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Volumn 385, Issue 1, 2005, Pages 197-206

Activation of an α2A-adrenoceptor-Gαo1 fusion protein dynamically regulates the palmitoylation status of the G protein but not of the receptor

Author keywords

Acylation; G protein; G protein coupled receptor (GPCR); Signal transduction

Indexed keywords

ACYLATION; BIOCHEMISTRY; CHEMICAL ACTIVATION; REACTION KINETICS;

EID: 12744274770     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20041432     Document Type: Article
Times cited : (16)

References (45)
  • 1
    • 0038757730 scopus 로고    scopus 로고
    • Role of palmitoylation/depalmitoylation reactions in G-protein-coupled receptor function
    • Qanbar, R. and Bouvier, M. (2003) Role of palmitoylation/depalmitoylation reactions in G-protein-coupled receptor function. Pharmacol. Ther. 97, 1-33
    • (2003) Pharmacol. Ther. , vol.97 , pp. 1-33
    • Qanbar, R.1    Bouvier, M.2
  • 2
    • 0037213362 scopus 로고    scopus 로고
    • The on-off story of protein palmitoylation
    • Bijlmakers, M. J. and Marsh, M. (2003) The on-off story of protein palmitoylation. Trends Cell Biol. 13, 32-42
    • (2003) Trends Cell Biol. , vol.13 , pp. 32-42
    • Bijlmakers, M.J.1    Marsh, M.2
  • 3
    • 0037450538 scopus 로고    scopus 로고
    • s is palmitoylated at the N-terminal glycine
    • s is palmitoylated at the N-terminal glycine. EMBO J. 22, 826-832
    • (2003) EMBO J. , vol.22 , pp. 826-832
    • Kleuss, C.1    Krause, E.2
  • 4
    • 0031752275 scopus 로고    scopus 로고
    • Lipid modifications and membrane targeting of Gα
    • Wedegaertner, P. B. (1998) Lipid modifications and membrane targeting of Gα. Biol. Signals Recept. 7, 125-135
    • (1998) Biol. Signals Recept. , vol.7 , pp. 125-135
    • Wedegaertner, P.B.1
  • 5
    • 0035952690 scopus 로고    scopus 로고
    • Regulation of G proteins by covalent modification
    • Chen, C. A. and Manning, D. R. (2001) Regulation of G proteins by covalent modification. Oncogene 20, 1643-1652
    • (2001) Oncogene , vol.20 , pp. 1643-1652
    • Chen, C.A.1    Manning, D.R.2
  • 6
    • 0032409112 scopus 로고    scopus 로고
    • Palmitoylation of the rat μ opioid receptor
    • Chen, C., Shahabi, V., Xu, W. and Liu-Chen, L. Y. (1998) Palmitoylation of the rat μ opioid receptor. FEBS Lett. 441, 148-152
    • (1998) FEBS Lett. , vol.441 , pp. 148-152
    • Chen, C.1    Shahabi, V.2    Xu, W.3    Liu-Chen, L.Y.4
  • 7
    • 0035851198 scopus 로고    scopus 로고
    • Palmitoylation of the vasopressin Via receptor reveals different conformational requirements for signaling, agonist-induced receptor phosphorylation, and sequestration
    • Hawtin, S. R., Tobin, A. B., Patel, S. and Wheatley, M. (2001) Palmitoylation of the vasopressin Via receptor reveals different conformational requirements for signaling, agonist-induced receptor phosphorylation, and sequestration. J. Biol. Chem. 276, 38139-38146
    • (2001) J. Biol. Chem. , vol.276 , pp. 38139-38146
    • Hawtin, S.R.1    Tobin, A.B.2    Patel, S.3    Wheatley, M.4
  • 8
    • 0028307839 scopus 로고
    • Fluorescence studies of the location and membrane accessibility of the palmitoylation sites of rhodopsin
    • Moench, S. J., Moreland, J., Stewart, D. H. and Dewey, T. G. (1994) Fluorescence studies of the location and membrane accessibility of the palmitoylation sites of rhodopsin. Biochemistry 33, 5791-5796
    • (1994) Biochemistry , vol.33 , pp. 5791-5796
    • Moench, S.J.1    Moreland, J.2    Stewart, D.H.3    Dewey, T.G.4
  • 10
    • 0024544232 scopus 로고
    • Palmitoylation of the human β2-adrenergic receptor. Mutation of Cys341 in the carboxyl tail leads to an uncoupled nonpalmitoylated form of the receptor
