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Volumn 288, Issue 44, 2013, Pages 32004-32019

Agonist-dependent signaling by group I metabotropic glutamate receptors is regulated by association with lipid domains

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVITY-DEPENDENT; COGNITIVE DEFICITS; CRITICAL FUNCTIONS; G PROTEIN COUPLED RECEPTORS; MEMBRANE CHOLESTEROL; METABOTROPIC GLUTAMATE RECEPTORS; POSITIVE ALLOSTERIC MODULATOR; SYNAPTIC PLASTICITY;

EID: 84887081316     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.475863     Document Type: Article
Times cited : (31)

References (82)
  • 1
    • 77949516412 scopus 로고    scopus 로고
    • Metabotropic glutamate receptors. Physiology, pharmacology, and disease
    • Niswender, C. M., and Conn, P. J. (2010) Metabotropic glutamate receptors. Physiology, pharmacology, and disease. Annu. Rev. Pharmacol. Toxicol. 50, 295-322
    • (2010) Annu. Rev. Pharmacol. Toxicol. , vol.50 , pp. 295-322
    • Niswender, C.M.1    Conn, P.J.2
  • 2
    • 60149095737 scopus 로고    scopus 로고
    • Metabotropic glutamate receptor-dependent long-term potentiation
    • Anwyl, R. (2009) Metabotropic glutamate receptor-dependent long-term potentiation. Neuropharmacology 56, 735-740
    • (2009) Neuropharmacology , vol.56 , pp. 735-740
    • Anwyl, R.1
  • 3
    • 76849116197 scopus 로고    scopus 로고
    • Group1 mGluR-dependent synaptic long-term depression. Mechanisms and implications for circuitry and disease
    • Lüscher, C., and Huber, K. M. (2010) Group1 mGluR-dependent synaptic long-term depression. Mechanisms and implications for circuitry and disease. Neuron 65, 445-459
    • (2010) Neuron , vol.65 , pp. 445-459
    • Lüscher, C.1    Huber, K.M.2
  • 4
    • 0035708880 scopus 로고    scopus 로고
    • Internalization of ionotropic glutamate receptors in response to mGluR activation
    • DOI 10.1038/nn746
    • Snyder, E. M., and Philpot., B. D., Huber, K. M., Dong, X., Fallon, J. R., and Bear, M. F. (2001) Internalization of ionotropic glutamate receptors in response to mGluR activation. Nat. Neurosci. 4, 1079-1085 (Pubitemid 34116552)
    • (2001) Nature Neuroscience , vol.4 , Issue.11 , pp. 1079-1085
    • Snyder, E.M.1    Philpot, B.D.2    Huber, K.M.3    Dong, X.4    Fallon, J.R.5    Bear, M.F.6
  • 5
    • 68649093278 scopus 로고    scopus 로고
    • Protein translation in synaptic plasticity. MGluR-LTD, fragile X
    • Waung, M. W., and Huber, K. M. (2009) Protein translation in synaptic plasticity. mGluR-LTD, fragile X. Curr. Opin. Neurobiol. 19, 319-326
    • (2009) Curr. Opin. Neurobiol. , vol.19 , pp. 319-326
    • Waung, M.W.1    Huber, K.M.2
  • 6
    • 36248998214 scopus 로고    scopus 로고
    • Group I metabotropic glutamate receptors: A role in neurodevelopmental disorders?
