133-E136.
    • (2000) Nat. Cell Biol. , vol.2
    • Lefkowitz, R.J.1
  • 7
    • 0035478746 scopus 로고    scopus 로고
    • Protein-protein interactions at G-protein-coupled receptors
    • Milligan G., White J.H. Protein-protein interactions at G-protein-coupled receptors. Trends Pharmacol. Sci. 22:2001;513-518.
    • (2001) Trends Pharmacol. Sci. , vol.22 , pp. 513-518
    • Milligan, G.1    White, J.H.2
  • 8
    • 0035258223 scopus 로고    scopus 로고
    • Heterodimerization of G protein coupled receptors in the CNS
    • Marshall F.H. Heterodimerization of G protein coupled receptors in the CNS. Curr. Opin. Pharmacol. 1:2001;40-44.
    • (2001) Curr. Opin. Pharmacol. , vol.1 , pp. 40-44
    • Marshall, F.H.1
  • 9
    • 0035318509 scopus 로고    scopus 로고
    • Oligomerization of G-protein-coupled transmitter receptors
    • Bouvier M. 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
  • 10
    • 0035313703 scopus 로고    scopus 로고
    • Expanding roles for β-arrestins as scaffolds and adapters in GPCR signalling and trafficking
    • Miller W.E., Lefkowitz R.J. Expanding roles for β-arrestins as scaffolds and adapters in GPCR signalling and trafficking. Curr. Opin. Cell Biol. 13:2001;139-145.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 139-145
    • Miller, W.E.1    Lefkowitz, R.J.2
  • 11
    • 0036473397 scopus 로고    scopus 로고
    • The role of β-arrestins in the termination and transduction of G-protein-coupled receptor signals
    • Luttrell L.M., Lefkowitz R.J. The role of β-arrestins in the termination and transduction of G-protein-coupled receptor signals. J. Cell Sci. 115:2002;445-465.
    • (2002) J. Cell Sci. , vol.115 , pp. 445-465
    • Luttrell, L.M.1    Lefkowitz, R.J.2
  • 12
    • 0035379704 scopus 로고    scopus 로고
    • Comodulation of CXCR4 and CD26 in human lymphocytes
    • Herrera C., et al. Comodulation of CXCR4 and CD26 in human lymphocytes. J. Biol. Chem. 276:2001;19532-19539.
    • (2001) J. Biol. Chem. , vol.276 , pp. 19532-19539
    • Herrera, C.1
  • 13
    • 0035839639 scopus 로고    scopus 로고
    • Kinetic investigation of chemokine truncation by CD26/dipeptidyl peptidase IV reveals a striking selectivity within the chemokine family
    • Lambeir A.M., et al. Kinetic investigation of chemokine truncation by CD26/dipeptidyl peptidase IV reveals a striking selectivity within the chemokine family. J. Biol. Chem. 276:2001;29839-29845.
    • (2001) J. Biol. Chem. , vol.276 , pp. 29839-29845
    • Lambeir, A.M.1
  • 14
    • 0029892284 scopus 로고    scopus 로고
    • Adenosine deaminase interacts with A1 adenosine receptors in pig brain cortical membranes
    • Saura C.A., et al. Adenosine deaminase interacts with A1 adenosine receptors in pig brain cortical membranes. J. Neurochem. 66:1996;1675-1682.
    • (1996) J. Neurochem. , vol.66 , pp. 1675-1682
    • Saura, C.A.1
  • 15
    • 0034746914 scopus 로고    scopus 로고
    • Adenosine A2B receptors behave as an alternative anchoring protein for cell surface adenosine deaminase in lymphocytes and cultured cells
    • Herrera C., et al. Adenosine A2B receptors behave as an alternative anchoring protein for cell surface adenosine deaminase in lymphocytes and cultured cells. Mol. Pharmacol. 59:2001;127-134.
    • (2001) Mol. Pharmacol. , vol.59 , pp. 127-134
    • Herrera, C.1
  • 16
    • 0025923551 scopus 로고
    • The binding of [3H]R-PIA to A1 adenosine receptors produces a conversion of the high- to the low-affinity states
    • Casadó V., et al. The binding of [3H]R-PIA to A1 adenosine receptors produces a conversion of the high- to the low-affinity states. FEBS Lett. 286:1991;221-224.
    • (1991) FEBS Lett. , vol.286 , pp. 221-224
    • Casadó, V.1
  • 17
    • 0034682445 scopus 로고    scopus 로고
    • Dopamine D1 and adenosine A1 receptors assemble into functionally interacting heteromic complexes
    • Ginés S., et al. Dopamine D1 and adenosine A1 receptors assemble into functionally interacting heteromic complexes. Proc. Natl. Acad. Sci. U. S. A. 97:2000;8606-8611.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 8606-8611
    • Ginés, S.1
  • 18
    • 0033621564 scopus 로고    scopus 로고
    • Activation of adenosine A1 and A2A receptors modulates dopamine D2 receptor-induced responses in stably transfected human neuroblastoma cells
    • Salim H., et al. Activation of adenosine A1 and A2A receptors modulates dopamine D2 receptor-induced responses in stably transfected human neuroblastoma cells. J. Neurochem. 74:2000;432-439.
