메뉴 건너뛰기




Volumn 375, Issue 3, 2003, Pages 503-515

Multifaceted roles of β-arrestins in the regulation of seven-membrane-spanning receptor trafficking and signalling

Author keywords

arrestin; Adapter protein; Desensitization; Endocytosis; G protein coupled receptor (GPCR); Seven membrane spanning receptor (7MSR)

Indexed keywords

BIOLOGICAL MEMBRANES; CELLS; CHEMICAL BONDS; CYTOLOGY; PROTEINS;

EID: 0242721361     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20031076     Document Type: Review
Times cited : (346)

References (117)
  • 2
    • 0020909362 scopus 로고
    • Phosphorylation of the β-adrenergic receptor accompanies catecholamine-induced desensitization of turkey erythrocyte adenylate cyclase
    • Stadel, J. M., Nambi, P., Shorr, R. G., Sawyer, D. F., Caron, M. G. and Lefkowitz, R. J. (1983) Phosphorylation of the β-adrenergic receptor accompanies catecholamine-induced desensitization of turkey erythrocyte adenylate cyclase. Trans. Assoc. Am. Physicians 96, 137-145
    • (1983) Trans. Assoc. Am. Physicians , vol.96 , pp. 137-145
    • Stadel, J.M.1    Nambi, P.2    Shorr, R.G.3    Sawyer, D.F.4    Caron, M.G.5    Lefkowitz, R.J.6
  • 3
    • 0021194360 scopus 로고
    • Desensitization of turkey erythrocyte adenylate cyclase. β-Adrenergic receptor phosphorylation is correlated with attenuation of adenylate cyclase activity
    • Sibley, D. R., Peters, J. R., Nambi, P., Caron, M. G. and Lefkowitz, R. J. (1984) Desensitization of turkey erythrocyte adenylate cyclase. β-Adrenergic receptor phosphorylation is correlated with attenuation of adenylate cyclase activity. J. Biol. Chem. 259, 9742-9749
    • (1984) J. Biol. Chem. , vol.259 , pp. 9742-9749
    • Sibley, D.R.1    Peters, J.R.2    Nambi, P.3    Caron, M.G.4    Lefkowitz, R.J.5
  • 4
    • 0032563291 scopus 로고    scopus 로고
    • G protein-coupled receptors. III. New roles for receptor kinases and β-arrestins in receptor signaling and desensitization
    • Lefkowitz, R. J. (1998) G protein-coupled receptors. III. New roles for receptor kinases and β-arrestins in receptor signaling and desensitization. J. Biol. Chem. 273, 18677-18680
    • (1998) J. Biol. Chem. , vol.273 , pp. 18677-18680
    • Lefkowitz, R.J.1
  • 5
    • 0344812247 scopus 로고
    • β-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. and Lefkowitz, R. J. (1986) β-adrenergic receptor kinase: identification of a novel protein kinase that phosphorylates the agonist-occupied form of the receptor. Proc. Natl. Acad. Sci. U.S.A. 83, 2797-2801
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 2797-2801
    • Benovic, J.L.1    Strasser, R.H.2    Caron, M.G.3    Lefkowitz, R.J.4
  • 8
    • 0028030060 scopus 로고
    • Palmitoylation of G protein-coupled receptor kinase, GRK6. Lipid modification diversity in the GRK family
    • Stoffel, R. H., Randall, R. R., Premont, R. T., Lefkowitz, R. J. and Inglese, J. (1994) Palmitoylation of G protein-coupled receptor kinase, GRK6. Lipid modification diversity in the GRK family. J. Biol. Chem. 269, 27791-27794
    • (1994) J. Biol. Chem. , vol.269 , pp. 27791-27794
    • Stoffel, R.H.1    Randall, R.R.2    Premont, R.T.3    Lefkowitz, R.J.4    Inglese, J.5
  • 11
    • 0032541974 scopus 로고    scopus 로고
    • Palmitoylation increases the kinase activity of the G protein-coupled receptor kinase, GRK6
    • Stoffel, R. H., Inglese, J., Macrae, A. D., Lefkowitz, R. J. and Premont, R. T. (1998) Palmitoylation increases the kinase activity of the G protein-coupled receptor kinase, GRK6. Biochemistry 37, 16053-16059
    • (1998) Biochemistry , vol.37 , pp. 16053-16059
    • Stoffel, R.H.1    Inglese, J.2    Macrae, A.D.3    Lefkowitz, R.J.4    Premont, R.T.5
  • 12
    • 0033548663 scopus 로고    scopus 로고
    • Real-time visualization of the cellular redistribution of G protein-coupled receptor kinase 2 and β-arrestin 2 during homologous desensitization of the substance P receptor
    • Barak, L. S., Warabi, K., Feng, X., Caron, M. G. and Kwatra, M. M. (1999) Real-time visualization of the cellular redistribution of G protein-coupled receptor kinase 2 and β-arrestin 2 during homologous desensitization of the substance P receptor. J. Biol. Chem. 274, 7565-7569
    • (1999) J. Biol. Chem. , vol.274 , pp. 7565-7569
    • Barak, L.S.1    Warabi, K.2    Feng, X.3    Caron, M.G.4    Kwatra, M.M.5
  • 13
    • 0035805528 scopus 로고    scopus 로고
    • Regulation of membrane targeting of the G protein-coupled receptor kinase 2 by protein kinase A and its anchoring protein akap79
    • Cong, M., Perry, S. J., Lin, F. T., Fraser, I. D., Hu, L. A., Chen, W., Pitcher, J. A., Scott, J. D. and Lefkowitz, R. J. (2001) Regulation of membrane targeting of the G protein-coupled receptor kinase 2 by protein kinase A and its anchoring protein akap79. J. Biol. Chem. 276, 15192-15199
    • (2001) J. Biol. Chem. , vol.276 , pp. 15192-15199
    • Cong, M.1    Perry, S.J.2    Lin, F.T.3    Fraser, I.D.4    Hu, L.A.5    Chen, W.6    Pitcher, J.A.7    Scott, J.D.8    Lefkowitz, R.J.9
  • 14
    • 0037044197 scopus 로고    scopus 로고
    • Phosphorylation-independent desensitization of G protein-coupled receptors?