    • DOI 10.1007/s12035-007-0022-1
    • Catania, M. V., D'Antoni, S., Bonaccorso, C. M., Aronica, E., Bear, M. F., and Nicoletti, F. (2007) Group I metabotropic glutamate receptors. A role in neurodevelopmental disorders? Mol. Neurobiol. 35, 298-307 (Pubitemid 350129691)
    • (2007) Molecular Neurobiology , vol.35 , Issue.3 , pp. 298-307
    • Catania, M.V.1    D'Antoni, S.2    Bonaccorso, C.M.3    Aronica, E.4    Bear, M.F.5    Nicoletti, F.6
  • 7
    • 40949090052 scopus 로고    scopus 로고
    • Role for metabotropic glutamate receptor 5 (mGluR5) in the pathogenesis of fragile X syndrome
    • DOI 10.1113/jphysiol.2008.150722
    • Dölen, G., and Bear, M. F. (2008) Role for metabotropic glutamate receptor 5 (mGluR5) in the pathogenesis of fragile X syndrome. J. Physiol. 586, 1503-1508 (Pubitemid 351404955)
    • (2008) Journal of Physiology , vol.586 , Issue.6 , pp. 1503-1508
    • Dolen, G.1    Bear, M.F.2
  • 10
    • 33846245536 scopus 로고    scopus 로고
    • Regulation of mitogen-activated protein kinases by glutamate receptors
    • DOI 10.1111/j.1471-4159.2006.04208.x
    • Wang, J. Q., and Fibuch., E. E., and Mao, L. (2007) Regulation of mitogen-activated protein kinases by glutamate receptors. J. Neurochem. 100, 1-11 (Pubitemid 46090772)
    • (2007) Journal of Neurochemistry , vol.100 , Issue.1 , pp. 1-11
    • Wang, J.Q.1    Fibuch, E.E.2    Mao, L.3
  • 11
    • 3242724040 scopus 로고    scopus 로고
    • Activation of the phosphoinositide 3-kinase-Akt-mammalian target of rapamycin signaling pathway is required for metabotropic glutamate receptor-dependent long-term depression
    • DOI 10.1523/JNEUROSCI.0995-04.2004
    • Hou, L., and Klann, E. (2004) Activation of the phosphoinositide 3-kinase-Akt-mammalian target of rapamycin signaling pathway is required for metabotropic glutamate receptor-dependent long-term depression. J. Neurosci. 24, 6352-6361 (Pubitemid 38944226)
    • (2004) Journal of Neuroscience , vol.24 , Issue.28 , pp. 6352-6361
    • Hou, L.1    Klann, E.2
  • 12
    • 74849118341 scopus 로고    scopus 로고
    • Lipid rafts as a membrane-organizing principle
    • Lingwood, D., and Simons, K. (2010) Lipid rafts as a membrane-organizing principle. Science 327, 46-50
    • (2010) Science , vol.327 , pp. 46-50
    • Lingwood, D.1    Simons, K.2
  • 13
    • 77955033375 scopus 로고    scopus 로고
    • Greasing their way. Lipid modifications determine protein association with membrane rafts
    • Levental, I., Grzybek, M., and Simons, K. (2010) Greasing their way. Lipid modifications determine protein association with membrane rafts. Biochemistry 49, 6305-6316
    • (2010) Biochemistry , vol.49 , pp. 6305-6316
    • Levental, I.1    Grzybek, M.2    Simons, K.3
  • 14
    • 80052275615 scopus 로고    scopus 로고
    • PI3K/Akt signaling requires spatial compartmentalization in plasma membrane microdomains
    • Gao, X., and Lowry., P. R., Zhou, X., Depry, C., Wei, Z., and Wong., G. W., and Zhang, J. (2011) PI3K/Akt signaling requires spatial compartmentalization in plasma membrane microdomains. Proc. Natl. Acad. Sci. U.S.A. 108, 14509-14514
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 14509-14514
    • Gao, X.1    Lowry, P.R.2    Zhou, X.3    Depry, C.4    Wei, Z.5    Wong, G.W.6    Zhang, J.7
  • 15
  • 16
    • 0041730473 scopus 로고    scopus 로고
    • Metabotropic glutamate type 1α receptor localizes in low-density caveolin-rich plasma membrane fractions
    • DOI 10.1046/j.1471-4159.2003.01842.x
    • Burgueño, J., Enrich, C., Canela, E. I., Mallol, J., Lluis, C., Franco, R., and Ciruela, F. (2003) Metabotropic glutamate type 1a receptor localizes in low density caveolin-rich plasma membrane fractions. J. Neurochem. 86, 785-791 (Pubitemid 36988792)