    • O'Dowd, B. F., Hnatowich, M., Caron, M. G., Lefkowitz, R. J. and Bouvier, M. (1989) Palmitoylation of the human β2-adrenergic receptor. Mutation of Cys341 in the carboxyl tail leads to an uncoupled nonpalmitoylated form of the receptor. J. Biol. Chem. 264, 7564-7569
    • (1989) J. Biol. Chem. , vol.264 , pp. 7564-7569
    • O'Dowd, B.F.1    Hnatowich, M.2    Caron, M.G.3    Lefkowitz, R.J.4    Bouvier, M.5
  • 11
    • 0027401994 scopus 로고
    • Mutations of the α 2A-adrenergic receptor that eliminate detectable palmitoylation do not perturb receptor-G-protein coupling
    • Kennedy, M. E. and Limbird, L. E. (1993) Mutations of the α 2A-adrenergic receptor that eliminate detectable palmitoylation do not perturb receptor-G-protein coupling. J. Biol. Chem. 268, 8003-8011
    • (1993) J. Biol. Chem. , vol.268 , pp. 8003-8011
    • Kennedy, M.E.1    Limbird, L.E.2
  • 12
    • 0028172976 scopus 로고
    • Palmitoylation of the α 2A-adrenergic receptor. Analysis of the sequence requirements for and the dynamic properties of α 2A-adrenergic receptor palmitoylation
    • Kennedy, M. E. and Limbird, L. E. (1994) Palmitoylation of the α 2A-adrenergic receptor. Analysis of the sequence requirements for and the dynamic properties of α 2A-adrenergic receptor palmitoylation. J. Biol. Chem. 269, 31915-31922
    • (1994) J. Biol. Chem. , vol.269 , pp. 31915-31922
    • Kennedy, M.E.1    Limbird, L.E.2
  • 13
    • 0029753014 scopus 로고    scopus 로고
    • Agonist stimulation increases the turnover rate of β2AR-bound palmitate and promotes receptor depalmitoylation
    • Loisel, T. P., Adam, L., Hebert, T. E. and Bouvier, M. (1996) Agonist stimulation increases the turnover rate of β2AR-bound palmitate and promotes receptor depalmitoylation. Biochemistry 35, 15923-15932
    • (1996) Biochemistry , vol.35 , pp. 15923-15932
    • Loisel, T.P.1    Adam, L.2    Hebert, T.E.3    Bouvier, M.4
  • 14
    • 0037169528 scopus 로고    scopus 로고
    • The 5-hydroxytryptamine(4a) receptor is palmitoylated at two different sites, and acylation is critically involved in regulation of receptor constitutive activity
    • Ponimaskin, E. G., Heine, M., Joubert, L., Sebben, M., Bickmeyer, U., Richter, D. W. and Dumuis, A. (2002) The 5-hydroxytryptamine(4a) receptor is palmitoylated at two different sites, and acylation is critically involved in regulation of receptor constitutive activity. J. Biol. Chem. 277, 2534-2546
    • (2002) J. Biol. Chem. , vol.277 , pp. 2534-2546
    • Ponimaskin, E.G.1    Heine, M.2    Joubert, L.3    Sebben, M.4    Bickmeyer, U.5    Richter, D.W.6    Dumuis, A.7
  • 15
    • 0037470048 scopus 로고    scopus 로고
    • Palmitoylation of the Human Prostacyclin Receptor. Functional implications of palmitoylation and isoprenylation
    • Miggin, S. M., Lawler, O. A. and Kinsella, B. T. (2003) Palmitoylation of the Human Prostacyclin Receptor. Functional implications of palmitoylation and isoprenylation. J. Biol. Chem. 278, 6947-6958
    • (2003) J. Biol. Chem. , vol.278 , pp. 6947-6958
    • Miggin, S.M.1    Lawler, O.A.2    Kinsella, B.T.3
  • 18
    • 0032747133 scopus 로고    scopus 로고
    • Activation of the β(2)-adrenergic receptor-Gα(s) complex leads to rapid depalmitoylation and inhibition of repalmitoylation of both the receptor and Gα(s)
    • Loisel, T. P., Ansanay, H., Adam, L., Marullo, S., Seifert, R., Lagace, M. and Bouvier, M. (1999) Activation of the β(2)-adrenergic receptor-Gα(s) complex leads to rapid depalmitoylation and inhibition of repalmitoylation of both the receptor and Gα(s). J. Biol. Chem. 274, 31014-31019
