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Volumn 11, Issue 7, 2004, Pages 637-642

Ligand-induced rearrangement of the dimeric metabotropic glutamate receptor 1α

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; GUANINE NUCLEOTIDE BINDING PROTEIN; LIGAND; METABOTROPIC RECEPTOR 1; METABOTROPIC RECEPTOR 1ALPHA; UNCLASSIFIED DRUG;

EID: 3042551375     PISSN: 15459993     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsmb770     Document Type: Article
Times cited : (159)

References (36)
  • 1
    • 0028139045 scopus 로고
    • Reduced hippocampal long-term potentiation and context-specific deficit in associative learning in mGluR 1 mutant mice
    • Aiba, A. et al. Reduced hippocampal long-term potentiation and context-specific deficit in associative learning in mGluR1 mutant mice. Cell 79, 365-375 (1994).
    • (1994) Cell , vol.79 , pp. 365-375
    • Aiba, A.1
  • 2
    • 0028149789 scopus 로고
    • Deficient cerebellar long-term depression and impaired motor learning in mGluR1 mutant mice
    • Aiba, A. et al. Deficient cerebellar long-term depression and impaired motor learning in mGluR1 mutant mice. Cell 79, 377-388 (1994).
    • (1994) Cell , vol.79 , pp. 377-388
    • Aiba, A.1
  • 3
    • 0027997686 scopus 로고
    • Motor deficit and impairment of synaptic plasticity in mice lacking mGluR1
    • Conquet, F. et al. Motor deficit and impairment of synaptic plasticity in mice lacking mGluR1. Nature 372, 237-243 (1994).
    • (1994) Nature , vol.372 , pp. 237-243
    • Conquet, F.1
  • 4
    • 0028284466 scopus 로고
    • Antibodies inactivating mGluR1 metabotropic glutamate receptor block long-term depression in cultured Purkinje cells
    • Shigemoto, R., Abe, T., Nomura, S., Nakanishi, S. & Hirano, T. Antibodies inactivating mGluR1 metabotropic glutamate receptor block long-term depression in cultured Purkinje cells. Neuron 12, 1245-1255 (1994).
    • (1994) Neuron , vol.12 , pp. 1245-1255
    • Shigemoto, R.1    Abe, T.2    Nomura, S.3    Nakanishi, S.4    Hirano, T.5
  • 5
    • 0035504328 scopus 로고    scopus 로고
    • Structural, signalling and regulatory properties of the group I metabotropic glutamate receptors: Prototypic family C G-protein-coupled receptors
    • Hermans, E. & Challiss, R.A. Structural, signalling and regulatory properties of the group I metabotropic glutamate receptors: prototypic family C G-protein-coupled receptors. Biochem. J. 359, 465-484 (2001).
    • (2001) Biochem. J. , vol.359 , pp. 465-484
    • Hermans, E.1    Challiss, R.A.2
  • 6
    • 0029907599 scopus 로고    scopus 로고
    • Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin
    • Farrens, D.L., Altenbach, C., Yang, K., Hubbell, W.L. & Khorana, H.G. Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin. Science 274, 768-770 (1996).
    • (1996) Science , vol.274 , pp. 768-770
    • Farrens, D.L.1    Altenbach, C.2    Yang, K.3    Hubbell, W.L.4    Khorana, H.G.5
  • 7
    • 0035932989 scopus 로고    scopus 로고
    • Agonist-induced conformational changes in the G-protein-coupling domain of the beta2 adrenergic receptor
    • Ghanouni, P., Steenhuis, J.J., Farrens, D.L. & Kobilka, B.K. Agonist-induced conformational changes in the G-protein-coupling domain of the beta 2 adrenergic receptor. Proc. Natl. Acad. Sci. USA 98, 5997-6002 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 5997-6002
    • Ghanouni, P.1    Steenhuis, J.J.2    Farrens, D.L.3    Kobilka, B.K.4
  • 8
    • 0038729670 scopus 로고    scopus 로고
    • Measurement of the millisecond activation switch of G protein-coupled receptors in living cells
    • Vilardaga, J.P., Bunemann, M., Krasel, C., Castro, M. & Lohse, M.J. Measurement of the millisecond activation switch of G protein-coupled receptors in living cells. Nat. Biotechnol. 21, 807-812 (2003).
