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Volumn 540, Issue 7631, 2016, Pages 60-68

Organization and functions of mGlu and GABA B receptor complexes

Author keywords

[No Author keywords available]

Indexed keywords

4 AMINOBUTYRIC ACID B RECEPTOR; BACLOFEN; G PROTEIN COUPLED RECEPTOR; G PROTEIN COUPLED RECEPTOR KINASE; HYDROXYBUTYRIC ACID; METABOTROPIC RECEPTOR; MULTIPROTEIN COMPLEX; OLIGOMER; PROTEIN HOMER; REGULATOR PROTEIN; RETINA S ANTIGEN; BETA 2 ADRENERGIC RECEPTOR;

EID: 85000366245     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature20566     Document Type: Review
Times cited : (200)

References (99)
  • 1
    • 84862068720 scopus 로고    scopus 로고
    • Regulation of neuronal GABAB receptor functionsby subunit composition
    • Gassmann, M., Bettler, B. Regulation of neuronal GABAB receptor functionsby subunit composition. Nat. Rev. Neurosci. 13, 380-394 (2012).
    • (2012) Nat. Rev. Neurosci. , vol.13 , pp. 380-394
    • Gassmann, M.1    Bettler, B.2
  • 2
    • 77949516412 scopus 로고    scopus 로고
    • Metabotropic glutamate receptors: Physiology,pharmacology, and disease
    • Niswender, C. M., Conn, P. J. Metabotropic glutamate receptors: physiology,pharmacology, and disease. Annu. Rev. Pharmacol. Toxicol. 50, 295-322 (2010).
    • (2010) Annu. Rev. Pharmacol. Toxicol. , vol.50 , pp. 295-322
    • Niswender, C.M.1    Conn, P.J.2
  • 3
    • 77955068362 scopus 로고    scopus 로고
    • Chemistry and pharmacology of GABAB receptor ligands
    • Froestl, W. Chemistry and pharmacology of GABAB receptor ligands. Adv.Pharmacol. 58, 19-62 (2010).
    • (2010) Adv.Pharmacol. , vol.58 , pp. 19-62
    • Froestl, W.1
  • 4
    • 84888040704 scopus 로고    scopus 로고
    • Development of allosteric modulators of GPCRs fortreatment of CNS disorders
    • Nickols, H. H., Conn, P. J. Development of allosteric modulators of GPCRs fortreatment of CNS disorders. Neurobiol. Dis. 61, 55-71 (2014).
    • (2014) Neurobiol. Dis. , vol.61 , pp. 55-71
    • Nickols, H.H.1    Conn, P.J.2
  • 8
    • 84997839811 scopus 로고    scopus 로고
    • Phospho-dependentaccumulation of GABABRs at presynaptic terminals after NMDAR activation
    • Hannan, S., Gerrow, K., Triller, A., Smart, T. G. Phospho-dependentaccumulation of GABABRs at presynaptic terminals after NMDAR activation.Cell Reports 16, 1962-1973 (2016).
    • (2016) Cell Reports , vol.16 , pp. 1962-1973
    • Hannan, S.1    Gerrow, K.2    Triller, A.3    Smart, T.G.4
  • 9
    • 79251591614 scopus 로고    scopus 로고
    • A new approach to analyze cell surface proteincomplexes reveals specific heterodimeric metabotropic glutamate receptors
    • Doumazane, E., et al. A new approach to analyze cell surface proteincomplexes reveals specific heterodimeric metabotropic glutamate receptors.FASEB J. 25, 66-77 (2011).
    • (2011) FASEB J. , vol.25 , pp. 66-77
    • Doumazane, E.1
  • 10
    • 79958785452 scopus 로고    scopus 로고
    • The oligomeric state sets GABAB receptor signallingefficacy
    • Comps-Agrar, L., et al. The oligomeric state sets GABAB receptor signallingefficacy. EMBO J. 30, 2336-2349 (2011).
    • (2011) EMBO J. , vol.30 , pp. 2336-2349
    • Comps-Agrar, L.1
  • 11
    • 77952422366 scopus 로고    scopus 로고
    • Native GABAB receptors are heteromultimers with a family ofauxiliary subunits
    • Proteomic identification of the KCTD proteins that constitutively associatewith the GABAB2 subunit of GABABRs and regulate the kinetics ofG signalling to K+ and Ca2+ effector channels
    • Schwenk, J., et al. Native GABAB receptors are heteromultimers with a family ofauxiliary subunits. Nature 465, 231-235 (2010).Proteomic identification of the KCTD proteins that constitutively associatewith the GABAB2 subunit of GABABRs and regulate the kinetics ofG signalling to K+ and Ca2+ effector channels
    • (2010) Nature , vol.465 , pp. 231-235
    • Schwenk, J.1
  • 12
    • 84956686910 scopus 로고    scopus 로고
    • Modular composition and dynamics of native GABABreceptors identified by high-resolution proteomics
    • Comprehensive proteomic study reporting the GABABR interactome in therodent brain, including a functional characterization of the interaction ofGABABRs with hyperpolarization-activated cyclic-nucleotide-gated HCNchannels
    • Schwenk, J., et al. Modular composition and dynamics of native GABABreceptors identified by high-resolution proteomics. Nat. Neurosci. 19,233-242 (2016).Comprehensive proteomic study reporting the GABABR interactome in therodent brain, including a functional characterization of the interaction ofGABABRs with hyperpolarization-activated cyclic-nucleotide-gated HCNchannels.
    • (2016) Nat. Neurosci. , vol.19 , pp. 233-242
    • Schwenk, J.1
  • 13
    • 0035341213 scopus 로고    scopus 로고
    • Allosteric interactions between GB1 and GB2 subunits arerequired for optimal GABAB receptor function
    • Galvez, T., et al. Allosteric interactions between GB1 and GB2 subunits arerequired for optimal GABAB receptor function. EMBO J. 20, 2152-2159(2001).