    • (2000) J. Neurochem. , vol.74 , pp. 432-439
    • Salim, H.1
  • 19
    • 0242460494 scopus 로고    scopus 로고
    • Metabotropic glutamate 1α and adenosine receptors assemble into functionally interacting complexes
    • Ciruela F., et al. Metabotropic glutamate 1α and adenosine 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
  • 20
    • 0035726693 scopus 로고    scopus 로고
    • G-protein-coupled receptor dimerization: Modulation of receptor function
    • Rios C.D., et al. G-protein-coupled receptor dimerization: modulation of receptor function. Pharmacol. Ther. 92:2001;71-87.
    • (2001) Pharmacol. Ther. , vol.92 , pp. 71-87
    • Rios, C.D.1
  • 21
    • 0033944602 scopus 로고    scopus 로고
    • The heat shock cognate protein hsc73 assembles with A1 adenosine receptors to form functional modules in the cell membrane
    • Sarrio A., et al. The heat shock cognate protein hsc73 assembles with A1 adenosine receptors to form functional modules in the cell membrane. Mol. Cell. Biol. 20:2000;5164-5174.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 5164-5174
    • Sarrio, A.1
  • 22
    • 0035032487 scopus 로고    scopus 로고
    • Involvement of caveolin in ligand-induced recruitment and internalization of A(1) adenosine receptor and adenosine deaminase in an epithelial cell line
    • Ginés S., et al. Involvement of caveolin in ligand-induced recruitment and internalization of A(1) adenosine receptor and adenosine deaminase in an epithelial cell line. Mol. Pharmacol. 59:2001;1314-1323.
    • (2001) Mol. Pharmacol. , vol.59 , pp. 1314-1323
    • Ginés, S.1
  • 23
    • 85031174631 scopus 로고    scopus 로고
    • Ligand-induced caveolae-mediated internalisation of A1 adenosine receptors. Morphological evidence of endosomal sorting and receptor recycling
    • in press
    • Escriche, M. et al. Ligand-induced caveolae-mediated internalisation of A1 adenosine receptors. Morphological evidence of endosomal sorting and receptor recycling. Exp. Cell Res. (in press).
    • Exp. Cell Res.
    • Escriche, M.1
  • 24
    • 0036729484 scopus 로고    scopus 로고
    • Seven-transmembrane receptors
    • Pierce K.C., et al. Seven-transmembrane receptors. Nat. Rev. Mol. Cell Biol. 3:2002;639-650.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 639-650
    • Pierce, K.C.1
  • 25
    • 0032503692 scopus 로고    scopus 로고
    • Adenosine deaminase and A1 adenosine receptors internalize together following agonist-induced receptor desensitization
    • Saura C.A., et al. Adenosine deaminase and A1 adenosine receptors internalize together following agonist-induced receptor desensitization. J. Biol. Chem. 273:1998;17610-17617.
    • (1998) J. Biol. Chem. , vol.273 , pp. 17610-17617
    • Saura, C.A.1
  • 26
    • 0018820668 scopus 로고
    • Specific binding of 2-[3H]chloroadenosine to rat brain cortical membranes
    • Wu P.H., et al. Specific binding of 2-[3H]chloroadenosine to rat brain cortical membranes. Can. J. Physiol. Pharmacol. 58:1980;576-579.
    • (1980) Can. J. Physiol. Pharmacol. , vol.58 , pp. 576-579
    • Wu, P.H.1
  • 27
    • 0019957347 scopus 로고
    • Adenosine receptors in rat brain membranes: Characterization of high affinity binding of [3H]-2-chloroadenosine
    • Wu P.H., Phillis J.W. Adenosine receptors in rat brain membranes: characterization of high affinity binding of [3H]-2-chloroadenosine. Int. J. Biochem. 14:1982;399-404.
    • (1982) Int. J. Biochem. , vol.14 , pp. 399-404
    • Wu, P.H.1    Phillis, J.W.2
  • 28
    • 1842792994 scopus 로고
    • Biochemical characterization of putative central purinergic receptors by using 2-chloro[3H]adenosine, a stable analog of adenosine
    • Williams M., Risley E.A. Biochemical characterization of putative central purinergic receptors by using 2-chloro[3H]adenosine, a stable analog of adenosine. Proc. Natl. Acad. Sci. U. S. A. 77:1980;6892-6896.
    • (1980) Proc. Natl. Acad. Sci. U. S. A. , vol.77 , pp. 6892-6896
    • Williams, M.1    Risley, E.A.2
  • 29
    • 0018876708 scopus 로고
    • High affinity binding of 2-chloroadenosine to rat brain synaptic membranes
    • Williams M., Risley E.A. High affinity binding of 2-chloroadenosine to rat brain synaptic membranes. Eur. J. Pharmacol. 64:1980;369-370.