    • (2003) Nat. Biotechnol. , vol.21 , pp. 807-812
    • Vilardaga, J.P.1    Bunemann, M.2    Krasel, C.3    Castro, M.4    Lohse, M.J.5
  • 9
    • 0034718925 scopus 로고    scopus 로고
    • Structural basis of glutamate recognition by a dimeric metabotropic glutamate receptor
    • Kunishima, N. et al. Structural basis of glutamate recognition by a dimeric metabotropic glutamate receptor. Nature 407, 971-977 (2000).
    • (2000) Nature , vol.407 , pp. 971-977
    • Kunishima, N.1
  • 11
    • 0033028258 scopus 로고    scopus 로고
    • CPCCOEt, a noncompetitive metabotropic glutamate receptor 1 antagonist, inhibits receptor signaling without affecting glutamate binding
    • Litschig, S. et al. CPCCOEt, a noncompetitive metabotropic glutamate receptor 1 antagonist, inhibits receptor signaling without affecting glutamate binding. Mol Pharmacol 55, 453-461 (1999).
    • (1999) Mol Pharmacol , vol.55 , pp. 453-461
    • Litschig, S.1
  • 13
    • 0033548048 scopus 로고    scopus 로고
    • Erythropoietin receptor activation by a ligand-induced conformation change
    • Remy, I., Wilson, I.A. & Michnick, S.W. Erythropoietin receptor activation by a ligand-induced conformation change. Science 283, 990-993 (1999).
    • (1999) Science , vol.283 , pp. 990-993
    • Remy, I.1    Wilson, I.A.2    Michnick, S.W.3
  • 14
    • 0037423395 scopus 로고    scopus 로고
    • Amino acid mutagenesis of the ligand binding site and the dimer interface of the metabotropic glutamate receptor 1. Identification of crucial residues for setting the activated state
    • Sato, T., Shimada, Y., Nagasawa, N., Nakanishi, S. & Jingami, H. Amino acid mutagenesis of the ligand binding site and the dimer interface of the metabotropic glutamate receptor 1. Identification of crucial residues for setting the activated state. J. Biol. Chem. 278, 4314-4321 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 4314-4321
    • Sato, T.1    Shimada, Y.2    Nagasawa, N.3    Nakanishi, S.4    Jingami, H.5
  • 15
    • 0038540540 scopus 로고    scopus 로고
    • 3+ binding site of metabotropic glutamate receptor 1α
    • 3+ binding site of metabotropic glutamate receptor 1α. FEBS Lett. 545, 233-238 (2003).
    • (2003) FEBS Lett. , vol.545 , pp. 233-238
    • Abe, H.1    Tateyama, M.2    Kubo, Y.3
  • 16
    • 0032489519 scopus 로고    scopus 로고
    • Role of the second and third intracellular loops of metabotropic glutamate receptors in mediating dual signal transduction activation
    • Francesconi, A. & Duvoisin, R.M. Role of the second and third intracellular loops of metabotropic glutamate receptors in mediating dual signal transduction activation. J. Biol. Chem. 273, 5615-5624 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 5615-5624
    • Francesconi, A.1    Duvoisin, R.M.2
  • 17
    • 0030050977 scopus 로고    scopus 로고
    • The second intracellular loop of metabotropic glutamate receptor 1 cooperates with the other intracellular domains to control coupling to G-proteins
    • Gomeza, J. et al. The second intracellular loop of metabotropic glutamate receptor 1 cooperates with the other intracellular domains to control coupling to G-proteins. J. Biol. Chem. 271, 2199-2205 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 2199-2205
    • Gomeza, J.1
  • 18
    • 0030610646 scopus 로고    scopus 로고
    • 2+ based on green fluorescent proteins and calmodulin
    • 2+ based on green fluorescent proteins and calmodulin. Nature 388, 882-887 (1997).