    • Pao, C. S. and Benovic, J. L. (2002) Phosphorylation-independent desensitization of G protein-coupled receptors? Sci. STKE 2002, PE42
    • (2002) Sci. STKE , vol.2002
    • Pao, C.S.1    Benovic, J.L.2
  • 15
    • 0030757504 scopus 로고    scopus 로고
    • Phosphorylation and desensitization of human endothelin A and B receptors. Evidence for G protein-coupled receptor kinase specificity
    • Freedman, N. J., Ament, A. S., Oppermann, M., Stoffel, R. H., Exum, S. T. and Lefkowitz, R. J. (1997) Phosphorylation and desensitization of human endothelin A and B receptors. Evidence for G protein-coupled receptor kinase specificity. J. Biol. Chem. 272, 17734-17743
    • (1997) J. Biol. Chem. , vol.272 , pp. 17734-17743
    • Freedman, N.J.1    Ament, A.S.2    Oppermann, M.3    Stoffel, R.H.4    Exum, S.T.5    Lefkowitz, R.J.6
  • 16
    • 0037067705 scopus 로고    scopus 로고
    • Phosphorylation-independent regulation of metabotropic glutamate receptor signaling by G protein-coupled receptor kinase 2
    • Dhami, G. K., Anborgh, P. H., Dale, L. B., Sterne-Marr, R. and Ferguson, S. S. (2002) Phosphorylation-independent regulation of metabotropic glutamate receptor signaling by G protein-coupled receptor kinase 2. J. Biol. Chem. 277, 25266-25272
    • (2002) J. Biol. Chem. , vol.277 , pp. 25266-25272
    • Dhami, G.K.1    Anborgh, P.H.2    Dale, L.B.3    Sterne-Marr, R.4    Ferguson, S.S.5
  • 17
    • 0037799206 scopus 로고    scopus 로고
    • Keeping G proteins at bay: A complex between G protein-coupled receptor kinase 2 and Gβγ
    • Lodowski, D. T., Pitcher, J. A., Capel, W. D., Lefkowitz, R. J. and Tesmer, J. J. (2003) Keeping G proteins at bay: a complex between G protein-coupled receptor kinase 2 and Gβγ. Science 300, 1256-1262
    • (2003) Science , vol.300 , pp. 1256-1262
    • Lodowski, D.T.1    Pitcher, J.A.2    Capel, W.D.3    Lefkowitz, R.J.4    Tesmer, J.J.5
  • 18
    • 0023515309 scopus 로고
    • Functional desensitization of the isolated β-adrenergic receptor by the β-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. and Lefkowitz, R. J. (1987) Functional desensitization of the isolated β-adrenergic receptor by the β-adrenergic receptor kinase: potential role of an analog of the retinal protein arrestin (48-kDa protein). Proc. Natl. Acad. Sci. U.S.A. 84, 8879-8882
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , 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
  • 19
    • 0025352299 scopus 로고
    • β-Arrestin: A protein that regulates β-adrenergic receptor function
    • Lohse, M. J., Benovic, J. L., Codina, J., Caron, M. G. and Lefkowitz, R. J. (1990) β-Arrestin: a protein that regulates β-adrenergic receptor function. Science 248, 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
  • 21
    • 0027939554 scopus 로고
    • Cone arrestin identified by targeting expression of a functional family
    • Craft, C. M., Whitmore, D. H. and Wiechmann, A. F. (1994) Cone arrestin identified by targeting expression of a functional family. J. Biol. Chem. 269, 4613-4619
    • (1994) J. Biol. Chem. , vol.269 , pp. 4613-4619
    • Craft, C.M.1    Whitmore, D.H.2    Wiechmann, A.F.3
  • 25
    • 0037016682 scopus 로고    scopus 로고
    • The association of arrestin-3 with the human lutropin/choriogonadotropin receptor depends mostly on receptor activation rather than on receptor phosphorylation
    • Min, L., Galet, C. and Ascoli, M. (2002) The association of arrestin-3 with the human lutropin/choriogonadotropin receptor depends mostly on receptor activation rather than on receptor phosphorylation. J. Biol. Chem. 277, 702-710
    • (2002) J. Biol. Chem. , vol.277 , pp. 702-710
    • Min, L.1    Galet, C.2    Ascoli, M.3
  • 26
    • 0034795335 scopus 로고    scopus 로고
    • Association of β-Arrestin1 with the type 1A angiotensin II receptor involves phosphorylation of the receptor carboxyl terminus and correlates with receptor internalization
    • Qian, H., Pipolo, L. and Thomas, W. G. (2001) Association of β-Arrestin1 with the type 1A angiotensin II receptor involves phosphorylation of the receptor carboxyl terminus and correlates with receptor internalization. Mol. Endocrinol. 15, 1706-1719
    • (2001) Mol. Endocrinol. , vol.15 , pp. 1706-1719
    • Qian, H.1    Pipolo, L.2    Thomas, W.G.3
  • 27
    • 0037737763 scopus 로고    scopus 로고
    • Trafficking patterns of β-arrestin and G protein-coupled receptors determined by the kinetics of β-arrestin deubiquitination
    • Shenoy, S. K. and Lefkowitz, R. J. (2003) Trafficking patterns of β-arrestin and G protein-coupled receptors determined by the kinetics of β-arrestin deubiquitination. J. Biol. Chem. 278, 14498-14506
    • (2003) J. Biol. Chem. , vol.278 , pp. 14498-14506
    • Shenoy, S.K.1    Lefkowitz, R.J.2
  • 28
    • 0030736417 scopus 로고    scopus 로고