    • (2003) Journal of Neurochemistry , vol.86 , Issue.4 , pp. 785-791
    • Burgueno, J.1    Enrich, C.2    Canela, E.I.3    Mallol, J.4    Lluis, C.5    Franco, R.6    Ciruela, F.7
  • 17
    • 63849088930 scopus 로고    scopus 로고
    • Regulation of group I metabotropic glutamate receptor trafficking and signaling by the caveolar/lipid raft pathway
    • Francesconi, A., Kumari, R., and Zukin, R. S. (2009) Regulation of group I metabotropic glutamate receptor trafficking and signaling by the caveolar/lipid raft pathway. J Neurosci 29, 3590-3602
    • (2009) J Neurosci , vol.29 , pp. 3590-3602
    • Francesconi, A.1    Kumari, R.2    Zukin, R.S.3
  • 18
    • 0026614196 scopus 로고
    • 3, 5-dihydroxyphenyl-glycine. A potent agonist of metabotropic glutamate receptors
    • Ito, I., Kohda, A., Tanabe, S., Hirose, E., Hayashi, M., Mitsunaga, S., and Sugiyama, H. (1992) 3, 5-Dihydroxyphenyl-glycine. A potent agonist of metabotropic glutamate receptors. Neuroreport 3, 1013-1016
    • (1992) Neuroreport , vol.3 , pp. 1013-1016
    • Ito, I.1    Kohda, A.2    Tanabe, S.3    Hirose, E.4    Hayashi, M.5    Mitsunaga, S.6    Sugiyama, H.7
  • 19
    • 0033028258 scopus 로고    scopus 로고
    • CPCCOEt, a noncompetitive metabotropic glutamate receptor 1 antagonist, inhibits receptor signaling without affecting glutamate binding
    • Litschig, S., Gasparini, F., Rueegg, D., Stoehr, N., and Flor., P. J., Vranesic, I., Prézeau, L., Pin, J. P., Thomsen, C., and Kuhn, R. (1999) CPCCOEt, a noncompetitive metabotropic glutamate receptor 1 antagonist, inhibits receptor signaling without affecting glutamate binding. Mol. Pharmacol. 55, 453-461 (Pubitemid 29128101)
    • (1999) Molecular Pharmacology , vol.55 , Issue.3 , pp. 453-461
    • Litschig, S.1    Gasparini, F.2    Rueegg, D.3    Stoehr, N.4    Flor, P.J.5    Vranesic, I.6    Prezeau, L.7    Pin, J.-P.8    Thomsen, C.9    Kuhn, R.10
  • 21
    • 80052798018 scopus 로고    scopus 로고
    • Identification of GPCR localization in detergent-resistant membranes
    • Kumari, R., and Francesconi, A. (2011) Identification of GPCR localization in detergent-resistant membranes. Methods Mol. Biol. 746, 411-423
    • (2011) Methods Mol. Biol. , vol.746 , pp. 411-423
    • Kumari, R.1    Francesconi, A.2
  • 22
    • 38449114971 scopus 로고    scopus 로고
    • Detergent resistance as a tool in membrane research
    • DOI 10.1038/nprot.2007.294, PII NPROT.2007.294
    • Lingwood, D., and Simons, K. (2007) Detergent resistance as a tool in membrane research. Nat. Protoc. 2, 2159-2165 (Pubitemid 351565854)
    • (2007) Nature Protocols , vol.2 , Issue.9 , pp. 2159-2165
    • Lingwood, D.1    Simons, K.2
  • 23
    • 0032489519 scopus 로고    scopus 로고
    • Role of the second and third intracellular loops of metabotropic glutamate receptors in mediating dual signal transduction activation
    • DOI 10.1074/jbc.273.10.5615
    • Francesconi, A., and Duvoisin, R. M. (1998) Role of the second and third intracellular loops of metabotropic glutamate receptors in mediating dual signal transduction activation. J. Biol. Chem. 273, 5615-5624 (Pubitemid 28124031)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.10 , pp. 5615-5624
    • Francesconi, A.1    Duvoisin, R.M.2
  • 25
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • DOI 10.1038/42408
    • Simons, K., and Ikonen, E. (1997) Functional rafts in cell membranes. Nature 387, 569-572 (Pubitemid 27248754)
    • (1997) Nature , vol.387 , Issue.6633 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 26
    • 22744437388 scopus 로고    scopus 로고
    • Detergent-resistant membranes should not be identified with membrane rafts