    • (1997) Nature , vol.388 , pp. 882-887
    • Miyawaki, A.1
  • 20
    • 0038664388 scopus 로고    scopus 로고
    • Conformational rearrangements associated with the gating of the G protein-coupled potassium channel revealed by FRET microscopy
    • Riven, I., Kalmanzon, E., Segev, L. & Reuveny, E. Conformational rearrangements associated with the gating of the G protein-coupled potassium channel revealed by FRET microscopy. Neuron 38, 225-235 (2003).
    • (2003) Neuron , vol.38 , pp. 225-235
    • Riven, I.1    Kalmanzon, E.2    Segev, L.3    Reuveny, E.4
  • 21
    • 0347364629 scopus 로고    scopus 로고
    • Gi protein activation in intact cells involves subunit rearrangement rather than dissociation
    • Bunemann, M., Frank, M. & Lohse, M.J. Gi protein activation in intact cells involves subunit rearrangement rather than dissociation. Proc. Natl. Acad. Sci. USA 100, 16077-16082 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 16077-16082
    • Bunemann, M.1    Frank, M.2    Lohse, M.J.3
  • 22
    • 0037343944 scopus 로고    scopus 로고
    • Visualization of the spatial and temporal dynamics of intracellular signaling
    • Miyawaki, A. Visualization of the spatial and temporal dynamics of intracellular signaling. Dev. Cell 4, 295-305 (2003).
    • (2003) Dev. Cell , vol.4 , pp. 295-305
    • Miyawaki, A.1
  • 23
    • 0035315984 scopus 로고    scopus 로고
    • A real-time view of life within 100 nm of the plasma membrane
    • Steyer, J.A. & Almers, W. A real-time view of life within 100 nm of the plasma membrane. Nat. Rev. Mol. Cell Biol. 2, 268-275 (2001).
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 268-275
    • Steyer, J.A.1    Almers, W.2
  • 24
    • 0034810232 scopus 로고    scopus 로고
    • Reliable and global measurement of fluorescence resonance energy transfer using fluorescence microscopes
    • Xia, Z. & Liu, Y. Reliable and global measurement of fluorescence resonance energy transfer using fluorescence microscopes. Biophys. J. 81, 2395-2402 (2001).
    • (2001) Biophys. J. , vol.81 , pp. 2395-2402
    • Xia, Z.1    Liu, Y.2
  • 25
    • 0036415131 scopus 로고    scopus 로고
    • Probing intermolecular protein-protein interactions in the calcium-sensing receptor homodimer using bioluminescence resonance energy transfer (BRET)
    • Jensen, A.A., Hansen, J.L., Sheikh, S.P. & Brauner-Osborne, H. Probing intermolecular protein-protein interactions in the calcium-sensing receptor homodimer using bioluminescence resonance energy transfer (BRET). Eur. J. Biochem. 269, 5076-5087 (2002).
    • (2002) Eur. J. Biochem. , vol.269 , pp. 5076-5087
    • Jensen, A.A.1    Hansen, J.L.2    Sheikh, S.P.3    Brauner-Osborne, H.4
  • 26
    • 0033624305 scopus 로고    scopus 로고
    • 2+ sensitivity of mGluR1α induces an increase in the basal cAMP level by direct coupling with Gs protein in transfected CHO cells
    • 2+ sensitivity of mGluR1α induces an increase in the basal cAMP level by direct coupling with Gs protein in transfected CHO cells. Receptors Channels 7, 77-91 (2000).
    • (2000) Receptors Channels , vol.7 , pp. 77-91
    • Miyashita, T.1    Kubo, Y.2
  • 27
    • 0029780351 scopus 로고    scopus 로고
    • The molecular structure of green fluorescent protein
    • Yang, F., Moss, L.G. & Phillips, G.N. Jr. The molecular structure of green fluorescent protein. Nat. Biotechnol. 14, 1246-1251 (1996).