    • (2001) EMBO J. , vol.20 , pp. 2152-2159
    • Galvez, T.1
  • 14
    • 84876272531 scopus 로고    scopus 로고
    • Protein complexes are under evolutionary selection toassemble via ordered pathways
    • Marsh, J. A., et al. Protein complexes are under evolutionary selection toassemble via ordered pathways. Cell 153, 461-470 (2013).
    • (2013) Cell , vol.153 , pp. 461-470
    • Marsh, J.A.1
  • 15
    • 84930341731 scopus 로고    scopus 로고
    • GABA receptor cell-surface export is controlled by anendoplasmic reticulum gatekeeper
    • Doly, S., et al. GABA receptor cell-surface export is controlled by anendoplasmic reticulum gatekeeper. Mol. Psychiatry 21, 480-490 (2016).
    • (2016) Mol. Psychiatry , vol.21 , pp. 480-490
    • Doly, S.1
  • 16
    • 84900474163 scopus 로고    scopus 로고
    • Heterodimeric coiled-coilinteractions of human GABAB receptor
    • Burmakina, S., Geng, Y., Chen, Y., Fan, Q. R. Heterodimeric coiled-coilinteractions of human GABAB receptor. Proc. Natl Acad. Sci. USA 111,6958-6963 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 6958-6963
    • Burmakina, S.1    Geng, Y.2    Chen, Y.3    Fan, Q.R.4
  • 17
    • 44449096254 scopus 로고    scopus 로고
    • Cell-surface protein-protein interaction analysis withtime-resolved FRET and snap-tag technologies: Application to GPCRoligomerization
    • Maurel, D., et al. Cell-surface protein-protein interaction analysis withtime-resolved FRET and snap-tag technologies: application to GPCRoligomerization. Nat. Methods 5, 561-567 (2008).
    • (2008) Nat. Methods , vol.5 , pp. 561-567
    • Maurel, D.1
  • 18
    • 3543036363 scopus 로고    scopus 로고
    • Closed state of both binding domains of homodimeric mGlureceptors is required for full activity
    • Kniazeff, J., et al. Closed state of both binding domains of homodimeric mGlureceptors is required for full activity. Nat. Struct. Mol. Biol. 11, 706-713(2004).
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 706-713
    • Kniazeff, J.1
  • 19
    • 84883148197 scopus 로고    scopus 로고
    • Segregation of family A G protein-coupled receptor protomersin the plasma membrane
    • Gavalas, A., et al. Segregation of family A G protein-coupled receptor protomersin the plasma membrane. Mol. Pharmacol. 84, 346-352 (2013).
    • (2013) Mol. Pharmacol. , vol.84 , pp. 346-352
    • Gavalas, A.1
  • 20
    • 84867045173 scopus 로고    scopus 로고
    • Distinct roles of metabotropic glutamate receptordimerization in agonist activation and G-protein coupling
    • El Moustaine, D., et al. Distinct roles of metabotropic glutamate receptordimerization in agonist activation and G-protein coupling. Proc. Natl Acad. Sci.USA 109, 16342-16347 (2012).
    • (2012) Proc. Natl Acad. Sci.USA , vol.109 , pp. 16342-16347
    • El Moustaine, D.1
  • 21
    • 84891438084 scopus 로고    scopus 로고
    • Selective actions of novel allosteric modulators reveal functionalheteromers of metabotropic glutamate receptors in the CNS
    • Yin, S., et al. Selective actions of novel allosteric modulators reveal functionalheteromers of metabotropic glutamate receptors in the CNS. J. Neurosci. 34,79-94 (2014).
    • (2014) J. Neurosci. , vol.34 , pp. 79-94
    • Yin, S.1
  • 22
    • 84991201313 scopus 로고    scopus 로고
    • Group 1 metabotropic glutamate receptors 1 and 5 form aprotein complex in mouse hippocampus and cortex
    • Pandya, N. J., et al. Group 1 metabotropic glutamate receptors 1 and 5 form aprotein complex in mouse hippocampus and cortex. Proteomics 16,2698-2705 (2016).
    • (2016) Proteomics , vol.16 , pp. 2698-2705
    • Pandya, N.J.1
  • 23
    • 84864773493 scopus 로고    scopus 로고
    • Stability ofGABAB receptor oligomers revealed by dual TR-FRET and drug-induced cellsurface targeting
    • Comps-Agrar, L., Kniazeff, J., Brock, C., Trinquet, E., Pin, J. P. Stability ofGABAB receptor oligomers revealed by dual TR-FRET and drug-induced cellsurface targeting. FASEB J. 26, 3430-3439 (2012).
    • (2012) FASEB J. , vol.26 , pp. 3430-3439
    • Comps-Agrar, L.1    Kniazeff, J.2    Brock, C.3    Trinquet, E.4    Pin, J.P.5
  • 24
    • 84872195772 scopus 로고    scopus 로고
    • Single-molecule analysis of fluorescently labeled G-proteincoupledreceptors reveals complexes with distinct dynamics and organization
    • Calebiro, D., et al. Single-molecule analysis of fluorescently labeled G-proteincoupledreceptors reveals complexes with distinct dynamics and organization.Proc. Natl Acad. Sci. USA 110, 743-748 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 743-748
    • Calebiro, D.1
  • 25
    • 72049124287 scopus 로고    scopus 로고
    • X-ray structure, symmetry andmechanism of an AMPA-subtype glutamate receptor
    • Sobolevsky, A. I., Rosconi, M. P., Gouaux, E. X-ray structure, symmetry andmechanism of an AMPA-subtype glutamate receptor. Nature 462, 745-756(2009).