    • DOI 10.1016/j.tibs.2005.06.004, PII S0968000405001830
    • Lichtenberg, D., Goñi, F. M., and Heerklotz, H. (2005) Detergent-resistant membranes should not be identified with membrane rafts. Trends Biochem. Sci. 30, 430-436 (Pubitemid 41033238)
    • (2005) Trends in Biochemical Sciences , vol.30 , Issue.8 , pp. 430-436
    • Lichtenberg, D.1    Goni, F.M.2    Heerklotz, H.3
  • 27
    • 0029963929 scopus 로고    scopus 로고
    • Changes in the carboxyl-terminal domain of metabotropic glutamate receptor 1 by alternative splicing generate receptors with differing agonist-independent activity
    • Prézeau, L., Gomeza, J., Ahern, S., Mary, S., Galvez, T., Bockaert, J., and Pin, J. P. (1996) Changes in the carboxyl-terminal domain of metabotropic glutamate receptor 1 by alternative splicing generate receptors with differing agonist-independent activity. Mol. Pharmacol. 49, 422-429
    • (1996) Mol. Pharmacol. , vol.49 , pp. 422-429
    • Prézeau, L.1    Gomeza, J.2    Ahern, S.3    Mary, S.4    Galvez, T.5    Bockaert, J.6    Pin, J.P.7
  • 29
    • 33846419488 scopus 로고    scopus 로고
    • Lipid raft microdomains and neurotransmitter signalling
    • DOI 10.1038/nrn2059, PII NRN2059
    • Allen, J. A., Halverson-Tamboli, R. A., and Rasenick, M. M. (2007) Lipid raft microdomains and neurotransmitter signalling. Nat. Rev. Neurosci. 8, 128-140 (Pubitemid 46146951)
    • (2007) Nature Reviews Neuroscience , vol.8 , Issue.2 , pp. 128-140
    • Allen, J.A.1    Halverson-Tamboli, R.A.2    Rasenick, M.M.3
  • 30
    • 41149124594 scopus 로고    scopus 로고
    • Caveolae as organizers of pharmacologically relevant signal transduction molecules
    • DOI 10.1146/annurev.pharmtox.48.121506.124841
    • Patel, H. H., Murray, F., and Insel, P. A. (2008) Caveolae as organizers of pharmacologically relevant signal transduction molecules. Annu. Rev. Pharmacol. Toxicol. 48, 359-391 (Pubitemid 351738158)
    • (2008) Annual Review of Pharmacology and Toxicology , vol.48 , pp. 359-391
    • Patel, H.H.1    Murray, F.2    Insel, P.A.3
  • 31
    • 65649122726 scopus 로고    scopus 로고
    • Lattices, rafts, and scaffolds. Domain regulation of receptor signaling at the plasma membrane
    • Lajoie, P., and Goetz., J. G., Dennis, J. W., and Nabi, I. R. (2009) Lattices, rafts, and scaffolds. Domain regulation of receptor signaling at the plasma membrane. J. Cell Biol. 185, 381-385
    • (2009) J. Cell Biol. , vol.185 , pp. 381-385
    • Lajoie, P.1    Goetz, J.G.2    Dennis, J.W.3    Nabi, I.R.4
  • 33
    • 0036830114 scopus 로고    scopus 로고
    • Multiple functions of caveolin-1
    • DOI 10.1074/jbc.R200020200
    • Liu, P., Rudick, M., and Anderson, R. G. (2002) Multiple functions of caveolin-1. J. Biol. Chem. 277, 41295-41298 (Pubitemid 35257426)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.44 , pp. 41295-41298
    • Rudick, M.1    Anderson, R.G.W.2
  • 34
    • 35548958819 scopus 로고    scopus 로고
    • Regulation of D1 dopamine receptor trafficking and signaling by caveolin-1
    • DOI 10.1124/mol.107.034769
    • Kong, M. M., Hasbi, A., Mattocks, M., Fan, T., O'Dowd, B. F., and George, S. R. (2007) Regulation of D1 dopamine receptor trafficking and signaling by caveolin-1. Mol. Pharmacol. 72, 1157-1170 (Pubitemid 350012590)
    • (2007) Molecular Pharmacology , vol.72 , Issue.5 , pp. 1157-1170
    • Kong, M.M.C.1    Hasbi, A.2    Mattocks, M.3    Fan, T.4    O'Dowd, B.F.5    George, S.R.6
  • 38
    • 0030695849 scopus 로고    scopus 로고
    • Use of cyclodextrins for manipulating cellular cholesterol content