    • (1996) Nat. Biotechnol. , vol.14 , pp. 1246-1251
    • Yang, F.1    Moss, L.G.2    Phillips Jr., G.N.3
  • 28
    • 0031983457 scopus 로고    scopus 로고
    • A cluster of basic residues in the carboxyl-terminal tail of the short metabotropic glutamate receptor 1 variants impairs their coupling to phospholipase C
    • Mary, S., Gomeza, J., Prezeau, L., Bockaert, J. & Pin, J.P. A cluster of basic residues in the carboxyl-terminal tail of the short metabotropic glutamate receptor 1 variants impairs their coupling to phospholipase C. J. Biol. Chem. 273, 425-432 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 425-432
    • Mary, S.1    Gomeza, J.2    Prezeau, L.3    Bockaert, J.4    Pin, J.P.5
  • 29
    • 0036462446 scopus 로고    scopus 로고
    • Allosteric modulators of group I metabotropic glutamate receptors: Novel subtype-selective ligands and therapeutic perspectives
    • Gasparini, F., Kuhn, R. & Pin, J.P. Allosteric modulators of group I metabotropic glutamate receptors: novel subtype-selective ligands and therapeutic perspectives. Curr. Opin. Pharmacol. 2, 43-49 (2002).
    • (2002) Curr. Opin. Pharmacol. , vol.2 , pp. 43-49
    • Gasparini, F.1    Kuhn, R.2    Pin, J.P.3
  • 30
    • 0034721795 scopus 로고    scopus 로고
    • The non-competitive antagonists 2-methyl-6-(phenylethynyl)pyridine and 7-hydroxyiminocyclopropan[b]chromen-1a-carboxylic acid ethyl ester interact with overlapping binding pockets in the transmembrane region of group I metabotropic glutamate receptors
    • Pagano, A. et al. The non-competitive antagonists 2-methyl-6- (phenylethynyl)pyridine and 7-hydroxyiminocyclopropan[b]chromen-1a-carboxylic acid ethyl ester interact with overlapping binding pockets in the transmembrane region of group I metabotropic glutamate receptors. J. Biol. Chem. 275, 33750-33758 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 33750-33758
    • Pagano, A.1
  • 31
    • 0032512921 scopus 로고    scopus 로고
    • 2+-sensing function of the metabotropic glutamate receptors
    • 2+-sensing function of the metabotropic glutamate receptors. Science 279, 1722-1725 (1998).
    • (1998) Science , vol.279 , pp. 1722-1725
    • Kubo, Y.1    Miyashita, T.2    Murata, Y.3
  • 33
    • 0034604451 scopus 로고    scopus 로고
    • Crystal structure of rhodopsin: A G protein-coupled receptor
    • Palczewski, K. et al. Crystal structure of rhodopsin: a G protein-coupled receptor. Science 289, 739-745 (2000).
    • (2000) Science , vol.289 , pp. 739-745
    • Palczewski, K.1
  • 34
    • 0042029701 scopus 로고    scopus 로고
    • Membrane topology of a metabotropic glutamate receptor
    • Bhave, G. et al. Membrane topology of a metabotropic glutamate receptor. J. Biol. Chem. 278, 30294-30301 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 30294-30301
    • Bhave, G.1
  • 35
    • 0032192487 scopus 로고    scopus 로고
    • Homer binds a novel proline-rich motif and links group 1 metabotropic glutamate receptors with IP3 receptors
    • Tu, J.C. et al. Homer binds a novel proline-rich motif and links group 1 metabotropic glutamate receptors with IP3 receptors. Neuron 21, 717-726 (1998).
    • (1998) Neuron , vol.21 , pp. 717-726
    • Tu, J.C.1
  • 36
    • 0038579336 scopus 로고    scopus 로고
    • Effects of coexpression with Homer isoforms on the function of metabotropic glutamate receptor 1α
    • Abe, H., Misaka, T., Tateyama, M. & Kubo, Y. Effects of coexpression with Homer isoforms on the function of metabotropic glutamate receptor 1α. Mol. Cell Neurosci. 23, 157-168 (2003).
    • (2003) Mol. Cell Neurosci. , vol.23 , pp. 157-168
    • Abe, H.1    Misaka, T.2    Tateyama, M.3    Kubo, Y.4


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