    • (2009) Nature , vol.462 , pp. 745-756
    • Sobolevsky, A.I.1    Rosconi, M.P.2    Gouaux, E.3
  • 26
    • 0034718925 scopus 로고    scopus 로고
    • Structural basis of glutamate recognition by a dimericmetabotropic glutamate receptor
    • Kunishima, N., et al. Structural basis of glutamate recognition by a dimericmetabotropic glutamate receptor. Nature 407, 971-977 (2000).
    • (2000) Nature , vol.407 , pp. 971-977
    • Kunishima, N.1
  • 27
    • 0037022586 scopus 로고    scopus 로고
    • Structuralviews of the ligand-binding cores of a metabotropic glutamate receptorcomplexed with an antagonist and both glutamate and Gd3+
    • Tsuchiya, D., Kunishima, N., Kamiya, N., Jingami, H., Morikawa, K. Structuralviews of the ligand-binding cores of a metabotropic glutamate receptorcomplexed with an antagonist and both glutamate and Gd3+. Proc. Natl Acad.Sci. USA 99, 2660-2665 (2002).
    • (2002) Proc. Natl Acad.Sci. USA , vol.99 , pp. 2660-2665
    • Tsuchiya, D.1    Kunishima, N.2    Kamiya, N.3    Jingami, H.4    Morikawa, K.5
  • 28
    • 34247210665 scopus 로고    scopus 로고
    • Structures of the extracellularregions of the group II/III metabotropic glutamate receptors
    • Muto, T., Tsuchiya, D., Morikawa, K., Jingami, H. Structures of the extracellularregions of the group II/III metabotropic glutamate receptors. Proc. Natl Acad.Sci. USA 104, 3759-3764 (2007).
    • (2007) Proc. Natl Acad.Sci. USA , vol.104 , pp. 3759-3764
    • Muto, T.1    Tsuchiya, D.2    Morikawa, K.3    Jingami, H.4
  • 29
    • 84890434896 scopus 로고    scopus 로고
    • Structural mechanism ofligand activation in human GABAB receptor
    • Geng, Y., Bush, M., Mosyak, L., Wang, F., Fan, Q. R. Structural mechanism ofligand activation in human GABAB receptor. Nature 504, 254-259 (2013).Crystal structures of the heterodimeric extracellular domains of GABAB1 andGABAB2 in the empty, agonist-bound and antagonist-bound forms, revealthat receptor activation involves the formation of a novel interface betweensubunits.
    • (2013) Nature , vol.504 , pp. 254-259
    • Geng, Y.1    Bush, M.2    Mosyak, L.3    Wang, F.4    Fan, Q.R.5
  • 30
    • 1642499173 scopus 로고    scopus 로고
    • Locking the dimeric GABAB G-protein-coupled receptor in itsactive state
    • Kniazeff, J., et al. Locking the dimeric GABAB G-protein-coupled receptor in itsactive state. J. Neurosci. 24, 370-377 (2004).
    • (2004) J. Neurosci. , vol.24 , pp. 370-377
    • Kniazeff, J.1
  • 31
    • 0037143619 scopus 로고    scopus 로고
    • Closure of the Venus flytrap module of mGlu8 receptor andthe activation process: Insights from mutations converting antagonists intoagonists
    • Bessis, A.-S., et al. Closure of the Venus flytrap module of mGlu8 receptor andthe activation process: insights from mutations converting antagonists intoagonists. Proc. Natl Acad. Sci. USA 99, 11097-11102 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 11097-11102
    • Bessis, A.-S.1
  • 32
    • 84862842176 scopus 로고    scopus 로고
    • Structure and functional interaction of the extracellular domainof human GABAB receptor GBR2
    • Geng, Y., et al. Structure and functional interaction of the extracellular domainof human GABAB receptor GBR2. Nat. Neurosci. 15, 970-978 (2012).
    • (2012) Nat. Neurosci. , vol.15 , pp. 970-978
    • Geng, Y.1
  • 33
    • 84904994581 scopus 로고    scopus 로고
    • Structure of class C GPCR metabotropic glutamate receptor 5transmembrane domain
    • Doré, A. S., et al. Structure of class C GPCR metabotropic glutamate receptor 5transmembrane domain. Nature 511, 557-562 (2014).
    • (2014) Nature , vol.511 , pp. 557-562
    • Doré, A.S.1
  • 34
    • 84897580006 scopus 로고    scopus 로고
    • Structure of a class C GPCR metabotropic glutamate receptor 1bound to an allosteric modulator
    • Wu, H., et al. Structure of a class C GPCR metabotropic glutamate receptor 1bound to an allosteric modulator. Science 344, 58-64 (2014).
    • (2014) Science , vol.344 , pp. 58-64
    • Wu, H.1
  • 35
    • 84940544977 scopus 로고    scopus 로고
    • Fragment and structure-based drug discovery for aclass C GPCR: Discovery of the mGlu5 negative allosteric modulatorHTL14242 (3-chloro-5-[6-(5-fluoropyridin-2-yl)pyrimidin-4-yl]benzonitrile)
    • Christopher, J. A., et al. Fragment and structure-based drug discovery for aclass C GPCR: discovery of the mGlu5 negative allosteric modulatorHTL14242 (3-chloro-5-[6-(5-fluoropyridin-2-yl)pyrimidin-4-yl]benzonitrile).J. Med. Chem. 58, 6653-6664 (2015).
    • (2015) J. Med. Chem. , vol.58 , pp. 6653-6664
    • Christopher, J.A.1
  • 36
    • 40849124248 scopus 로고    scopus 로고
    • N-{4-chloro-2-[(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)methyl]phenyl}-2-hydroxybenzamide (CPPHA) actsthrough a novel site as a positive allosteric modulator of group 1 metabotropicglutamate receptors
    • Chen, Y., Goudet, C., Pin, J.-P., Conn, P. J. N. N-{4-chloro-2-[(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)methyl]phenyl}-2-hydroxybenzamide (CPPHA) actsthrough a novel site as a positive allosteric modulator of group 1 metabotropicglutamate receptors. Mol. Pharmacol. 73, 909-918 (2008).
