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Volumn 74, Issue 2-3, 2003, Pages 217-224

Mechanisms regulating membrane trafficking of G protein-coupled receptors in the endocytic pathway

Author keywords

Desensitization; Down regulation; Endocytosis; G protein; Sorting

Indexed keywords

BETA 2 ADRENERGIC RECEPTOR; G PROTEIN COUPLED RECEPTOR; RHODOPSIN;

EID: 0242384217     PISSN: 00243205     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.lfs.2003.09.008     Document Type: Conference Paper
Times cited : (153)

References (43)
  • 3
    • 0344310763 scopus 로고    scopus 로고
    • Mechanisms of beta-adrenergic receptor desensitization and resensitization
    • Lefkowitz R.J., Pitcher J., Krueger K., Daaka Y. Mechanisms of beta-adrenergic receptor desensitization and resensitization. Advances in Pharmacology. 42:1998;416-420.
    • (1998) Advances in Pharmacology , vol.42 , pp. 416-420
    • Lefkowitz, R.J.1    Pitcher, J.2    Krueger, K.3    Daaka, Y.4
  • 4
    • 0032571340 scopus 로고    scopus 로고
    • Molecular mechanisms of G protein-coupled receptor desensitization and resensitization
    • Ferguson S.S., Zhang J., Barak L.S., Caron M.G. Molecular mechanisms of G protein-coupled receptor desensitization and resensitization. Life Sci. 62:1998;1561-1565.
    • (1998) Life Sci. , vol.62 , pp. 1561-1565
    • Ferguson, S.S.1    Zhang, J.2    Barak, L.S.3    Caron, M.G.4
  • 6
    • 0020339975 scopus 로고
    • Rapid and reversible disappearance of beta-adrenergic cell surface receptors
    • Staehelin M., Simons P. Rapid and reversible disappearance of beta-adrenergic cell surface receptors. Embo J. 1:1982;187-190.
    • (1982) Embo J. , vol.1 , pp. 187-190
    • Staehelin, M.1    Simons, P.2
  • 8
    • 0031747997 scopus 로고    scopus 로고
    • The role of receptor kinases and arrestins in G protein-coupled receptor regulation
    • Krupnick J.G., Benovic J.L. The role of receptor kinases and arrestins in G protein-coupled receptor regulation. Annual Review of Pharmacology and Toxicology. 38:1998;289-319.
    • (1998) Annual Review of Pharmacology and Toxicology , vol.38 , pp. 289-319
    • Krupnick, J.G.1    Benovic, J.L.2
  • 9
    • 0017396648 scopus 로고
    • Light-induced phosphorylation of rhodopsin in cattle photoreceptor membranes: Substrate activation and inactivation
    • McDowell J.H., Kuhn H. Light-induced phosphorylation of rhodopsin in cattle photoreceptor membranes: substrate activation and inactivation. Biochemistry. 16:1977;4054-4060.
    • (1977) Biochemistry , vol.16 , pp. 4054-4060
    • McDowell, J.H.1    Kuhn, H.2
  • 10
    • 0023841528 scopus 로고
    • Inactivation of photoexcited rhodopsin in retinal rods: The roles of rhodopsin kinase and 48-kDa protein (arrestin)
    • Bennett N., Sitaramayya A. Inactivation of photoexcited rhodopsin in retinal rods: the roles of rhodopsin kinase and 48-kDa protein (arrestin). Biochemistry. 27:1988;1710-1715.
    • (1988) Biochemistry , vol.27 , pp. 1710-1715
    • Bennett, N.1    Sitaramayya, A.2
  • 11
    • 0021925095 scopus 로고
    • Homologous desensitization of adenylate cyclase is associated with phosphorylation of the beta-adrenergic receptor
    • Sibley D.R., Strasser R.H., Caron M.G., Lefkowitz R.J. Homologous desensitization of adenylate cyclase is associated with phosphorylation of the beta-adrenergic receptor. J. Biol. Chem. 260:1985;3883-3886.
    • (1985) J. Biol. Chem. , vol.260 , pp. 3883-3886
    • Sibley, D.R.1    Strasser, R.H.2    Caron, M.G.3    Lefkowitz, R.J.4
  • 12
    • 0344812247 scopus 로고
    • Beta-adrenergic receptor kinase: Identification of a novel protein kinase that phosphorylates the agonist-occupied form of the receptor
    • Benovic J.L., Strasser R.H., Caron M.G., Lefkowitz R.J. Beta-adrenergic receptor kinase: identification of a novel protein kinase that phosphorylates the agonist-occupied form of the receptor. Proc. Natl. Acad. Sci. USA. 83:1986;2797-2801.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 2797-2801