    • Christian, A. E., and Haynes., M. P., Phillips, M. C, and Rothblat, G. H. (1997) Use of cyclodextrins for manipulating cellular cholesterol content. J. Lipid Res. 38, 2264-2272 (Pubitemid 27495385)
    • (1997) Journal of Lipid Research , vol.38 , Issue.11 , pp. 2264-2272
    • Christian, A.E.1    Haynes, M.P.2    Phillips, M.C.3    Rothblat, G.H.4
  • 40
    • 78650664669 scopus 로고    scopus 로고
    • Palmitoylation regulates raft affinity for the majority of integral raft proteins
    • Levental, I., Lingwood, D., Grzybek, M., Coskun, U., and Simons, K. (2010) Palmitoylation regulates raft affinity for the majority of integral raft proteins. Proc. Natl. Acad. Sci. U.S.A. 107, 22050-22054
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 22050-22054
    • Levental, I.1    Lingwood, D.2    Grzybek, M.3    Coskun, U.4    Simons, K.5
  • 41
    • 54249148026 scopus 로고    scopus 로고
    • CSS-palm 2.0. An updated software for palmitoylation sites prediction
    • Ren, J., Wen, L., Gao, X., Jin, C, Xue, Y., and Yao, X. (2008) CSS-Palm 2.0. An updated software for palmitoylation sites prediction. Protein Eng. Des. Sel. 21, 639-644
    • (2008) Protein Eng. Des. Sel. , vol.21 , pp. 639-644
    • Ren, J.1    Wen, L.2    Gao, X.3    Jin, C.4    Xue, Y.5    Yao, X.6
  • 42
    • 0028924655 scopus 로고
    • The metabotropic glutamate receptor mGluR4, but not mGluR1α, is palmitoylated when expressed in BHK cells
    • Alaluf, S., and Mulvihill., E. R., and McIlhinney, R. A. (1995) The metabotropic glutamate receptor mGluR4, but not mGluR1α, is palmitoylated when expressed in BHK cells. J. Neurochem 64, 1548-1555
    • (1995) J. Neurochem , vol.64 , pp. 1548-1555
    • Alaluf, S.1    Mulvihill, E.R.2    McIlhinney, R.A.3
  • 43
    • 45449105538 scopus 로고    scopus 로고
    • Proteins and cholesterol-rich domains
    • Epand, R. M. (2008) Proteins and cholesterol-rich domains. Biochim. Biophys. Acta 1778, 1576-1582
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1576-1582
    • Epand, R.M.1
  • 44
    • 48249144810 scopus 로고    scopus 로고
    • Agonistselective signaling is determined by the receptor location within the membrane domains
    • Zheng, H., Chu, J., Qiu, Y., Loh, H. H., and Law, P. Y. (2008) Agonistselective signaling is determined by the receptor location within the membrane domains. Proc. Natl. Acad. Sci. U.S.A. 105, 9421-9426
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 9421-9426
    • Zheng, H.1    Chu, J.2    Qiu, Y.3    Loh, H.H.4    Law, P.Y.5
  • 45
    • 0037333737 scopus 로고    scopus 로고
    • Statin effects on cholesterol micro-domains in brain plasma membranes
    • DOI 10.1016/S0006-2952(02)01654-4
    • Kirsch, C, and Eckert., G. P., and Mueller, W. E. (2003) Statin effects on cholesterol micro-domains in brain plasma membranes. Biochem. Pharmacol. 65, 843-856 (Pubitemid 36293701)
    • (2003) Biochemical Pharmacology , vol.65 , Issue.5 , pp. 843-856
    • Kirsch, C.1    Eckert, G.P.2    Mueller, W.E.3
  • 46
    • 41149132355 scopus 로고    scopus 로고
    • Simvastatin reduces the association of NMDA receptors to lipid rafts: A cholesterol-mediated effect in neuroprotection
    • DOI 10.1161/STROKEAHA.107.498923, PII 0000767020080400000035
    • Ponce, J., de la Ossa, N. P., Hurtado, O., Millan, M., Arenillas, J. F., Dávalos, A., and Gasull, T. (2008) Simvastatin reduces the association of NMDA receptors to lipid rafts. A cholesterol-mediated effect in neuroprotection. Stroke 39, 1269-1275 (Pubitemid 351440701)
    • (2008) Stroke , vol.39 , Issue.4 , pp. 1269-1275
    • Ponce, J.1    De La Ossa, N.P.2    Hurtado, O.3    Millan, M.4    Arenillas, J.F.5    Davalos, A.6    Gasull, T.7
  • 47
    • 0344585437 scopus 로고    scopus 로고
    • Lipid rafts. Elusive or illusive?