    • (1980) Eur. J. Pharmacol. , vol.64 , pp. 369-370
    • Williams, M.1    Risley, E.A.2
  • 30
    • 0026434561 scopus 로고
    • Atomic structure of adenosine deaminase complexed with a transition-state analog: Understanding catalysis and immunodeficiency mutations
    • Wilson D.K., et al. Atomic structure of adenosine deaminase complexed with a transition-state analog: understanding catalysis and immunodeficiency mutations. Science. 252:1991;1278-1284.
    • (1991) Science , vol.252 , pp. 1278-1284
    • Wilson, D.K.1
  • 31
    • 0037009163 scopus 로고    scopus 로고
    • Interactions among adenosine deaminase, adenosine A1 receptors and dopamine D(1) receptors in stably cotransfected fibroblast cells and neurons
    • Torvinen M., et al. Interactions among adenosine deaminase, adenosine A1 receptors and dopamine D(1) receptors in stably cotransfected fibroblast cells and neurons. Neuroscience. 113:2002;709-719.
    • (2002) Neuroscience , vol.113 , pp. 709-719
    • Torvinen, M.1
  • 32
    • 0037150272 scopus 로고    scopus 로고
    • On the regulatory role of dipeptidyl peptidase IV (MCD26Madenosine deaminase complexing protein) on adenosine deaminase activity
    • Ben-Shooshan A., et al. On the regulatory role of dipeptidyl peptidase IV (MCD26Madenosine deaminase complexing protein) on adenosine deaminase activity. Biochim. Biophys. Acta. 1587:2002;21-30.
    • (2002) Biochim. Biophys. Acta , vol.1587 , pp. 21-30
    • Ben-Shooshan, A.1
  • 33
    • 0029963151 scopus 로고    scopus 로고
    • The cluster-arranged cooperative model: A model that accounts for the kinetics of binding to A1 adenosine receptors
    • Franco R., et al. The cluster-arranged cooperative model: a model that accounts for the kinetics of binding to A1 adenosine receptors. Biochemistry. 35:1996;3007-3015.
    • (1996) Biochemistry , vol.35 , pp. 3007-3015
    • Franco, R.1
  • 34
    • 0030729833 scopus 로고    scopus 로고
    • Ligand-induced phosphorylation, clustering and desensitization of A1 adenosine receptors
    • Ciruela F., et al. Ligand-induced phosphorylation, clustering and desensitization of A1 adenosine receptors. Mol. Pharmacol. 52:1997;788-797.
    • (1997) Mol. Pharmacol. , vol.52 , pp. 788-797
    • Ciruela, F.1
  • 35
    • 0037124032 scopus 로고    scopus 로고
    • Coaggregation, cointernalization, and codesensitization of adenosine A2A receptors and dopamine D2 receptors
    • Hillion J., et al. Coaggregation, cointernalization, and codesensitization of adenosine A2A receptors and dopamine D2 receptors. J. Biol. Chem. 277:2002;18091-18097.
    • (2002) J. Biol. Chem. , vol.277 , pp. 18091-18097
    • Hillion, J.1
  • 36
    • 0033975265 scopus 로고    scopus 로고
    • Hierarchical neuronal modeling of cognitive functions: From synaptic transmission to the Tower of London
    • Changeaux J.-P., Dehaene S. Hierarchical neuronal modeling of cognitive functions: from synaptic transmission to the Tower of London. Int. J. Psychophysiol. 35:2000;179-187.
    • (2000) Int. J. Psychophysiol. , vol.35 , pp. 179-187
    • Changeaux, J.-P.1    Dehaene, S.2
  • 37
    • 0026040285 scopus 로고
    • Adenosine receptors in myelin fractions and subfractions: The effect of the agonist (R)-phenylisopropyladenosine on lyelin membrane microvscosity
    • Casadó V., et al. Adenosine receptors in myelin fractions and subfractions: the effect of the agonist (R)-phenylisopropyladenosine on lyelin membrane microvscosity. J. Neurochem. 57:1991;1623-1629.
    • (1991) J. Neurochem. , vol.57 , pp. 1623-1629
    • Casadó, V.1
  • 38
    • 0024797710 scopus 로고
    • Adenosine, a cytoprotective autacoid: Effects of adenosine on neutrophil plasma membrane microviscosity and chemoattractant receptor display
    • Cronstein B.N., et al. Adenosine, a cytoprotective autacoid: effects of adenosine on neutrophil plasma membrane microviscosity and chemoattractant receptor display. Biochim. Biophys. Acta. 987:1989;176-180.
    • (1989) Biochim. Biophys. Acta , vol.987 , pp. 176-180
    • Cronstein, B.N.1
  • 39
    • 0041524715 scopus 로고    scopus 로고
    • Molecular basis of learning and memory: Modelling based on receptor mosaics
    • B. Apolloni, & F. Kurfess. Kluwer Academic Publisher
    • Agnati L.F., et al. Molecular basis of learning and memory: modelling based on receptor mosaics. Apolloni B., Kurfess F. From Synapses to Rules: Discovering Symbolic Rules from Neural Processed Data. 2002;Kluwer Academic Publisher.
    • (2002) From Synapses to Rules: Discovering Symbolic Rules from Neural Processed Data
    • Agnati, L.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.