    • A β-arrestin/green fluorescent protein biosensor for detecting G protein-coupled receptor activation
    • Barak, L. S., Ferguson, S. S., Zhang, J. and Caron, M. G. (1997) A β-arrestin/green fluorescent protein biosensor for detecting G protein-coupled receptor activation. J. Biol. Chem. 272, 27497-27500
    • (1997) J. Biol. Chem. , vol.272 , pp. 27497-27500
    • Barak, L.S.1    Ferguson, S.S.2    Zhang, J.3    Caron, M.G.4
  • 31
    • 0033527663 scopus 로고    scopus 로고
    • Association of β-arrestin with G protein-coupled receptors during clathrin-mediated endocytosis dictates the profile of receptor resensitization
    • Oakley, R. H., Laporte, S. A., Holt, J. A., Barak, L. S. and Caron, M. G. (1999) Association of β-arrestin with G protein-coupled receptors during clathrin-mediated endocytosis dictates the profile of receptor resensitization. J. Biol. Chem. 274, 32248-32257
    • (1999) J. Biol. Chem. , vol.274 , pp. 32248-32257
    • Oakley, R.H.1    Laporte, S.A.2    Holt, J.A.3    Barak, L.S.4    Caron, M.G.5
  • 32
    • 0033548433 scopus 로고    scopus 로고
    • Targeted construction of phosphorylation-independent β-arrestin mutants with constitutive activity in cells
    • Kovoor, A., Celver, J., Abdryashitov, R. I., Chavkin, C. and Gurevich, V. V. (1999) Targeted construction of phosphorylation-independent β-arrestin mutants with constitutive activity in cells. J. Biol. Chem. 274, 6831-6834
    • (1999) J. Biol. Chem. , vol.274 , pp. 6831-6834
    • Kovoor, A.1    Celver, J.2    Abdryashitov, R.I.3    Chavkin, C.4    Gurevich, V.V.5
  • 34
    • 0033582296 scopus 로고    scopus 로고
    • A direct role for arrestins in desensitization of the luteinizing hormone/choriogonadotropin receptor in porcine ovarian follicular membranes
    • Mukherjee, S., Palczewski, K., Gurevich, V., Benovic, J. L., Banga, J. P. and Hunzicker-Dunn, M. (1999) A direct role for arrestins in desensitization of the luteinizing hormone/choriogonadotropin receptor in porcine ovarian follicular membranes. Proc. Natl. Acad. Sci. U.S.A. 96, 493-498
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 493-498
    • Mukherjee, S.1    Palczewski, K.2    Gurevich, V.3    Benovic, J.L.4    Banga, J.P.5    Hunzicker-Dunn, M.6
  • 35
    • 0037452623 scopus 로고    scopus 로고
    • Desensitization, internalization, and signaling functions of β-arrestins demonstrated by RNA interference
    • Ahn, S., Nelson, C. D., Garrison, T. R., Miller, W. E. and Lefkowitz, R. J. (2003) Desensitization, internalization, and signaling functions of β-arrestins demonstrated by RNA interference. Proc. Natl. Acad. Sci. U.S.A. 100, 1740-1744
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 1740-1744
    • Ahn, S.1    Nelson, C.D.2    Garrison, T.R.3    Miller, W.E.4    Lefkowitz, R.J.5
  • 36
    • 0033529339 scopus 로고    scopus 로고
    • Characterization of G protein-coupled receptor regulation in antisense mRNA-expressing cells with reduced arrestin levels
    • Mundell, S. J., Loudon, R. P. and Benovic, J. L. (1999) Characterization of G protein-coupled receptor regulation in antisense mRNA-expressing cells with reduced arrestin levels. Biochemistry 38, 8723-8732
    • (1999) Biochemistry , vol.38 , pp. 8723-8732
    • Mundell, S.J.1    Loudon, R.P.2    Benovic, J.L.3
  • 37
    • 0035852697 scopus 로고    scopus 로고
    • β-Arrestin1 and 2 differentially regulate heptahelical receptor signaling and trafficking
    • Kohout, T. A., Lin, F. S., Perry, S. J., Conner, D. A. and Lefkowitz, R. J. (2001) β-Arrestin1 and 2 differentially regulate heptahelical receptor signaling and trafficking. Proc. Natl. Acad. Sci. U.S.A. 98, 1601-1606
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 1601-1606
    • Kohout, T.A.1    Lin, F.S.2    Perry, S.J.3    Conner, D.A.4    Lefkowitz, R.J.5
  • 38
    • 0037059795 scopus 로고    scopus 로고
    • β-Arrestins regulate protease-activated receptor-1 desensitization but not internalization or down-regulation
    • Paing, M. M., Stutts, A. B., Kohout, T. A., Lefkowitz, R. J. and Trejo, J. (2002) β-Arrestins regulate protease-activated receptor-1 desensitization but not internalization or down-regulation. J. Biol. Chem. 277, 1292-1300
    • (2002) J. Biol. Chem. , vol.277 , pp. 1292-1300
    • Paing, M.M.1    Stutts, A.B.2    Kohout, T.A.3    Lefkowitz, R.J.4    Trejo, J.5
  • 40
    • 0030732503 scopus 로고    scopus 로고
    • β-Arrestin1 knockout mice appear normal but demonstrate altered cardiac responses to β-adrenergic stimulation
    • Conner, D. A., Mathier, M. A., Mortensen, R. M., Christe, M., Vatner, S. F., Seidman, C. E. and Seidman, J. G. (1997) β-Arrestin1 knockout mice appear normal but demonstrate altered cardiac responses to β-adrenergic stimulation. Circ. Res. 81, 1021-1026
    • (1997) Circ. Res. , vol.81 , pp. 1021-1026