    • (1999) J. Biol. Chem. , vol.274 , pp. 31014-31019
    • Loisel, T.P.1    Ansanay, H.2    Adam, L.3    Marullo, S.4    Seifert, R.5    Lagace, M.6    Bouvier, M.7
  • 19
    • 0035929656 scopus 로고    scopus 로고
    • Coordinated agonist regulation of receptor and G-protein palmitoylation and functional rescue of palmitoylation-deficient mutants of the G protein G11α following fusion to the α1b-adrenoreceptor: Palmitoylation of G11α is not required for interaction with β/γ complex
    • Stevens, P. A., Pediani, J., Carrillo, J. J. and Milligan, G. (2001) Coordinated agonist regulation of receptor and G-protein palmitoylation and functional rescue of palmitoylation-deficient mutants of the G protein G11α following fusion to the α1b-adrenoreceptor: palmitoylation of G11α is not required for interaction with β/γ complex. J. Biol. Chem. 276, 35883-35890
    • (2001) J. Biol. Chem. , vol.276 , pp. 35883-35890
    • Stevens, P.A.1    Pediani, J.2    Carrillo, J.J.3    Milligan, G.4
  • 20
    • 0033956330 scopus 로고    scopus 로고
    • Insights into ligand pharmacology using receptor-G-protein fusion proteins
    • Milligan, G. (2000) Insights into ligand pharmacology using receptor-G-protein fusion proteins. Trends Pharmacol. Sci. 21, 24-28
    • (2000) Trends Pharmacol. Sci. , vol.21 , pp. 24-28
    • Milligan, G.1
  • 21
    • 0034604616 scopus 로고    scopus 로고
    • The regulator of G protein signaling RGS4 selectively enhances α 2A-adreoreceptor stimulation of the GTPase activity of Go1α and Gi2α
    • Cavalli, A., Druey, K. M. and Milligan, G. (2000) The regulator of G protein signaling RGS4 selectively enhances α 2A-adreoreceptor stimulation of the GTPase activity of Go1α and Gi2α. J. Biol. Chem. 275, 23693-23699
    • (2000) J. Biol. Chem. , vol.275 , pp. 23693-23699
    • Cavalli, A.1    Druey, K.M.2    Milligan, G.3
  • 22
    • 0030813046 scopus 로고    scopus 로고
    • Rescue of functional interactions between the α2A-adrenoreceptor and acylation-resistant forms of Gi1α by expressing the proteins from chimeric open reading frames
    • Wise, A. and Milligan, G. (1997) Rescue of functional interactions between the α2A-adrenoreceptor and acylation-resistant forms of Gi1α by expressing the proteins from chimeric open reading frames. J. Biol. Chem. 272, 24673-24678
    • (1997) J. Biol. Chem. , vol.272 , pp. 24673-24678
    • Wise, A.1    Milligan, G.2
  • 23
    • 0025602883 scopus 로고
    • o, in neuroblastoma x glioma hybrid cells. Independent regulation during cyclic AMP-induced differentiation
    • o, in neuroblastoma x glioma hybrid cells. Independent regulation during cyclic AMP-induced differentiation. J. Neurochem. 55, 1890-1898
    • (1990) J. Neurochem. , vol.55 , pp. 1890-1898
    • Mullaney, I.1    Milligan, G.2
  • 25
    • 0037432328 scopus 로고    scopus 로고
    • Partial rescue of functional interactions of a nonpalmitoylated mutant of the G-protein Gα(s) by Fusion to the β-adrenergic receptor
    • Ugur, O., Onaran, H. O. and Jones, T. L. (2003) Partial rescue of functional interactions of a nonpalmitoylated mutant of the G-protein Gα(s) by Fusion to the β-adrenergic receptor. Biochemistry 42, 2607-2615
    • (2003) Biochemistry , vol.42 , pp. 2607-2615
    • Ugur, O.1    Onaran, H.O.2    Jones, T.L.3
  • 26
    • 0942298112 scopus 로고    scopus 로고
    • The 5-hydroxytryptamine(1A) receptor is stably palmitoylated, and acylation is critical for communication of receptor with Gi protein
    • Papoucheva, E., Dumuis, A., Sebben, M., Richter, D. W. and Ponimaskin, E. G. (2004) The 5-hydroxytryptamine(1A) receptor is stably palmitoylated, and acylation is critical for communication of receptor with Gi protein. J. Biol. Chem. 279, 3280-3291