    • Benovic, J.L.1    Strasser, R.H.2    Caron, M.G.3    Lefkowitz, R.J.4
  • 13
    • 0025845424 scopus 로고
    • CDNA cloning and chromosomal localization of the human beta-adrenergic receptor kinase
    • Benovic J.L., Stone W.C., Huebner K., Croce C., Caron M.G., Lefkowitz R.J. cDNA cloning and chromosomal localization of the human beta-adrenergic receptor kinase. FEBS Lett. 283:1991;122-126.
    • (1991) FEBS Lett. , vol.283 , pp. 122-126
    • Benovic, J.L.1    Stone, W.C.2    Huebner, K.3    Croce, C.4    Caron, M.G.5    Lefkowitz, R.J.6
  • 14
    • 0025352299 scopus 로고
    • Beta-Arrestin: A protein that regulates beta-adrenergic receptor function
    • Lohse M.J., Benovic J.L., Codina J., Caron M.G., Lefkowitz R.J. beta-Arrestin: a protein that regulates beta-adrenergic receptor function. Science. 248:1990;1547-1550.
    • (1990) Science , vol.248 , pp. 1547-1550
    • Lohse, M.J.1    Benovic, J.L.2    Codina, J.3    Caron, M.G.4    Lefkowitz, R.J.5
  • 15
    • 0023515309 scopus 로고
    • Functional desensitization of the isolated beta-adrenergic receptor by the beta-adrenergic receptor kinase: Potential role of an analog of the retinal protein arrestin (48-kDa protein)
    • Benovic J.L., Kuhn H., Weyand I., Codina J., Caron M.G., Lefkowitz R.J. Functional desensitization of the isolated beta-adrenergic receptor by the beta-adrenergic receptor kinase: potential role of an analog of the retinal protein arrestin (48-kDa protein). Proc. Natl. Acad. Sci. USA. 84:1987;8879-8882.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 8879-8882
    • Benovic, J.L.1    Kuhn, H.2    Weyand, I.3    Codina, J.4    Caron, M.G.5    Lefkowitz, R.J.6
  • 16
    • 0031015458 scopus 로고    scopus 로고
    • Mechanism of phosphorylation-recognition by visual arrestin and the transition of arrestin into a high affinity binding state
    • Gurevich V.V., Benovic J.L. Mechanism of phosphorylation-recognition by visual arrestin and the transition of arrestin into a high affinity binding state. Mol. Pharmacol. 51:1997;161-169.
    • (1997) Mol. Pharmacol. , vol.51 , pp. 161-169
    • Gurevich, V.V.1    Benovic, J.L.2
  • 17
    • 0021321393 scopus 로고
    • Agonist-induced changes in beta-adrenergic receptors on intact cells
    • Toews M.L., Perkins J.P. Agonist-induced changes in beta-adrenergic receptors on intact cells. J. Biol. Chem. 259:1984;2227-2235.
    • (1984) J. Biol. Chem. , vol.259 , pp. 2227-2235
    • Toews, M.L.1    Perkins, J.P.2
  • 18
    • 0026662535 scopus 로고
    • Ligand-regulated internalization and recycling of human beta 2-adrenergic receptors between the plasma membrane and endosomes containing transferrin receptors
    • von Zastrow M., Kobilka B.K. Ligand-regulated internalization and recycling of human beta 2-adrenergic receptors between the plasma membrane and endosomes containing transferrin receptors. J. Biol. Chem. 267:1992;3530-3538.
    • (1992) J. Biol. Chem. , vol.267 , pp. 3530-3538
    • Von Zastrow, M.1    Kobilka, B.K.2
  • 19
    • 0026573774 scopus 로고
    • Isoproterenol-initiated beta-adrenergic receptor diacytosis in cultured cells
    • Kurz J.B., Perkins J.P. Isoproterenol-initiated beta-adrenergic receptor diacytosis in cultured cells. Mol. Pharmacol. 41:1992;375-381.
    • (1992) Mol. Pharmacol. , vol.41 , pp. 375-381
    • Kurz, J.B.1    Perkins, J.P.2
  • 21
    • 0028238350 scopus 로고
    • Antagonist -dependent and -independent steps in the mechanism of adrenergic receptor internalization
    • von Zastrow M., Kobilka B.K. Antagonist -dependent and -independent steps in the mechanism of adrenergic receptor internalization. J. Biol. Chem. 269:1994;18448-18452.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18448-18452
    • Von Zastrow, M.1    Kobilka, B.K.2
  • 24
    • 0029780757 scopus 로고    scopus 로고
    • Dynamin and beta-arrestin reveal distinct mechanisms for G protein-coupled receptor internalization
    • Zhang J., Ferguson S., Barak L.S., Menard L., Caron M.G. Dynamin and beta-arrestin reveal distinct mechanisms for G protein-coupled receptor internalization. J. Biol. Chem. 271:1996;18302-18305.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18302-18305