    • Conner, D.A.1    Mathier, M.A.2    Mortensen, R.M.3    Christe, M.4    Vatner, S.F.5    Seidman, C.E.6    Seidman, J.G.7
  • 42
    • 0034619796 scopus 로고    scopus 로고
    • Mu-opioid receptor desensitization by β-arrestin-2 determines morphine tolerance but not dependence
    • Bohn, L. M., Gainetdinov, R. R., Lin, F. T., Lefkowitz, R. J. and Caron, M. G. (2000) Mu-opioid receptor desensitization by β-arrestin-2 determines morphine tolerance but not dependence. Nature (London) 408, 720-723
    • (2000) Nature (London) , vol.408 , pp. 720-723
    • Bohn, L.M.1    Gainetdinov, R.R.2    Lin, F.T.3    Lefkowitz, R.J.4    Caron, M.G.5
  • 43
    • 0344310763 scopus 로고    scopus 로고
    • Mechanisms of β-adrenergic receptor desensitization and resensitization
    • Lefkowitz, R. J., Pitcher, J., Krueger, K. and Daaka, Y. (1998) Mechanisms of β-adrenergic receptor desensitization and resensitization. Adv. Pharmacol. 42, 416-420
    • (1998) Adv. Pharmacol. , vol.42 , pp. 416-420
    • Lefkowitz, R.J.1    Pitcher, J.2    Krueger, K.3    Daaka, Y.4
  • 47
    • 0036209874 scopus 로고    scopus 로고
    • Endocytosis of G protein-coupled receptors: Roles of G protein-coupled receptor kinases and β-arrestin proteins
    • Claing, A., Laporte, S. A., Caron, M. G. and Lefkowitz, R. J. (2002) Endocytosis of G protein-coupled receptors: roles of G protein-coupled receptor kinases and β-arrestin proteins. Prog. Neurobiol. 66, 61-79
    • (2002) Prog. Neurobiol. , vol.66 , pp. 61-79
    • Claing, A.1    Laporte, S.A.2    Caron, M.G.3    Lefkowitz, R.J.4
  • 48
    • 0026662535 scopus 로고
    • 2-adrenergic receptors between the plasma membrane and endosomes containing transferrin receptors
    • 2-adrenergic receptors between the plasma membrane and endosomes containing transferrin receptors. J. Biol. Chem. 267, 3530-3538
    • (1992) J. Biol. Chem. , vol.267 , pp. 3530-3538
    • Von Zastrow, M.1    Kobilka, B.K.2
  • 49
    • 0030593035 scopus 로고    scopus 로고
    • Role of β-arrestin in mediating agonist-promoted G protein-coupled receptor internalization
    • Ferguson, S. S., Downey, III, W. E., Colapietro, A. M., Barak, L. S., Menard, L. and Caron, M. G. (1996) Role of β-arrestin in mediating agonist-promoted G protein-coupled receptor internalization. Science 271, 363-366
    • (1996) Science , vol.271 , pp. 363-366
    • Ferguson, S.S.1    Downey III, W.E.2    Colapietro, A.M.3    Barak, L.S.4    Menard, L.5    Caron, M.G.6
  • 51
    • 12644259509 scopus 로고    scopus 로고
    • Arrestin/clathrin interaction. Localization of the arrestin binding locus to the clathrin terminal domain
    • Goodman, Jr, O. B., Krupnick, J. G., Gurevich, V. V., Benovic, J. L. and Keen, J. H. (1997) Arrestin/clathrin interaction. Localization of the arrestin binding locus to the clathrin terminal domain. J. Biol. Chem. 272, 15017-15022
    • (1997) J. Biol. Chem. , vol.272 , pp. 15017-15022
    • Goodman Jr., O.B.1    Krupnick, J.G.2    Gurevich, V.V.3    Benovic, J.L.4    Keen, J.H.5
  • 52
    • 0030967614 scopus 로고    scopus 로고
    • Arrestin/clathrin interaction. Localization of the clathrin binding domain of nonvisual arrestins to the carboxy terminus
    • Krupnick, J. G., Goodman, Jr, O. B., Keen, J. H. and Benovic, J. L. (1997) Arrestin/clathrin interaction. Localization of the clathrin binding domain of nonvisual arrestins to the carboxy terminus. J. Biol. Chem. 272, 15011-15016
    • (1997) J. Biol. Chem. , vol.272 , pp. 15011-15016
    • Krupnick, J.G.1    Goodman Jr., O.B.2    Keen, J.H.3    Benovic, J.L.4
  • 55
    • 0033557715 scopus 로고    scopus 로고
    • Arrestin function in G protein-coupled receptor endocytosis requires phosphoinositide binding
    • Gaidarov, I., Krupnick, J. G., Falck, J. R., Benovic, J. L. and Keen, J. H. (1999) Arrestin function in G protein-coupled receptor endocytosis requires phosphoinositide binding. EMBO J. 18, 871-881
    • (1999) EMBO J. , vol.18 , pp. 871-881
    • Gaidarov, I.1    Krupnick, J.G.2    Falck, J.R.3    Benovic, J.L.4    Keen, J.H.5
  • 59
    • 0030680131 scopus 로고    scopus 로고
    • Clathrin-mediated endocytosis of the β-adrenergic receptor is regulated by phosphorylation/dephosphorylation of β-arrestin1
    • Lin, F. T., Krueger, K. M., Kendall, H. E., Daaka, Y., Fredericks, Z. L., Pitcher, J. A. and Lefkowitz, R. J. (1997) Clathrin-mediated endocytosis of the β-adrenergic receptor is regulated by phosphorylation/ dephosphorylation of β-arrestin1. J. Biol. Chem. 272, 31051-31057
    • (1997) J. Biol. Chem. , vol.272 , pp. 31051-31057
    • Lin, F.T.1    Krueger, K.M.2    Kendall, H.E.3    Daaka, Y.4    Fredericks, Z.L.5    Pitcher, J.A.6    Lefkowitz, R.J.7
  • 61
    • 0037053280 scopus 로고    scopus 로고
    • Regulation of arrestin-3 phosphorylation by casein kinase II