    • (2004) J. Biol. Chem. , vol.279 , pp. 3280-3291
    • Papoucheva, E.1    Dumuis, A.2    Sebben, M.3    Richter, D.W.4    Ponimaskin, E.G.5
  • 27
    • 0036450783 scopus 로고    scopus 로고
    • The use of receptor-G protein fusion proteins for the study of ligand activity
    • Milligan, G. (2002) The use of receptor-G protein fusion proteins for the study of ligand activity. Receptors Channels 8, 309-317
    • (2002) Receptors Channels , vol.8 , pp. 309-317
    • Milligan, G.1
  • 29
    • 0038237526 scopus 로고    scopus 로고
    • The dynamics of formation and action of the ternary complex revealed in living cells using a G-protein gated K+ channel as a biosensor
    • Benians, A., Leaney, J. L., Milligan, G. and Tinker, A. (2003) The dynamics of formation and action of the ternary complex revealed in living cells using a G-protein gated K+ channel as a biosensor. J. Biol. Chem. 278, 10851-10858
    • (2003) J. Biol. Chem. , vol.278 , pp. 10851-10858
    • Benians, A.1    Leaney, J.L.2    Milligan, G.3    Tinker, A.4
  • 32
    • 0035163581 scopus 로고    scopus 로고
    • The palmitoylation state of the β(2)-adrenergic receptor regulates the synergistic action of cyclic AMP-dependent protein kinase and β-adrenergic receptor kinase involved in its phosphorylation and desensitization
    • Moffett, S., Rousseau, G., Lagace, M. and Bouvier, M. (2001) The palmitoylation state of the β(2)-adrenergic receptor regulates the synergistic action of cyclic AMP-dependent protein kinase and β-adrenergic receptor kinase involved in its phosphorylation and desensitization. J. Neurochem. 76, 269-279
    • (2001) J. Neurochem. , vol.76 , pp. 269-279
    • Moffett, S.1    Rousseau, G.2    Lagace, M.3    Bouvier, M.4
  • 33
    • 0029833903 scopus 로고    scopus 로고
    • Palmitoylation of endothelin receptor A. Differential modulation of signal transduction activity by post-translational modification
    • Horstmeyer, A., Cramer, H., Sauer, T., Muller-Esterl, W. and Schroeder, C. (1996) Palmitoylation of endothelin receptor A. Differential modulation of signal transduction activity by post-translational modification. J. Biol. Chem. 271, 20811-20819
    • (1996) J. Biol. Chem. , vol.271 , pp. 20811-20819
    • Horstmeyer, A.1    Cramer, H.2    Sauer, T.3    Muller-Esterl, W.4    Schroeder, C.5
  • 35
    • 0034825632 scopus 로고    scopus 로고
    • Palmitoylation of the luteinizing hormone/human chorionic gonadotropin receptor regulates receptor interaction with the arrestin-mediated internalization pathway
    • Munshi, U. M., Peegel, H. and Menon, K. M. (2001) Palmitoylation of the luteinizing hormone/human chorionic gonadotropin receptor regulates receptor interaction with the arrestin-mediated internalization pathway. Eur. J. Biochem. 268, 1631-1639
    • (2001) Eur. J. Biochem. , vol.268 , pp. 1631-1639
    • Munshi, U.M.1    Peegel, H.2    Menon, K.M.3
  • 36
    • 0037126682 scopus 로고    scopus 로고
    • Subtype-specific regulation of receptor internalization and recycling by the C-terminal domains of the human A1 and rat A3 adenosine receptors: Consequences for agonist-stimulated translocation of arrestin3
    • Ferguson, G., Watterson, K. R. and Palmer, T. M. (2002) Subtype-specific regulation of receptor internalization and recycling by the C-terminal domains of the human A1 and rat A3 adenosine receptors: consequences for agonist-stimulated translocation of arrestin3. Biochemistry 41, 14748-14761
    • (2002) Biochemistry , vol.41 , pp. 14748-14761
    • Ferguson, G.1    Watterson, K.R.2    Palmer, T.M.3
  • 37