    • Munro, S. (2003) Lipid rafts. Elusive or illusive? Cell 115, 377-388
    • (2003) Cell , vol.115 , pp. 377-388
    • Munro, S.1
  • 48
    • 29144484142 scopus 로고    scopus 로고
    • Partitioning of membrane molecules between raft and non-raft domains: Insights from model-membrane studies
    • DOI 10.1016/j.bbamcr.2005.09.003, PII S0167488905001989, Lipid Refts: From Model Membranes to Cells
    • Silvius, J. R. (2005) Partitioning of membrane molecules between raft and non-raft domains. Insights from model-membrane studies. Biochim. Biophys. Acta 1746, 193-202 (Pubitemid 41815016)
    • (2005) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1746 , Issue.3 , pp. 193-202
    • Silvius, J.R.1
  • 51
    • 4544383544 scopus 로고    scopus 로고
    • q-coupled protein receptors
    • DOI 10.1074/jbc.M404673200
    • Bhatnagar, A., and Sheffler., D. J., Kroeze, W. K., Compton-Toth, B., and Roth, B. L. (2004) Caveolin-1 interacts with 5-HT2A serotonin receptors and profoundly modulates the signaling of selected Gα-coupled protein receptors. J. Biol. Chem. 279, 34614-34623 (Pubitemid 39318091)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.33 , pp. 34614-34623
    • Bhatnagar, A.1    Sheffler, D.J.2    Kroeze, W.K.3    Compton-Toth, B.4    Roth, B.L.5
  • 53
    • 54049106162 scopus 로고    scopus 로고
    • Cholesterol-dependent separation of the β2-adrenergic receptor from its partners determines signaling efficacy. Insight into nanoscale organization of signal transduction
    • Pontier, S. M., Percherancier, Y., Galandrin, S., Breit, A., Galés, C, and Bouvier, M. (2008) Cholesterol-dependent separation of the β2-adrenergic receptor from its partners determines signaling efficacy. Insight into nanoscale organization of signal transduction. J. Biol. Chem. 283, 24659-24672
    • (2008) J. Biol. Chem. , vol.283 , pp. 24659-24672
    • Pontier, S.M.1    Percherancier, Y.2    Galandrin, S.3    Breit, A.4    Galés, C.5    Bouvier, M.6
  • 54
    • 84858319313 scopus 로고    scopus 로고
    • Palmitoylation and membrane cholesterol stabilize μ-opioid receptor homodimerization and G protein coupling
    • Zheng, H., and Pearsall., E. A., Hurst, D. P., Zhang, Y., Chu, J., Zhou, Y., Reggio, P. H, Loh, H. H., and Law, P. Y. (2012) Palmitoylation and membrane cholesterol stabilize μ-opioid receptor homodimerization and G protein coupling. BMC Cell Biol. 13, 6
    • (2012) BMC Cell Biol. , vol.13 , pp. 6
    • Zheng, H.1    Pearsall, E.A.2    Hurst, D.P.3    Zhang, Y.4    Chu, J.5    Zhou, Y.6    Reggio, P.H.7    Loh, H.H.8    Law, P.Y.9
  • 56
    • 49049108218 scopus 로고    scopus 로고
    • G-protein-coupled receptor-signaling components in membrane raft and caveolae microdomains
    • Patel, H. H., Murray, F., and Insel, P. A. (2008) G-protein-coupled receptor-signaling components in membrane raft and caveolae microdomains. Handb. Exp. Pharmacol. 186, 167-184
    • (2008) Handb. Exp. Pharmacol. , vol.186 , pp. 167-184
    • Patel, H.H.1    Murray, F.2    Insel, P.A.3
  • 57
    • 78650720054 scopus 로고    scopus 로고
    • Caveolin-1 knockout mice exhibit impaired induction of mGluR-dependent long-term depression at CA3-CA1 synapses
    • Takayasu, Y., Takeuchi, K., Kumari, R., Bennett, M. V., and Zukin., R. S., and Francesconi, A. (2010) Caveolin-1 knockout mice exhibit impaired induction of mGluR-dependent long-term depression at CA3-CA1 synapses. Proc. Natl. Acad. Sci. U.S.A. 107, 21778-21783
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 21778-21783
    • Takayasu, Y.1    Takeuchi, K.2    Kumari, R.3    Bennett, M.V.4    Zukin, R.S.5    Francesconi, A.6