    • Kim, Y. M., Barak, L. S., Caron, M. G. and Benovic, J. L. (2002) Regulation of arrestin-3 phosphorylation by casein kinase II. J. Biol. Chem. 277, 16837-16846
    • (2002) J. Biol. Chem. , vol.277 , pp. 16837-16846
    • Kim, Y.M.1    Barak, L.S.2    Caron, M.G.3    Benovic, J.L.4
  • 62
    • 0034595860 scopus 로고    scopus 로고
    • Differential affinities of visual arrestin, β arrestin1, and β arrestin2 for G protein-coupled receptors delineate two major classes of receptors
    • Oakley, R. H., Laporte, S. A., Holt, J. A., Caron, M. G. and Barak, L. S. (2000) Differential affinities of visual arrestin, β arrestin1, and β arrestin2 for G protein-coupled receptors delineate two major classes of receptors. J. Biol. Chem. 275, 17201-17210
    • (2000) J. Biol. Chem. , vol.275 , pp. 17201-17210
    • Oakley, R.H.1    Laporte, S.A.2    Holt, J.A.3    Caron, M.G.4    Barak, L.S.5
  • 63
    • 0035374624 scopus 로고    scopus 로고
    • Molecular determinants underlying the formation of stable intracellular GPCR/β-arrestin complexes following receptor endocytosis
    • Oakley, R. H., Laporte, S. A., Holt, J. A., Barak, L. S. and Caron, M. G. (2001) Molecular determinants underlying the formation of stable intracellular GPCR/β-arrestin complexes following receptor endocytosis. J. Biol. Chem. 276, 19452-19460
    • (2001) J. Biol. Chem. , vol.276 , pp. 19452-19460
    • Oakley, R.H.1    Laporte, S.A.2    Holt, J.A.3    Barak, L.S.4    Caron, M.G.5
  • 65
    • 0030457014 scopus 로고    scopus 로고
    • Ubiquitin-dependent protein degradation
    • Hochstrasser, M. (1996) Ubiquitin-dependent protein degradation. Annu. Rev. Genet. 30, 405-439
    • (1996) Annu. Rev. Genet. , vol.30 , pp. 405-439
    • Hochstrasser, M.1
  • 66
    • 0029353809 scopus 로고
    • Proteolysis. The proteasome: A protein-degrading organelle?
    • Rubin, D. M. and Finley, D. (1995) Proteolysis. The proteasome: a protein-degrading organelle? Curr. Biol. 5, 854-858
    • (1995) Curr. Biol. , vol.5 , pp. 854-858
    • Rubin, D.M.1    Finley, D.2
  • 69
    • 0032954038 scopus 로고    scopus 로고
    • Structural motifs involved in ubiquitin-mediated processing of the NF-κB precursor p105: Roles of the glycine-rich region and a downstream ubiquitination domain
    • Orian, A., Schwartz, A. L., Israel, A., Whiteside, S., Kahana, C. and Ciechanover, A. (1999) Structural motifs involved in ubiquitin-mediated processing of the NF-κB precursor p105: roles of the glycine-rich region and a downstream ubiquitination domain. Mol. Cell. Biol. 19, 3664-3673
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 3664-3673
    • Orian, A.1    Schwartz, A.L.2    Israel, A.3    Whiteside, S.4    Kahana, C.5    Ciechanover, A.6
  • 70
  • 72
    • 0031583962 scopus 로고    scopus 로고
    • Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53
    • 71a Honda, R., Tanaka, H. and Yasuda, H. (1997) Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53. FEBS Lett. 420, 25-27
    • (1997) FEBS Lett. , vol.420 , pp. 25-27
    • Honda, R.1    Tanaka, H.2    Yasuda, H.3
  • 73
    • 0034708458 scopus 로고    scopus 로고
    • Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53
    • 71b Fang, S., Jensen, J. P., Ludwig, R. L., Vousden, K. H. and Weissman, A. M. (2000) Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53. J. Biol. Chem. 275, 8945-8951
    • (2000) J. Biol. Chem. , vol.275 , pp. 8945-8951
    • Fang, S.1    Jensen, J.P.2    Ludwig, R.L.3    Vousden, K.H.4    Weissman, A.M.5
  • 74
    • 0035824563 scopus 로고    scopus 로고
    • Agonist-promoted ubiquitination of the G protein-coupled receptor CXCR4 mediates lysosomal sorting
    • Marchese, A. and Benovic, J. L. (2001) Agonist-promoted ubiquitination of the G protein-coupled receptor CXCR4 mediates lysosomal sorting. J. Biol. Chem. 276, 45509-45512
    • (2001) J. Biol. Chem. , vol.276 , pp. 45509-45512
    • Marchese, A.1    Benovic, J.L.2
  • 75
    • 0035960759 scopus 로고    scopus 로고
    • β-arrestin and Mdm2, unsuspected partners in signaling from the cell surface
    • Strous, G. J. and Schantl, J. A. (2001) β-arrestin and Mdm2, unsuspected partners in signaling from the cell surface. Sci STKE (2001), PE41
    • (2001) Sci STKE , vol.2001
    • Strous, G.J.1    Schantl, J.A.2
  • 76
    • 0032550179 scopus 로고    scopus 로고
    • Cytoplasmic tail phosphorylation of the α-factor receptor is required for its ubiquitination and internalization
    • Hicke, L., Zanolari, B. and Riezman, H. (1998) Cytoplasmic tail phosphorylation of the α-factor receptor is required for its ubiquitination and internalization. J. Cell Biol. 141, 349-358
    • (1998) J. Cell Biol. , vol.141 , pp. 349-358
    • Hicke, L.1    Zanolari, B.2    Riezman, H.3
  • 77
    • 0031603760 scopus 로고    scopus 로고
    • A function for monoubiquitination in the internalization of a G protein-coupled receptor