    • (2008) Mol. Pharmacol. , vol.73 , pp. 909-918
    • Chen, Y.1    Goudet, C.2    Pin, J.-P.3    Conn, P.J.N.4
  • 37
    • 84928704210 scopus 로고    scopus 로고
    • Overlapping binding sites drive allosteric agonism and positivecooperativity in type 4 metabotropic glutamate receptors
    • Rovira, X., et al. Overlapping binding sites drive allosteric agonism and positivecooperativity in type 4 metabotropic glutamate receptors. FASEB J. 29,116-130 (2015).
    • (2015) FASEB J. , vol.29 , pp. 116-130
    • Rovira, X.1
  • 38
    • 0035927783 scopus 로고    scopus 로고
    • Agonist-independent activation of metabotropic glutamatereceptors by the intracellular protein Homer
    • Ango, F., et al. Agonist-independent activation of metabotropic glutamatereceptors by the intracellular protein Homer. Nature 411, 962-965(2001).
    • (2001) Nature , vol.411 , pp. 962-965
    • Ango, F.1
  • 39
    • 27844482134 scopus 로고    scopus 로고
    • A close structural analog of 2-methyl-6-(phenylethynyl)-pyridine acts as a neutral allosteric site ligand on metabotropic glutamatereceptor subtype 5 and blocks the effects of multiple allosteric modulators
    • Rodriguez, A. L., et al. A close structural analog of 2-methyl-6-(phenylethynyl)-pyridine acts as a neutral allosteric site ligand on metabotropic glutamatereceptor subtype 5 and blocks the effects of multiple allosteric modulators.Mol. Pharmacol. 68, 1793-1802 (2005).
    • (2005) Mol. Pharmacol. , vol.68 , pp. 1793-1802
    • Rodriguez, A.L.1
  • 40
    • 84930274249 scopus 로고    scopus 로고
    • Biased mGlu5-positive allosteric modulators provide in vivoefficacy without potentiating mGlu5 modulation of NMDAR currents
    • Rook, J. M., et al. Biased mGlu5-positive allosteric modulators provide in vivoefficacy without potentiating mGlu5 modulation of NMDAR currents. Neuron86, 1029-1040 (2015).Development of a biased mGlu5 PAM with therapeutic efficacy and animproved side-effect profile.
    • (2015) Neuron , vol.86 , pp. 1029-1040
    • Rook, J.M.1
  • 41
    • 34249661141 scopus 로고    scopus 로고
    • Common structural requirements for heptahelical domainfunction in class A and class C G protein-coupled receptors
    • Binet, V., et al. Common structural requirements for heptahelical domainfunction in class A and class C G protein-coupled receptors. J. Biol. Chem. 282,12154-12163 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 12154-12163
    • Binet, V.1
  • 42
    • 84876065856 scopus 로고    scopus 로고
    • Illuminating the activation mechanisms and allostericproperties of metabotropic glutamate receptors
    • Doumazane, E., et al. Illuminating the activation mechanisms and allostericproperties of metabotropic glutamate receptors. Proc. Natl Acad. Sci. USA 110,E1416-E1425 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. E1416-E1425
    • Doumazane, E.1
  • 43
    • 84948949784 scopus 로고    scopus 로고
    • Fine tuning of sub-millisecond conformational dynamicscontrols metabotropic glutamate receptors agonist efficacy
    • Olofsson, L., et al. Fine tuning of sub-millisecond conformational dynamicscontrols metabotropic glutamate receptors agonist efficacy. Nat. Commun. 5,5206 (2014).
    • (2014) Nat. Commun. , vol.5 , pp. 5206
    • Olofsson, L.1
  • 44
    • 84940478169 scopus 로고    scopus 로고
    • Conformational dynamics of a class CG-protein-coupled receptor
    • Vafabakhsh, R., Levitz, J., Isacoff, E. Y. Conformational dynamics of a class CG-protein-coupled receptor. Nature 524, 497-501 (2015).
    • (2015) Nature , vol.524 , pp. 497-501
    • Vafabakhsh, R.1    Levitz, J.2    Isacoff, E.Y.3
  • 45
    • 80053057994 scopus 로고    scopus 로고
    • Interdomain movements in metabotropic glutamate receptoractivation
    • Huang, S., et al. Interdomain movements in metabotropic glutamate receptoractivation. Proc. Natl Acad. Sci. USA 108, 15480-15485,2011
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 15480-15485
    • Huang, S.1
  • 46
    • 3042551375 scopus 로고    scopus 로고
    • Ligand-inducedrearrangement of the dimeric metabotropic glutamate receptor 1
    • Tateyama, M., Abe, H., Nakata, H., Saito, O., Kubo, Y. Ligand-inducedrearrangement of the dimeric metabotropic glutamate receptor 1 .Nat. Struct. Mol. Biol. 11, 637-642 (2004).
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 637-642
    • Tateyama, M.1    Abe, H.2    Nakata, H.3    Saito, O.4    Kubo, Y.5
  • 47
    • 84865180885 scopus 로고    scopus 로고
    • Sequential inter-and intrasubunit rearrangements duringactivation of dimeric metabotropic glutamate receptor 1
    • Hlavackova, V., et al. Sequential inter-and intrasubunit rearrangements duringactivation of dimeric metabotropic glutamate receptor 1. Sci. Signal. 5, 59(2012).
    • (2012) Sci. Signal. , vol.5 , pp. 59
    • Hlavackova, V.1
  • 48
    • 20044364938 scopus 로고    scopus 로고
    • Evidence for a single heptahelical domain being turned onupon activation of a dimeric GPCR
    • Hlavackova, V., et al. Evidence for a single heptahelical domain being turned onupon activation of a dimeric GPCR. EMBO J. 24, 499-509 (2005).