  • 58
    • 79951964192 scopus 로고    scopus 로고
    • Modulation of monoamine receptors by adaptor proteins and lipid rafts. Role in some effects of centrally acting drugs and therapeutic agents
    • Björk, K., and Svenningsson, P. (2011) Modulation of monoamine receptors by adaptor proteins and lipid rafts. Role in some effects of centrally acting drugs and therapeutic agents. Annu. Rev. Pharmacol. Toxicol. 51, 211-242
    • (2011) Annu. Rev. Pharmacol. Toxicol. , vol.51 , pp. 211-242
    • Björk, K.1    Svenningsson, P.2
  • 66
    • 78650919372 scopus 로고    scopus 로고
    • Identification of cholesterol recognition amino acid consensus (CRAC) motif in G-protein-coupled receptors
    • Jafurulla, M., Tiwari, S., and Chattopadhyay, A. (2011) Identification of cholesterol recognition amino acid consensus (CRAC) motif in G-protein-coupled receptors. Biochem. Biophys. Res. Commun. 404, 569-573
    • (2011) Biochem. Biophys. Res. Commun. , vol.404 , pp. 569-573
    • Jafurulla, M.1    Tiwari, S.2    Chattopadhyay, A.3
  • 67
    • 79851494039 scopus 로고    scopus 로고
    • Functional characterization of putative cholesterol binding sequence (CRAC) in human type-1 cannabinoid receptor
    • Oddi, S., Dainese, E., Fezza, F., Lanuti, M., Barcaroli, D., De Laurenzi, V., Centonze, D., and Maccarrone, M. (2011) Functional characterization of putative cholesterol binding sequence (CRAC) in human type-1 cannabinoid receptor. J. Neurochem. 116, 858-865
    • (2011) J. Neurochem. , vol.116 , pp. 858-865
    • Oddi, S.1    Dainese, E.2    Fezza, F.3    Lanuti, M.4    Barcaroli, D.5    De Laurenzi, V.6    Centonze, D.7    Maccarrone, M.8
  • 68
    • 33746265808 scopus 로고    scopus 로고
    • A novel class of positive allosteric modulators of metabotropic glutamate receptor subtype 1 interact with a site distinct from that of negative allosteric modulators
    • DOI 10.1124/mol.105.021857
    • Hemstapat, K., de Paulis, T., Chen, Y., Brady, A. E., and Grover., V. K., Alagille, D., Tamagnan, G. D., and Conn, P. J. (2006) A novel class of positive allosteric modulators of metabotropic glutamate receptor subtype 1 interact with a site distinct from that of negative allosteric modulators. Mol. Pharmacol. 70, 616-626 (Pubitemid 44092322)
    • (2006) Molecular Pharmacology , vol.70 , Issue.2 , pp. 616-626
    • Hemstapat, K.1    De Paulis, T.2    Chen, Y.3    Brady, A.E.4    Grover, V.K.5    Alagille, D.6    Tamagnan, G.D.7    Conn, P.J.8
  • 69
    • 84864751433 scopus 로고    scopus 로고
    • Membrane-sensitive conformational states of helix 8 in the metabotropic glu2 receptor, a class C GPCR
    • Bruno, A., Costantino, G., de Fabritiis, G., Pastor, M., and Selent, J. (2012) Membrane-sensitive conformational states of helix 8 in the metabotropic Glu2 receptor, a class C GPCR. PLoS ONE 7, e42023
    • (2012) PLoS ONE , vol.7
    • Bruno, A.1    Costantino, G.2    De Fabritiis, G.3    Pastor, M.4    Selent, J.5
  • 71
    • 82955248059 scopus 로고    scopus 로고
    • Uncovering the intimate relationship between lipids, cholesterol, and GPCR activation
    • Oates, J., and Watts, A. (2011) Uncovering the intimate relationship between lipids, cholesterol, and GPCR activation. Curr. Opin. Struct. Biol. 21, 802-807
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 802-807
    • Oates, J.1    Watts, A.2
  • 72
    • 0029983948 scopus 로고    scopus 로고
    • Cloning and functional expression of a Drosophila metabotropic glutamate receptor expressed in the embryonic CNS