    • Terrell, J., Shih, S., Dunn, R. and Hicke, L. (1998) A function for monoubiquitination in the internalization of a G protein-coupled receptor. Mol. Cell 1, 193-202
    • (1998) Mol. Cell , vol.1 , pp. 193-202
    • Terrell, J.1    Shih, S.2    Dunn, R.3    Hicke, L.4
  • 78
    • 0035854827 scopus 로고    scopus 로고
    • Multiple roles for Rsp5p-dependent ubiquitination at the internalization step of endocytosis
    • Dunn, R. and Hicke, L. (2001) Multiple roles for Rsp5p-dependent ubiquitination at the internalization step of endocytosis. J. Biol. Chem. 276, 25974-25981
    • (2001) J. Biol. Chem. , vol.276 , pp. 25974-25981
    • Dunn, R.1    Hicke, L.2
  • 79
    • 0035149694 scopus 로고    scopus 로고
    • Domains of the rsp5 ubiquitin-protein ligase required for receptor-mediated and fluid-phase endocytosis
    • Dunn, R. and Hicke, L. (2001) Domains of the rsp5 ubiquitin-protein ligase required for receptor-mediated and fluid-phase endocytosis. Mol. Biol. Cell 12, 421-435
    • (2001) Mol. Biol. Cell , vol.12 , pp. 421-435
    • Dunn, R.1    Hicke, L.2
  • 80
    • 0034677991 scopus 로고    scopus 로고
    • Ubiquitination of the PEST-like endocytosis signal of the yeast a-factor receptor
    • Roth, A. F. and Davis, N. G. (2000) Ubiquitination of the PEST-like endocytosis signal of the yeast a-factor receptor. J. Biol. Chem. 275, 8143-8153
    • (2000) J. Biol. Chem. , vol.275 , pp. 8143-8153
    • Roth, A.F.1    Davis, N.G.2
  • 81
    • 0036333651 scopus 로고    scopus 로고
    • Insulin induces heterologous desensitization of G-protein-coupled receptor and insulin-like growth factor I signaling by downregulating β-arrestin-1
    • Dalle, S., Imamura, T., Rose, D. W., Worrall, D. S., Ugi, S., Hupfeld, C. J. and Olefsky, J. M. (2002) Insulin induces heterologous desensitization of G-protein-coupled receptor and insulin-like growth factor I signaling by downregulating β-arrestin-1. Mol. Cell. Biol. 22, 6272-6285
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6272-6285
    • Dalle, S.1    Imamura, T.2    Rose, D.W.3    Worrall, D.S.4    Ugi, S.5    Hupfeld, C.J.6    Olefsky, J.M.7
  • 83
    • 0033610892 scopus 로고    scopus 로고
    • β-arrestins regulate mitogenic signaling and clathrin-mediated endocytosis of the insulin-like growth factor I receptor
    • Lin, F. T., Daaka, Y. and Lefkowitz, R. J. (1998) β-arrestins regulate mitogenic signaling and clathrin-mediated endocytosis of the insulin-like growth factor I receptor. J. Biol. Chem. 273, 31640-31643
    • (1998) J. Biol. Chem. , vol.273 , pp. 31640-31643
    • Lin, F.T.1    Daaka, Y.2    Lefkowitz, R.J.3
  • 84
    • 0035909783 scopus 로고    scopus 로고
    • β-Arrestin1 modulates lymphoid enhancer factor transcriptional activity through interaction with phosphorylated dishevelled proteins
    • Chen, W., Hu, L. A., Semenov, M. V., Yanagawa, S., Kikuchi, A., Lefkowitz, R. J. and Miller, W. E. (2001) β-Arrestin1 modulates lymphoid enhancer factor transcriptional activity through interaction with phosphorylated dishevelled proteins. Proc. Natl. Acad. Sci. U.S.A. 98, 14889-14894
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 14889-14894
    • Chen, W.1    Hu, L.A.2    Semenov, M.V.3    Yanagawa, S.4    Kikuchi, A.5    Lefkowitz, R.J.6    Miller, W.E.7
  • 86
    • 0032938716 scopus 로고    scopus 로고
    • Regulation of tyrosine kinase cascades by G-protein-coupled receptors
    • Luttrell, L. M., Daaka, Y. and Lefkowitz, R. J. (1999) Regulation of tyrosine kinase cascades by G-protein-coupled receptors. Curr. Opin. Cell Biol. 11, 177-183
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 177-183
    • Luttrell, L.M.1    Daaka, Y.2    Lefkowitz, R.J.3
  • 87
    • 0034646687 scopus 로고    scopus 로고
    • β-arrestin1 interacts with the catalytic domain of the tyrosine kinase c-SRC. Role of βarrestin1-dependent targeting of c-SRC in receptor endocytosis
    • Miller, W. E., Maudsley, S., Ahn, S., Khan, K. D., Luttrell, L. M. and Lefkowitz, R. J. (2000) β-arrestin1 interacts with the catalytic domain of the tyrosine kinase c-SRC. Role of βarrestin1-dependent targeting of c-SRC in receptor endocytosis. J. Biol. Chem. 275, 11312-11319
    • (2000) J. Biol. Chem. , vol.275 , pp. 11312-11319
    • Miller, W.E.1    Maudsley, S.2    Ahn, S.3    Khan, K.D.4    Luttrell, L.M.5    Lefkowitz, R.J.6
  • 89
    • 0034718604 scopus 로고    scopus 로고
    • The proliferative and antiapoptotic effects of substance P are facilitated by formation of a β-arrestin-dependent scaffolding complex
    • DeFea, K. A., Vaughn, Z. D., O'Bryan, E. M., Nishijima, D., Dery, O. and Bunnett, N. W. (2000) The proliferative and antiapoptotic effects of substance P are facilitated by formation of a β-arrestin-dependent scaffolding complex. Proc. Natl. Acad. Sci. U.S.A. 97, 11086-11091