    • Zhang, J.1    Ferguson, S.2    Barak, L.S.3    Menard, L.4    Caron, M.G.5
  • 25
    • 0032544735 scopus 로고    scopus 로고
    • Regulated endocytosis of G protein-coupled receptors by a biochemically and functionally distinct subpopulation of clathrin-coated pits
    • Cao T.C., Mays R.W., von Zastrow M. Regulated endocytosis of G protein-coupled receptors by a biochemically and functionally distinct subpopulation of clathrin-coated pits. J. Biol. Chem. 273:1998;24592-24602.
    • (1998) J. Biol. Chem. , vol.273 , pp. 24592-24602
    • Cao, T.C.1    Mays, R.W.2    Von Zastrow, M.3
  • 27
    • 0034725650 scopus 로고    scopus 로고
    • The interaction of beta-arrestin with the AP-2 adaptor is required for the clustering of beta 2-adrenergic receptor into clathrin-coated pits
    • Laporte S.A., Oakley R.H., Holt J.A., Barak L.S., Caron M.G. The interaction of beta-arrestin with the AP-2 adaptor is required for the clustering of beta 2-adrenergic receptor into clathrin-coated pits. J. Biol. Chem. 275:2000;23120-23126.
    • (2000) J. Biol. Chem. , vol.275 , pp. 23120-23126
    • Laporte, S.A.1    Oakley, R.H.2    Holt, J.A.3    Barak, L.S.4    Caron, M.G.5
  • 28
    • 0032557450 scopus 로고    scopus 로고
    • Arrestin-independent internalization of the m1, m3, and m4 subtypes of muscarinic cholinergic receptors
    • Lee K.B., Pals R.R., Benovic J.L., Hosey M.M. Arrestin-independent internalization of the m1, m3, and m4 subtypes of muscarinic cholinergic receptors. J. Biol. Chem. 273:1998;12967-12972.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12967-12972
    • Lee, K.B.1    Pals, R.R.2    Benovic, J.L.3    Hosey, M.M.4
  • 30
    • 0029804995 scopus 로고    scopus 로고
    • Agonist-induced functional desensitization of the mu-opioid receptor is mediated by loss of membrane receptors rather than uncoupling from G protein
    • Pak Y., Kouvelas A., Scheideler M.A., Rasmussen J., O'Dowd B.F., George S.R. Agonist-induced functional desensitization of the mu-opioid receptor is mediated by loss of membrane receptors rather than uncoupling from G protein. Molecular Pharmacology. 50:1996;1214-1222.
    • (1996) Molecular Pharmacology , vol.50 , pp. 1214-1222
    • Pak, Y.1    Kouvelas, A.2    Scheideler, M.A.3    Rasmussen, J.4    O'Dowd, B.F.5    George, S.R.6
  • 31
    • 0028986859 scopus 로고
    • Sequestration and recycling of beta 2-adrenergic receptors permit receptor resensitization
    • Pippig S., Andexinger S., Lohse M.J. Sequestration and recycling of beta 2-adrenergic receptors permit receptor resensitization. Mol. Pharmacol. 47:1995;666-676.
    • (1995) Mol. Pharmacol. , vol.47 , pp. 666-676
    • Pippig, S.1    Andexinger, S.2    Lohse, M.J.3
  • 32
    • 0027528961 scopus 로고
    • Overexpression of beta-arrestin and beta-adrenergic receptor kinase augment desensitization of beta 2-adrenergic receptors
    • Pippig S., Andexinger S., Daniel K., Puzicha M., Caron M.G., Lefkowitz R.J., Lohse M.J. Overexpression of beta-arrestin and beta-adrenergic receptor kinase augment desensitization of beta 2-adrenergic receptors. J. Biol. Chem. 268:1993;3201-3208.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3201-3208
    • Pippig, S.1    Andexinger, S.2    Daniel, K.3    Puzicha, M.4    Caron, M.G.5    Lefkowitz, R.J.6    Lohse, M.J.7
  • 33
    • 0027404263 scopus 로고
    • Beta-adrenergic receptor sequestration. A potential mechanism of receptor resensitization
    • Yu S.S., Lefkowitz R.J., Hausdorff W.P. Beta-adrenergic receptor sequestration. A potential mechanism of receptor resensitization. J. Biol. Chem. 268:1993;337-341.
    • (1993) J. Biol. Chem. , vol.268 , pp. 337-341
    • Yu, S.S.1    Lefkowitz, R.J.2    Hausdorff, W.P.3
  • 34
    • 0029160524 scopus 로고
    • The G-protein-coupled receptor phosphatase: A protein phosphatase type 2A with a distinct subcellular distribution and substrate specificity