    • Parmentier, M. L., and Pin., J. P., Bockaert, J., and Grau, Y. (1996) Cloning and functional expression of a Drosophila metabotropic glutamate receptor expressed in the embryonic CNS. J. Neurosci. 16, 6687-6694 (Pubitemid 26359352)
    • (1996) Journal of Neuroscience , vol.16 , Issue.21 , pp. 6687-6694
    • Parmentier, M.-L.1    Pin, J.-P.2    Bockaert, J.3    Grau, Y.4
  • 74
    • 0035984890 scopus 로고    scopus 로고
    • Functional reconstitution of purified metabotropic glutamate receptor expressed in the fly eye
    • DOI 10.1093/embo-reports/kvf088
    • Eroglu, C, Cronet, P., Panneels, V., Beaufils, P., and Sinning, I. (2002) Functional reconstitution of purified metabotropic glutamate receptor expressed in the fly eye. EMBO Rep. 3, 491-496 (Pubitemid 34567439)
    • (2002) EMBO Reports , vol.3 , Issue.5 , pp. 491-496
    • Eroglu, C.1    Cronet, P.2    Panneels, V.3    Beaufils, P.4    Sinning, I.5
  • 75
    • 33846901907 scopus 로고    scopus 로고
    • Metabotropic glutamate receptors: Intracellular signaling pathways
    • DOI 10.1016/j.coph.2006.08.008, PII S1471489206001706, Neurosciences
    • Gerber, U., and Gee., C. E., and Benquet, P. (2007) Metabotropic glutamate receptors. Intracellular signaling pathways. Curr. Opin. Pharmacol. 7, 56-61 (Pubitemid 46238032)
    • (2007) Current Opinion in Pharmacology , vol.7 , Issue.1 , pp. 56-61
    • Gerber, U.1    Gee, C.E.2    Benquet, P.3
  • 78
    • 2442637740 scopus 로고    scopus 로고
    • Extracellular signal-regulated protein kinase activation is required for metabotropic glutamate receptor-dependent long-term depression in hippocampal area CA1
    • DOI 10.1523/JNEUROSCI.5407-03.2004
    • Gallagher, S. M., and Daly., C. A., Bear, M. F., and Huber, K. M. (2004) Extracellular signal-regulated protein kinase activation is required for metabotropic glutamate receptor-dependent long-term depression in hippocampal area CA1. J. Neurosci. 24, 4859-4864 (Pubitemid 38668210)
    • (2004) Journal of Neuroscience , vol.24 , Issue.20 , pp. 4859-4864
    • Gallagher, S.M.1    Daly, C.A.2    Bear, M.F.3    Huber, K.M.4
  • 80
    • 67649878531 scopus 로고    scopus 로고
    • Activation switch in the transmembrane domain of metabotropic glutamate receptor
    • Yanagawa, M., Yamashita, T., and Shichida, Y. (2009) Activation switch in the transmembrane domain of metabotropic glutamate receptor. Mol. Pharmacol. 76, 201-207
    • (2009) Mol. Pharmacol. , vol.76 , pp. 201-207
    • Yanagawa, M.1    Yamashita, T.2    Shichida, Y.3
  • 81
    • 0037072884 scopus 로고    scopus 로고
    • Caveolar localization dictates physiologic signaling of β 2-adrenoceptors in neonatal cardiac myocytes
    • Xiang, Y., and Rybin., V. O., Steinberg, S. F., and Kobilka, B. (2002) Caveolar localization dictates physiologic signaling of β 2-adrenoceptors in neonatal cardiac myocytes. J. Biol. Chem. 277, 34280-34286
    • (2002) J. Biol. Chem. , vol.277 , pp. 34280-34286
    • Xiang, Y.1    Rybin, V.O.2    Steinberg, S.F.3    Kobilka, B.4
  • 82
    • 84872716739 scopus 로고    scopus 로고
    • Lovastatin corrects excess protein synthesis and prevents epileptogenesis in a mouse model of fragile X syndrome
    • Osterweil, E. K., and Chuang., S. C., Chubykin, A. A., Sidorov, M., Bianchi, R., and Wong., R. K., and Bear, M. F. (2013) Lovastatin corrects excess protein synthesis and prevents epileptogenesis in a mouse model of fragile X syndrome. Neuron 77, 243-250
    • (2013) Neuron , vol.77 , pp. 243-250
    • Osterweil, E.K.1    Chuang, S.C.2    Chubykin, A.A.3    Sidorov, M.4    Bianchi, R.5    Wong, R.K.6    Bear, M.F.7


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