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 11086-11091
    • DeFea, K.A.1    Vaughn, Z.D.2    O'Bryan, E.M.3    Nishijima, D.4    Dery, O.5    Bunnett, N.W.6
  • 90
  • 92
    • 0035195491 scopus 로고    scopus 로고
    • The Ste5p scaffold
    • Elion, E. A. (2001) The Ste5p scaffold. J. Cell Sci. 114, 3967-3978
    • (2001) J. Cell Sci. , vol.114 , pp. 3967-3978
    • Elion, E.A.1
  • 94
  • 96
    • 0034689003 scopus 로고    scopus 로고
    • β-arrestin-dependent endocytosis of proteinase-activated receptor2 is required for intracellular targeting of activated ERK1/2
    • DeFea, K. A., Zalevsky, J., Thoma, M. S., Dery, O., Mullins, R. D. and Bunnett, N. W. (2000) β-arrestin-dependent endocytosis of proteinase-activated receptor2 is required for intracellular targeting of activated ERK1/2. J. Cell Biol. 148, 1267-1281
    • (2000) J. Cell Biol. , 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
  • 99
    • 0037458614 scopus 로고    scopus 로고
    • The stability of the G protein-coupled receptor-β-arrestin interaction determines the mechanism and functional consequence of ERK activation
    • Tohgo, A., Choy, E. W., Gesty-Palmer, D., Pierce, K. L., Laporte, S., Oakley, R. H., Caron, M. G., Lefkowitz, R. J. and Luttrell, L. M. (2003) The stability of the G protein-coupled receptor-β-arrestin interaction determines the mechanism and functional consequence of ERK activation. J. Biol. Chem. 278, 6258-6267
    • (2003) J. Biol. Chem. , vol.278 , pp. 6258-6267
    • Tohgo, A.1    Choy, E.W.2    Gesty-Palmer, D.3    Pierce, K.L.4    Laporte, S.5    Oakley, R.H.6    Caron, M.G.7    Lefkowitz, R.J.8    Luttrell, L.M.9
  • 100
    • 0033522896 scopus 로고    scopus 로고
    • Feedback regulation of β-arrestin1 function by extracellular signal-regulated kinases
    • Lin, F. T., Miller, W. E., Luttrell, L. M. and Lefkowitz, R. J. (1999) Feedback regulation of β-arrestin1 function by extracellular signal-regulated kinases. J. Biol. Chem. 274, 15971-15974
    • (1999) J. Biol. Chem. , vol.274 , pp. 15971-15974
    • Lin, F.T.1    Miller, W.E.2    Luttrell, L.M.3    Lefkowitz, R.J.4
  • 101
    • 0033521109 scopus 로고    scopus 로고
    • Feedback inhibition of G protein-coupled receptor kinase 2 (GRK2) activity by extracellular signal-regulated kinases
    • Pitcher, J. A., Tesmer, J. J., Freeman, J. L., Capel, W. D., Stone, W. C. and Lefkowitz, R. J. (1999) Feedback inhibition of G protein-coupled receptor kinase 2 (GRK2) activity by extracellular signal-regulated kinases. J. Biol. Chem. 274, 34531-34534
    • (1999) J. Biol. Chem. , vol.274 , pp. 34531-34534
    • Pitcher, J.A.1    Tesmer, J.J.2    Freeman, J.L.3    Capel, W.D.4    Stone, W.C.5    Lefkowitz, R.J.6
  • 102
    • 0034672063 scopus 로고    scopus 로고
    • Erk1/2-dependent phosphorylation of Gα-interacting protein stimulates its GTPase accelerating activity and autophagy in human colon cancer cells
    • Ogier-Denis, E., Pattingre, S., El Benna, J. and Codogno, P. (2000) Erk1/2-dependent phosphorylation of Gα-interacting protein stimulates its GTPase accelerating activity and autophagy in human colon cancer cells. J. Biol. Chem. 275, 39090-39095
    • (2000) J. Biol. Chem. , vol.275 , pp. 39090-39095
    • Ogier-Denis, E.1    Pattingre, S.2    El Benna, J.3    Codogno, P.4
  • 104
    • 0037147145 scopus 로고    scopus 로고
    • β-arrestin2 is critically involved in CXCR4-mediated chemotaxis, and this is mediated by its enhancement of p38 MAPK activation
    • Sun, Y., Cheng, Z., Ma, L. and Pei, G. (2002) β-arrestin2 is critically involved in CXCR4-mediated chemotaxis, and this is mediated by its enhancement of p38 MAPK activation. J. Biol. Chem. 277, 49212-49219
    • (2002) J. Biol. Chem. , vol.277 , pp. 49212-49219
    • Sun, Y.1    Cheng, Z.2    Ma, L.3    Pei, G.4
  • 105
    • 0037821781 scopus 로고    scopus 로고
    • G-protein-coupled receptor (GPCR) kinase phosphorylation and β-arrestin recruitment regulate the constitutive signaling activity of the human cytomegalovirus US28 GPCR
    • Miller, W. E., Houtz, D. A., Nelson, C. D., Kolattukudy, P. E. and Lefkowitz, R. J. (2003) G-protein-coupled receptor (GPCR) kinase phosphorylation and β-arrestin recruitment regulate the constitutive signaling activity of the human cytomegalovirus US28 GPCR. J. Biol. Chem. 278, 21663-21671
    • (2003) J. Biol. Chem. , vol.278 , pp. 21663-21671
    • Miller, W.E.1    Houtz, D.A.2    Nelson, C.D.3    Kolattukudy, P.E.4    Lefkowitz, R.J.5
  • 106
    • 0033617576 scopus 로고    scopus 로고
    • A cell's sense of direction
    • Parent, C. A. and Devreotes, P. N. (1999) A cell's sense of direction. Science 284, 765-770
    • (1999) Science , vol.284 , pp. 765-770
    • Parent, C.A.1    Devreotes, P.N.2
  • 108
    • 0141483377 scopus 로고    scopus 로고