    • Pitcher J.A., Payne E.S., Csortos C., DePaoli R.A., Lefkowitz R.J. The G-protein-coupled receptor phosphatase: a protein phosphatase type 2A with a distinct subcellular distribution and substrate specificity. Proc. Natl. Acad. Sci. USA. 92:1995;8343-8347.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8343-8347
    • Pitcher, J.A.1    Payne, E.S.2    Csortos, C.3    DePaoli, R.A.4    Lefkowitz, R.J.5
  • 35
    • 0035252096 scopus 로고    scopus 로고
    • Role of endocytosis in mediating downregulation of G-protein-coupled receptors
    • Tsao P., Cao T., von Zastrow M. Role of endocytosis in mediating downregulation of G-protein-coupled receptors. Trends Pharmacol. Sci. 22:2001;91-96.
    • (2001) Trends Pharmacol. Sci. , vol.22 , pp. 91-96
    • Tsao, P.1    Cao, T.2    Von Zastrow, M.3
  • 36
    • 0032549568 scopus 로고    scopus 로고
    • Role of clathrin-mediated endocytosis in agonist-induced down-regulation of the beta2-adrenergic receptor
    • Gagnon A.W., Kallal L., Benovic J.L. Role of clathrin-mediated endocytosis in agonist-induced down-regulation of the beta2-adrenergic receptor. Journal of Biological Chemistry. 273:1998;6976-6981.
    • (1998) Journal of Biological Chemistry , vol.273 , pp. 6976-6981
    • Gagnon, A.W.1    Kallal, L.2    Benovic, J.L.3
  • 37
    • 0034646719 scopus 로고    scopus 로고
    • Type-specific sorting of G protein-coupled receptors after endocytosis
    • Tsao P.I., von Zastrow M. Type-specific sorting of G protein-coupled receptors after endocytosis. Journal of Biological Chemistry. 275:2000;11130-11140.
    • (2000) Journal of Biological Chemistry , vol.275 , pp. 11130-11140
    • Tsao, P.I.1    Von Zastrow, M.2
  • 38
    • 0033593210 scopus 로고    scopus 로고
    • The cytoplasmic tails of protease-activated receptor-1 and substance P receptor specify sorting to lysosomes versus recycling
    • Trejo J., Coughlin S.R. The cytoplasmic tails of protease-activated receptor-1 and substance P receptor specify sorting to lysosomes versus recycling. Journal of Biological Chemistry. 274:1999;2216-2224.
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 2216-2224
    • Trejo, J.1    Coughlin, S.R.2
  • 39
    • 0033575916 scopus 로고    scopus 로고
    • A kinase-regulated PDZ-domain interaction controls endocytic sorting of the beta2-adrenergic receptor
    • Cao T.T., Deacon H.W., Reczek D., Bretscher A., von Zastrow M. A kinase-regulated PDZ-domain interaction controls endocytic sorting of the beta2-adrenergic receptor. Nature. 401:1999;286-290.
    • (1999) Nature , vol.401 , pp. 286-290
    • Cao, T.T.1    Deacon, H.W.2    Reczek, D.3    Bretscher, A.4    Von Zastrow, M.5
  • 42
    • 0034689003 scopus 로고    scopus 로고
    • Beta-Arrestin-dependent endocytosis of proteinase-activated receptor 2 is required for intracellular targeting of activated ERK1/2
    • DeFea K.A., Zalevsky J., Thoma M.S., Dery O., Mullins R.D., Bunnett N.W. beta-Arrestin-dependent endocytosis of proteinase-activated receptor 2 is required for intracellular targeting of activated ERK1/2. Journal of Cell Biology. 148:2000;1267-1281.
    • (2000) Journal of Cell Biology , vol.148 , pp. 1267-1281
    • DeFea, K.A.1    Zalevsky, J.2    Thoma, M.S.3    Dery, O.4    Mullins, R.D.5    Bunnett, N.W.6
  • 43
    • 0034737483 scopus 로고    scopus 로고
    • The beta(2)-adrenergic receptor mediates extracellular signal-regulated kinase activation via assembly of a multi-receptor complex with the epidermal growth factor receptor
    • Maudsley S., Pierce K.L., Zamah A.M., Miller W.E., Ahn S., Daaka Y., Lefkowitz R.J., Luttrell L.M. The beta(2)-adrenergic receptor mediates extracellular signal-regulated kinase activation via assembly of a multi-receptor complex with the epidermal growth factor receptor. J. Biol. Chem. 275:2000;9572-9580.
    • (2000) J. Biol. Chem. , vol.275 , pp. 9572-9580
    • Maudsley, S.1    Pierce, K.L.2    Zamah, A.M.3    Miller, W.E.4    Ahn, S.5    Daaka, Y.6    Lefkowitz, R.J.7    Luttrell, L.M.8


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