    • 0142039784 scopus 로고    scopus 로고
    • Palmitoylation of the V2 vasopressin receptor carboxyl tail enhances β-arrestin recruitment leading to efficient receptor endocytosis and ERK1/2 activation
    • Charest, P. G. and Bouvier, M. (2003) Palmitoylation of the V2 vasopressin receptor carboxyl tail enhances β-arrestin recruitment leading to efficient receptor endocytosis and ERK1/2 activation. J. Biol. Chem. 278, 41541-41551
    • (2003) J. Biol. Chem. , vol.278 , pp. 41541-41551
    • Charest, P.G.1    Bouvier, M.2
  • 40
    • 0033621812 scopus 로고    scopus 로고
    • Interaction with Gβγ is required for membrane targeting and palmitoylation of Galpha(s) and Galpha(q)
    • Evanko, D. S., Thiyagarajan, M. M. and Wedegaertner, P. B. (2000) Interaction with Gβγ is required for membrane targeting and palmitoylation of Galpha(s) and Galpha(q). J. Biol. Chem. 275, 1327-1336
    • (2000) J. Biol. Chem. , vol.275 , pp. 1327-1336
    • Evanko, D.S.1    Thiyagarajan, M.M.2    Wedegaertner, P.B.3
  • 41
    • 0035968248 scopus 로고    scopus 로고
    • Gβγ isoforms selectively rescue plasma membrane localization and palmitoylation of mutant Gαs and Gαq
    • Evanko, D. S., Thiyagarajan, M. M., Siderovski, D. P. and Wedegaertner, P. B. (2001) Gβγ isoforms selectively rescue plasma membrane localization and palmitoylation of mutant Gαs and Gαq. J. Biol. Chem. 276, 23945-23953
    • (2001) J. Biol. Chem. , vol.276 , pp. 23945-23953
    • Evanko, D.S.1    Thiyagarajan, M.M.2    Siderovski, D.P.3    Wedegaertner, P.B.4
  • 43
    • 0037903425 scopus 로고    scopus 로고
    • Concerted stimulation and deactivation of pertussis toxin-sensitive G proteins by chimeric G protein-coupled receptor-regulator of G protein signaling 4 fusion proteins: Analysis of the contribution of palmitoylated cysteine residues to the GAP activity of RGS4
    • Bahia, D. S., Sartania, N., Ward, R. J., Cavalli, A., Jones, T. L., Druey, K. M. and Milligan, G. (2003) Concerted stimulation and deactivation of pertussis toxin-sensitive G proteins by chimeric G protein-coupled receptor-regulator of G protein signaling 4 fusion proteins: analysis of the contribution of palmitoylated cysteine residues to the GAP activity of RGS4. J. Neurochem, 85, 1289-1298
    • (2003) J. Neurochem. , vol.85 , pp. 1289-1298
    • Bahia, D.S.1    Sartania, N.2    Ward, R.J.3    Cavalli, A.4    Jones, T.L.5    Druey, K.M.6    Milligan, G.7
  • 44
    • 0036082516 scopus 로고    scopus 로고
    • NK1 receptor fused to β-arrestin displays a single-component, high-affinity molecular phenotype
    • Martini, L., Hastrup, H., Holst, B., Fraile-Ramos, A., Marsh, M. and Schwartz, T. W. (2002) NK1 receptor fused to β-arrestin displays a single-component, high-affinity molecular phenotype. Mol. Pharmacol. 62, 30-37
    • (2002) Mol. Pharmacol. , vol.62 , pp. 30-37
    • Martini, L.1    Hastrup, H.2    Holst, B.3    Fraile-Ramos, A.4    Marsh, M.5    Schwartz, T.W.6
  • 45
    • 85047695322 scopus 로고    scopus 로고
    • Localization of the human oxytocin receptor in caveolin-1 enriched domains turns the receptor-mediated inhibition of cell growth into a proliferative response
    • Guzzi, F., Zanchetta, D., Cassoni, P., Guzzi, V., Francolini, M., Parenti, M. and Chini, B. (2002) Localization of the human oxytocin receptor in caveolin-1 enriched domains turns the receptor-mediated inhibition of cell growth into a proliferative response. Oncogene 21, 1658-1667
    • (2002) Oncogene , vol.21 , pp. 1658-1667
    • Guzzi, F.1    Zanchetta, D.2    Cassoni, P.3    Guzzi, V.4    Francolini, M.5    Parenti, M.6    Chini, B.7


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