    • (2005) EMBO J. , vol.24 , pp. 499-509
    • Hlavackova, V.1
  • 49
    • 84919704267 scopus 로고    scopus 로고
    • Major ligand-induced rearrangement of the heptahelical domaininterface in a GPCR dimer
    • Xue, L., et al. Major ligand-induced rearrangement of the heptahelical domaininterface in a GPCR dimer. Nat. Chem. Biol. 11, 134-140 (2015).
    • (2015) Nat. Chem. Biol. , vol.11 , pp. 134-140
    • Xue, L.1
  • 50
    • 80052027428 scopus 로고    scopus 로고
    • Asymmetry of GPCR oligomers supportstheir functional relevance
    • Maurice, P., Kamal, M. & Jockers, R. Asymmetry of GPCR oligomers supports their functional relevance. Trends Pharmacol. Sci. 32, 514-520 (2011).
    • (2011) Trends Pharmacol. Sci. , vol.32 , pp. 514-520
    • Maurice, P.1    Kamal, M.2    Jockers, R.3
  • 51
    • 78650920787 scopus 로고    scopus 로고
    • Trans-activation between 7TM domains: Implication inheterodimeric GABAB receptor activation
    • Monnier, C., et al. Trans-activation between 7TM domains: implication inheterodimeric GABAB receptor activation. EMBO J. 30, 32-42 (2011).
    • (2011) EMBO J. , vol.30 , pp. 32-42
    • Monnier, C.1
  • 52
    • 21644435532 scopus 로고    scopus 로고
    • Asymmetric functioning of dimeric metabotropic glutamatereceptors disclosed by positive allosteric modulators
    • Goudet, C., et al. Asymmetric functioning of dimeric metabotropic glutamatereceptors disclosed by positive allosteric modulators. J. Biol. Chem. 280,24380-24385 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 24380-24385
    • Goudet, C.1
  • 53
    • 84975311440 scopus 로고    scopus 로고
    • A negative allosteric modulator modulates GABAB-receptorsignalling through GB2 subunits
    • Sun, B., et al. A negative allosteric modulator modulates GABAB-receptorsignalling through GB2 subunits. Biochem. J. 473, 779-787 (2016).
    • (2016) Biochem. J. , vol.473 , pp. 779-787
    • Sun, B.1
  • 54
    • 0346458626 scopus 로고    scopus 로고
    • Heptahelical domain of metabotropic glutamate receptor 5behaves like rhodopsin-like receptors
    • Goudet, C., et al. Heptahelical domain of metabotropic glutamate receptor 5behaves like rhodopsin-like receptors. Proc. Natl Acad. Sci. USA 101, 378-383(2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 378-383
    • Goudet, C.1
  • 55
    • 84879118132 scopus 로고    scopus 로고
    • Arrestins come of age: A personal historical perspective
    • Lefkowitz, R. J. Arrestins come of age: a personal historical perspective. Prog.Mol. Biol. Transl. Sci. 118, 3-18 (2013).
    • (2013) Prog.Mol. Biol. Transl. Sci. , vol.118 , pp. 3-18
    • Lefkowitz, R.J.1
  • 56
    • 84872138902 scopus 로고    scopus 로고
    • Molecular mechanisms that desensitizemetabotropic glutamate receptor signaling: An overview
    • Iacovelli, L., Nicoletti, F., De Blasi, A. Molecular mechanisms that desensitizemetabotropic glutamate receptor signaling: an overview. Neuropharmacology66, 24-30 (2013).
    • (2013) Neuropharmacology , vol.66 , pp. 24-30
    • Iacovelli, L.1    Nicoletti, F.2    De Blasi, A.3
  • 57
    • 0042575596 scopus 로고    scopus 로고
    • Phosphorylationindependentdesensitization of GABAB receptor by GRK4
    • Perroy, J., Adam, L., Qanbar, R., Chénier, S., Bouvier, M. Phosphorylationindependentdesensitization of GABAB receptor by GRK4. EMBO J. 22,3816-3824 (2003).
    • (2003) EMBO J. , vol.22 , pp. 3816-3824
    • Perroy, J.1    Adam, L.2    Qanbar, R.3    Chénier, S.4    Bouvier, M.5
  • 58
    • 0038146946 scopus 로고    scopus 로고
    • The metabotropic glutamate receptor mGluR5 isendocytosed by a clathrin-independent pathway
    • Fourgeaud, L., et al. The metabotropic glutamate receptor mGluR5 isendocytosed by a clathrin-independent pathway. J. Biol. Chem. 278,12222-12230 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 12222-12230
    • Fourgeaud, L.1
  • 59
    • 1842424991 scopus 로고    scopus 로고
    • Phosphorylation and chronic agonist treatment atypicallymodulate GABAB receptor cell surface stability
    • Fairfax, B. P., et al. Phosphorylation and chronic agonist treatment atypicallymodulate GABAB receptor cell surface stability. J. Biol. Chem. 279,12565-12573 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 12565-12573
    • Fairfax, B.P.1
  • 60
    • 84855839174 scopus 로고    scopus 로고
    • GABAB receptors-associated proteins: Potential drugtargets in neurological disorders
    • Lujan, R., Ciruela, F. GABAB receptors-associated proteins: potential drugtargets in neurological disorders Curr. Drug Targets 13, 129-144(2012).
    • (2012) Curr. Drug Targets , vol.13 , pp. 129-144
    • Lujan, R.1    Ciruela, F.2
  • 61
    • 33646529626 scopus 로고    scopus 로고
    • Molecular diversity, trafficking and subcellularlocalization of GABAB receptors
    • Bettler, B., Tiao, J. Y. Molecular diversity, trafficking and subcellularlocalization of GABAB receptors. Pharmacol. Ther. 110, 533-543 (2006).