    • A β-arrestin-dependent scaffold is associated with prolonged MAPK activation in pseudopodia during protease-activated receptor-2-induced chemotaxis
    • Ge, L., Ly, Y., Hollenberg, M. and DeFea, K. (2003) A β-arrestin-dependent scaffold is associated with prolonged MAPK activation in pseudopodia during protease-activated receptor-2-induced chemotaxis. J. Biol. Chem. 278, 34418-34426
    • (2003) J. Biol. Chem. , vol.278 , pp. 34418-34426
    • Ge, L.1    Ly, Y.2    Hollenberg, M.3    DeFea, K.4
  • 109
    • 0035852894 scopus 로고    scopus 로고
    • Arrestins as signaling molecules involved in apoptotic pathways: A real eye opener
    • Miller, W. E. and Lefkowitz, R. J. (2001) Arrestins as signaling molecules involved in apoptotic pathways: a real eye opener. Sci STKE (2001), PE1
    • (2001) Sci STKE , Issue.2001
    • Miller, W.E.1    Lefkowitz, R.J.2
  • 110
    • 0033636313 scopus 로고    scopus 로고
    • The formation of stable rhodopsin-arrestin complexes induces apoptosis and photoreceptor cell degeneration
    • Alloway, P. G., Howard, L. and Dolph, P. J. (2000) The formation of stable rhodopsin-arrestin complexes induces apoptosis and photoreceptor cell degeneration. Neuron 28, 129-138
    • (2000) Neuron , vol.28 , pp. 129-138
    • Alloway, P.G.1    Howard, L.2    Dolph, P.J.3
  • 111
    • 0033638395 scopus 로고    scopus 로고
    • A molecular pathway for light-dependent photoreceptor apoptosis in Drosophila
    • Kiselev, A., Socolich, M., Vinos, J., Hardy R. W., Zuker, C. S. and Ranganathan, R. (2000) A molecular pathway for light-dependent photoreceptor apoptosis in Drosophila. Neuron 28, 139-152
    • (2000) Neuron , vol.28 , pp. 139-152
    • Kiselev, A.1    Socolich, M.2    Vinos, J.3    Hardy, R.W.4    Zuker, C.S.5    Ranganathan, R.6
  • 112
    • 0037436537 scopus 로고    scopus 로고
    • Cell biology. A matter of life or death
    • Ranganathan, R. (2003) Cell biology. A matter of life or death. Science 299, 1677-1679
    • (2003) Science , vol.299 , pp. 1677-1679
    • Ranganathan, R.1
  • 113
    • 0037436579 scopus 로고    scopus 로고
    • Modulating sphingolipid biosynthetic pathway rescues photoreceptor degeneration
    • Acharya, U., Patel, S., Koundakjian, E., Nagashima, K., Han, X. and Acharya, J. K. (2003) Modulating sphingolipid biosynthetic pathway rescues photoreceptor degeneration. Science 299, 1740-1743
    • (2003) Science , vol.299 , pp. 1740-1743
    • Acharya, U.1    Patel, S.2    Koundakjian, E.3    Nagashima, K.4    Han, X.5    Acharya, J.K.6
  • 114
    • 0037458705 scopus 로고    scopus 로고
    • β-arrestin2 functions as a G-protein-coupled receptor-activated regulator of oncoprotein Mdm2
    • Wang, P., Gao, H., Ni, Y., Wang, B., Wu, Y., Ji, L., Qin, L., Ma, L. and Pei, G. (2003) β-arrestin2 functions as a G-protein-coupled receptor-activated regulator of oncoprotein Mdm2. J. Biol. Chem. 278, 6363-6370
    • (2003) J. Biol. Chem. , vol.278 , pp. 6363-6370
    • Wang, P.1    Gao, H.2    Ni, Y.3    Wang, B.4    Wu, Y.5    Ji, L.6    Qin, L.7    Ma, L.8    Pei, G.9
  • 115
    • 0037020264 scopus 로고    scopus 로고
    • Differential nucleocytoplasmic shuttling of β-arrestins. Characterization of a leucine-rich nuclear export signal in β-arrestin2
    • Scott, M. G., Le Rouzic, E., Perianin, A., Pierotti, V., Enslen, H., Benichou, S., Marullo, S. and Benmerah, A. (2002) Differential nucleocytoplasmic shuttling of β-arrestins. Characterization of a leucine-rich nuclear export signal in β-arrestin2. J. Biol. Chem. 277, 37693-37701
    • (2002) J. Biol. Chem. , vol.277 , pp. 37693-37701
    • Scott, M.G.1    Le Rouzic, E.2    Perianin, A.3    Pierotti, V.4    Enslen, H.5    Benichou, S.6    Marullo, S.7    Benmerah, A.8
  • 116
    • 0038514264 scopus 로고    scopus 로고
    • Subcellular localization of β-arrestins is determined by their intact N domain and the nuclear export signal at the C terminus
    • Wang, P., Wu, Y., Ge, X., Ma, L. and Pei, G. (2003) Subcellular localization of β-arrestins is determined by their intact N domain and the nuclear export signal at the C terminus. J. Biol. Chem. 278, 11648-11653
    • (2003) J. Biol. Chem. , vol.278 , pp. 11648-11653
    • Wang, P.1    Wu, Y.2    Ge, X.3    Ma, L.4    Pei, G.5
  • 117
    • 0033588242 scopus 로고    scopus 로고
    • Nuclear shuttling of yeast scaffold Ste5 is required for its recruitment to the plasma membrane and activation of the mating MAPK cascade
    • Mahanty, S. K., Wang, Y., Farley, F. W. and Elion, E. A. (1999) Nuclear shuttling of yeast scaffold Ste5 is required for its recruitment to the plasma membrane and activation of the mating MAPK cascade. Cell 98, 501-512
    • (1999) Cell , vol.98 , pp. 501-512
    • Mahanty, S.K.1    Wang, Y.2    Farley, F.W.3    Elion, E.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.