    • (2006) Pharmacol. Ther. , vol.110 , pp. 533-543
    • Bettler, B.1    Tiao, J.Y.2
  • 62
    • 84887476732 scopus 로고    scopus 로고
    • GABAB receptor trafficking and interacting proteins: Targets for thedevelopment of highly specific therapeutic strategies to treat neurologicaldisorders Biochem
    • Benke, D. GABAB receptor trafficking and interacting proteins: targets for thedevelopment of highly specific therapeutic strategies to treat neurologicaldisorders Biochem. Pharmacol. 86, 1525-1530 (2013).
    • (2013) Pharmacol. , vol.86 , pp. 1525-1530
    • Benke, D.1
  • 63
    • 77949494310 scopus 로고    scopus 로고
    • GPCR interactingproteins (GIPs) in the nervous system: Roles in physiology and pathologies
    • Bockaert, J., Perroy, J., Bécamel, C., Marin, P., Fagni, L. GPCR interactingproteins (GIPs) in the nervous system: roles in physiology and pathologies.Annu. Rev. Pharmacol. Toxicol. 50, 89-109 (2010).
    • (2010) Annu. Rev. Pharmacol. Toxicol. , vol.50 , pp. 89-109
    • Bockaert, J.1    Perroy, J.2    Bécamel, C.3    Marin, P.4    Fagni, L.5
  • 64
    • 84855828229 scopus 로고    scopus 로고
    • Metabotropic glutamate receptors and interacting proteins: Evolvingdrug targets
    • Enz, R. Metabotropic glutamate receptors and interacting proteins: evolvingdrug targets. Curr. Drug Targets 13, 145-156 (2012).
    • (2012) Curr. Drug Targets , vol.13 , pp. 145-156
    • Enz, R.1
  • 65
    • 84901840531 scopus 로고    scopus 로고
    • Auxiliary GABAB receptor subunits uncouple G protein subunits from effector channels to induce desensitization
    • Turecek, R., et al. Auxiliary GABAB receptor subunits uncouple G protein subunits from effector channels to induce desensitization. Neuron 82,1032-1044 (2014).
    • (2014) Neuron , vol.82 , pp. 1032-1044
    • Turecek, R.1
  • 66
    • 0018125541 scopus 로고
    • Mode of coupling between the-adrenergicreceptor and adenylate cyclase in turkey erythrocytes
    • Tolkovsky, A. M., Levitzki, A. Mode of coupling between the-adrenergicreceptor and adenylate cyclase in turkey erythrocytes. Biochemistry 17,3795 (1978).
    • (1978) Biochemistry , vol.17 , pp. 3795
    • Tolkovsky, A.M.1    Levitzki, A.2
  • 67
    • 84908374412 scopus 로고    scopus 로고
    • Pharmacological characterization of GABAB receptor subtypesassembled with auxiliary KCTD subunits
    • Rajalu, M., et al. Pharmacological characterization of GABAB receptor subtypesassembled with auxiliary KCTD subunits. Neuropharmacology 88, 145-154(2015).
    • (2015) Neuropharmacology , vol.88 , pp. 145-154
    • Rajalu, M.1
  • 68
    • 84922708295 scopus 로고    scopus 로고
    • GABA blocks pathological but not acute TRPV1 pain signals
    • Hanack, C., et al. GABA blocks pathological but not acute TRPV1 pain signals. Cell160, 759-770 (2015).
    • (2015) Cell , vol.160 , pp. 759-770
    • Hanack, C.1
  • 69
    • 84865412736 scopus 로고    scopus 로고
    • Endoplasmic reticulum sorting and kinesin-1 command thetargeting of axonal GABAB receptors
    • Valdés, V., et al. Endoplasmic reticulum sorting and kinesin-1 command thetargeting of axonal GABAB receptors. PLoS One 7, e44168 (2012).
    • (2012) PLoS One , vol.7 , pp. e44168
    • Valdés, V.1
  • 70
    • 0035809914 scopus 로고    scopus 로고
    • Cargo of kinesin identified as JIP scaffolding proteins andassociated signaling molecules
    • Verhey, K. J., et al. Cargo of kinesin identified as JIP scaffolding proteins andassociated signaling molecules. J. Cell Biol. 152, 959-970 (2001).
    • (2001) J. Cell Biol. , vol.152 , pp. 959-970
    • Verhey, K.J.1
  • 71
    • 64849104680 scopus 로고    scopus 로고
    • Calsyntenins mediate TGN exit of APP in a kinesin-1-dependent manner
    • Ludwig, A., et al. Calsyntenins mediate TGN exit of APP in a kinesin-1-dependent manner. Traffic 10, 572-589 (2009).
    • (2009) Traffic , vol.10 , pp. 572-589
    • Ludwig, A.1
  • 72
    • 84864881068 scopus 로고    scopus 로고
    • Impairment of GABAB receptor dimer by endogenous 14-3-3in chronic pain conditions
    • Laffray, S., et al. Impairment of GABAB receptor dimer by endogenous 14-3-3in chronic pain conditions. EMBO J. 31, 3239-3251 (2012).
    • (2012) EMBO J. , vol.31 , pp. 3239-3251
    • Laffray, S.1
  • 73
    • 84924655016 scopus 로고    scopus 로고
    • Rapid antidepressants stimulate the decoupling ofGABAB receptors from GIRK/Kir3 channels through increased protein stabilityof 14-3-3
    • Workman, E. R., et al. Rapid antidepressants stimulate the decoupling ofGABAB receptors from GIRK/Kir3 channels through increased protein stabilityof 14-3-3 . Mol. Psychiatry 20, 298-310 (2015).
    • (2015) Mol. Psychiatry , vol.20 , pp. 298-310
    • Workman, E.R.1
  • 74
    • 65549160499 scopus 로고    scopus 로고
    • Metabotropic glutamate type 5, dopamine D2 and adenosineA2a receptors form higher-order oligomers in living cells
    • Cabello, N., et al. Metabotropic glutamate type 5, dopamine D2 and adenosineA2a receptors form higher-order oligomers in living cells. J. Neurochem. 109,1497-1507 (2009).
    • (2009) J. Neurochem. , vol.109 , pp. 1497-1507
    • Cabello, N.1
  • 75
    • 81855189491 scopus 로고    scopus 로고
    • Decoding the signaling of a GPCR heteromeric complexreveals a unifying mechanism of action of antipsychotic drugs
    • Fribourg, M., et al. Decoding the signaling of a GPCR heteromeric complexreveals a unifying mechanism of action of antipsychotic drugs. Cell 147,1011-1023 (2011).
    • (2011) Cell , vol.147 , pp. 1011-1023
    • Fribourg, M.1
  • 76
    • 84879966473 scopus 로고    scopus 로고
    • Ligands that interact with putative MOR-mGluR5 heteromer inmice with inflammatory pain produce potent antinociception
    • Akgün, E., et al. Ligands that interact with putative MOR-mGluR5 heteromer inmice with inflammatory pain produce potent antinociception. Proc. Natl Acad.Sci. USA 110, 11595-11599 (2013).
    • (2013) Proc. Natl Acad.Sci. USA , vol.110 , pp. 11595-11599
    • Akgün, E.1
  • 77
    • 84975061697 scopus 로고    scopus 로고
    • A critical role of striatal A2A R-mGlu5 R interactions inmodulating the psychomotor and drug-seeking effects of methamphetamine
    • Wright, S. R., et al. A critical role of striatal A2A R-mGlu5 R interactions inmodulating the psychomotor and drug-seeking effects of methamphetamine.Addict. Biol. 21, 811-825 (2016).
    • (2016) Addict. Biol. , vol.21 , pp. 811-825
    • Wright, S.R.1
  • 78
    • 84979010983 scopus 로고    scopus 로고
    • Functional role of striatal A2A D2 and mGlu5 receptorinteractions in regulating striatopallidal GABA neuronal transmission
    • Beggiato, S., et al. Functional role of striatal A2A, D2, and mGlu5 receptorinteractions in regulating striatopallidal GABA neuronal transmission.J. Neurochem. 138, 254-264 (2016).
    • (2016) J. Neurochem. , vol.138 , pp. 254-264
    • Beggiato, S.1
  • 79
    • 84947500240 scopus 로고    scopus 로고
    • The effective application of biased signaling to new drug discovery
    • Kenakin, T. The effective application of biased signaling to new drug discovery.Mol. Pharmacol. 88, 1055-1061 (2015).
    • (2015) Mol. Pharmacol. , vol.88 , pp. 1055-1061
    • Kenakin, T.1
  • 80
    • 78650230675 scopus 로고    scopus 로고
    • Homeostatic scaling requires group i mGluR activationmediated by Homer1a
    • Hu, J. H., et al. Homeostatic scaling requires group I mGluR activationmediated by Homer1a. Neuron 68, 1128-1142 (2010).
    • (2010) Neuron , vol.68 , pp. 1128-1142
    • Hu, J.H.1
  • 81
    • 84862777306 scopus 로고    scopus 로고
    • Disrupted Homer scaffolds mediate abnormal mGluR5function in a mouse model of fragile X syndrome
    • Ronesi, J.A., et al. Disrupted Homer scaffolds mediate abnormal mGluR5function in a mouse model of fragile X syndrome. Nat. Neurosci. 15,431-440 (2012).
    • (2012) Nat. Neurosci. , vol.15 , pp. 431-440
    • Ronesi, J.A.1
  • 82
    • 84939164437 scopus 로고    scopus 로고
    • Novel allosteric modulators of Gprotein-coupled receptors
    • Gentry, P. R., Sexton, P. M., Christopoulos, A. Novel allosteric modulators of Gprotein-coupled receptors. J. Biol. Chem. 290, 19478-19488 (2015).
    • (2015) J. Biol. Chem. , vol.290 , pp. 19478-19488
    • Gentry, P.R.1    Sexton, P.M.2    Christopoulos, A.3
  • 83
    • 84978402413 scopus 로고    scopus 로고
    • Cellular synaptic, and circuit effects ofantibodies in autoimmune CNS synaptopathies
    • Jain, A., Balice-Gordon, R. Cellular, synaptic, and circuit effects ofantibodies in autoimmune CNS synaptopathies. Handb. Clin. Neurol. 133,77-93 (2016).
    • (2016) Handb. Clin. Neurol. , vol.133 , pp. 77-93
    • Jain, A.1    Balice-Gordon, R.2
  • 84
    • 84857753632 scopus 로고    scopus 로고
    • A high-affinity, dimeric inhibitor of PSD-95 bivalently interactswith PDZ1-2 and protects against ischemic brain damage
    • Bach, A., et al. A high-affinity, dimeric inhibitor of PSD-95 bivalently interactswith PDZ1-2 and protects against ischemic brain damage. Proc. Natl Acad. Sci.USA 109, 3317-3322 (2012).
    • (2012) Proc. Natl Acad. Sci.USA , vol.109 , pp. 3317-3322
    • Bach, A.1
  • 85
    • 57649223726 scopus 로고    scopus 로고
    • The sushi domains of secreted GABAB1 isoforms selectively impairGABAB heteroreceptor function
    • Tiao, J. Y., et al. The sushi domains of secreted GABAB1 isoforms selectively impairGABAB heteroreceptor function. J. Biol. Chem. 283, 31005-31011 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 31005-31011
    • Tiao, J.Y.1
  • 87
    • 75349088067 scopus 로고    scopus 로고
    • The sushi domains of GABAB receptors function as axonaltargeting signals
    • Biermann, B., et al. The sushi domains of GABAB receptors function as axonaltargeting signals. J. Neurosci. 30, 1385-1394 (2010).
    • (2010) J. Neurosci. , vol.30 , pp. 1385-1394
    • Biermann, B.1
  • 88
    • 77956389608 scopus 로고    scopus 로고
    • NMDA receptor-dependent GABAB receptor internalization viaCaMKII phosphorylation of serine 867 in GABAB1
    • Guetg, N., et al. NMDA receptor-dependent GABAB receptor internalization viaCaMKII phosphorylation of serine 867 in GABAB1. Proc. Natl Acad. Sci. USA107, 13924-13929 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 13924-13929
    • Guetg, N.1
  • 89
    • 33846809418 scopus 로고    scopus 로고
    • GISP: A novel brain-specific protein that promotessurface expression and function of GABAB receptors
    • Kantamneni, S., et al. GISP: a novel brain-specific protein that promotessurface expression and function of GABAB receptors. J. Neurochem. 100,1003-1017 (2007).
    • (2007) J. Neurochem. , vol.100 , pp. 1003-1017
    • Kantamneni, S.1
  • 90
    • 84934887578 scopus 로고    scopus 로고
    • GABAB receptor deficiency causes failure of neuronalhomeostasis in hippocampal networks
    • Vertkin, I., et al. GABAB receptor deficiency causes failure of neuronalhomeostasis in hippocampal networks. Proc. Natl Acad. Sci. USA 112,E3291-E3299 (2015).
    • (2015) Proc. Natl Acad. Sci. USA , vol.112 , pp. E3291-E3299
    • Vertkin, I.1
  • 91
    • 84908014949 scopus 로고    scopus 로고
    • GINIP, a Gi-interacting protein, functions as a keymodulator of peripheral GABAB receptor-mediated analgesia
    • Gaillard, S., et al. GINIP, a Gi-interacting protein, functions as a keymodulator of peripheral GABAB receptor-mediated analgesia. Neuron 84,123-136 (2014).
    • (2014) Neuron , vol.84 , pp. 123-136
    • Gaillard, S.1
  • 92
    • 77952886365 scopus 로고    scopus 로고
    • G 5 recruits R7 RGS proteins to GIRK channels to regulate thetiming of neuronal inhibitory signaling
    • Xie, K., et al. G 5 recruits R7 RGS proteins to GIRK channels to regulate thetiming of neuronal inhibitory signaling. Nat. Neurosci. 13, 661-663 (2010).
    • (2010) Nat. Neurosci. , vol.13 , pp. 661-663
    • Xie, K.1
  • 93
    • 0032192487 scopus 로고    scopus 로고
    • Homer binds a novel proline-rich motif and links group 1metabotropic glutamate receptors with IP3 receptors
    • Tu, J. C., et al. Homer binds a novel proline-rich motif and links group 1metabotropic glutamate receptors with IP3 receptors. Neuron 21, 717-726(1998).
    • (1998) Neuron , vol.21 , pp. 717-726
    • Tu, J.C.1
  • 94
    • 79955776373 scopus 로고    scopus 로고
    • Differential binding of calmodulin to groupI metabotropic glutamate receptors regulates receptor trafficking andsignaling
    • Choi, K. Y., Chung, S., Roche, K. W. Differential binding of calmodulin to groupI metabotropic glutamate receptors regulates receptor trafficking andsignaling. J. Neurosci. 31, 5921-5930 (2011).
    • (2011) J. Neurosci. , vol.31 , pp. 5921-5930
    • Choi, K.Y.1    Chung, S.2    Roche, K.W.3
  • 95
    • 84861539413 scopus 로고    scopus 로고
    • Preso1 dynamically regulates group i metabotropic glutamatereceptors
    • Hu, J. H., et al. Preso1 dynamically regulates group I metabotropic glutamatereceptors. Nat. Neurosci. 15, 836-844 (2012).
    • (2012) Nat. Neurosci. , vol.15 , pp. 836-844
    • Hu, J.H.1
  • 96
    • 84869068065 scopus 로고    scopus 로고
    • PKC phosphorylation regulates mGluR5 trafficking by enhancingbinding of Siah-1A
    • Ko, S. J., et al. PKC phosphorylation regulates mGluR5 trafficking by enhancingbinding of Siah-1A. J. Neurosci. 32, 16391-16401 (2012).
    • (2012) J. Neurosci. , vol.32 , pp. 16391-16401
    • Ko, S.J.1
  • 97
    • 0037083370 scopus 로고    scopus 로고
    • Tamalin, a PDZ domain-containing protein, links a proteincomplex formation of group 1 metabotropic glutamate receptors and theguanine nucleotide exchange factor cytohesins
    • Kitano, J., et al. Tamalin, a PDZ domain-containing protein, links a proteincomplex formation of group 1 metabotropic glutamate receptors and theguanine nucleotide exchange factor cytohesins. J. Neurosci. 22, 1280-1289(2002).
    • (2002) J. Neurosci. , vol.22 , pp. 1280-1289
    • Kitano, J.1
  • 98
    • 0344443184 scopus 로고    scopus 로고
    • Activation of the TRPC1 cation channel by metabotropicglutamate receptor mGluR1
    • Kim, S. J., et al. Activation of the TRPC1 cation channel by metabotropicglutamate receptor mGluR1. Nature 426, 285-291 (2003).
    • (2003) Nature , vol.426 , pp. 285-291
    • Kim, S.J.1
  • 99
    • 27744487501 scopus 로고    scopus 로고
    • Metabotropic glutamate receptor 8-expressing nerveterminals target subsets of GABAergic neurons in the hippocampus
    • Ferraguti, F., et al. Metabotropic glutamate receptor 8-expressing nerveterminals target subsets of GABAergic neurons in the hippocampus.J. Neurosci. 25, 10520-10536 (2005).
    • (2005) J. Neurosci. , vol.25 , pp. 10520-10536
    • Ferraguti, F.1


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