메뉴 건너뛰기




Volumn 25, Issue 9, 2005, Pages 2215-2225

Glutamate receptor trafficking: Endoplasmic reticulum quality control involves ligand binding and receptor function

Author keywords

Binding site; ER retention; Glutamate receptor; Kainate receptor; Mutant; Trafficking

Indexed keywords

AMPA RECEPTOR; ENDOGLYCOSIDASE H; GLUTAMATE RECEPTOR; GLYCOSIDASE; KAINIC ACID RECEPTOR; UNCLASSIFIED DRUG;

EID: 14644444154     PISSN: 02706474     EISSN: None     Source Type: Journal    
DOI: 10.1523/JNEUROSCI.4573-04.2005     Document Type: Article
Times cited : (82)

References (70)
  • 1
    • 0040355740 scopus 로고    scopus 로고
    • Agonist-induced isomerization in a glutamate receptor ligand-binding domain
    • Abele R, Keinanen K, Madden DR (2000) Agonist-induced isomerization in a glutamate receptor ligand-binding domain. J Biol Chem 275:21355-21363.
    • (2000) J Biol Chem , vol.275 , pp. 21355-21363
    • Abele, R.1    Keinanen, K.2    Madden, D.R.3
  • 2
    • 0031961764 scopus 로고    scopus 로고
    • Identification of amino acid residues of the NR2A subunit that control glutamate potency in recombinant NR1/NR2A NMDA receptors
    • Anson LC, Chen PE, Wyllie DJ, Colquhoun D, Schoepfer R (1998) Identification of amino acid residues of the NR2A subunit that control glutamate potency in recombinant NR1/NR2A NMDA receptors. J Neurosci 18:581-589.
    • (1998) J Neurosci , vol.18 , pp. 581-589
    • Anson, L.C.1    Chen, P.E.2    Wyllie, D.J.3    Colquhoun, D.4    Schoepfer, R.5
  • 3
    • 0033636314 scopus 로고    scopus 로고
    • Mechanisms for activation and antagonism of an AMPA-sensitive glutamate receptor: Crystal structures of the GluR2 ligand binding core
    • Armstrong N, Gouaux E (2000) Mechanisms for activation and antagonism of an AMPA-sensitive glutamate receptor: crystal structures of the GluR2 ligand binding core. Neuron 28:165-181.
    • (2000) Neuron , vol.28 , pp. 165-181
    • Armstrong, N.1    Gouaux, E.2
  • 4
    • 0032578635 scopus 로고    scopus 로고
    • Structure of a glutamate-receptor ligand-binding core in complex with kainate
    • Armstrong N, Sun Y, Chen GQ, Gouaux E (1998) Structure of a glutamate-receptor ligand-binding core in complex with kainate. Nature 395:913-917.
    • (1998) Nature , vol.395 , pp. 913-917
    • Armstrong, N.1    Sun, Y.2    Chen, G.Q.3    Gouaux, E.4
  • 5
    • 0034884750 scopus 로고    scopus 로고
    • Functional assembly of AMPA and kainate receptors is mediated by several discrete protein-protein interactions
    • Ayalon G, Stern-Bach Y (2001) Functional assembly of AMPA and kainate receptors is mediated by several discrete protein-protein interactions. Neuron 19:103-113.
    • (2001) Neuron , vol.19 , pp. 103-113
    • Ayalon, G.1    Stern-Bach, Y.2
  • 6
    • 0017348472 scopus 로고
    • The distribution of glycine, GABA, glutamate and aspartate in rabbit spinal cord, cerebellum and hippocampus
    • Berger SJ, Carter JC, Lowry OH (1977) The distribution of glycine, GABA, glutamate and aspartate in rabbit spinal cord, cerebellum and hippocampus. J Neurochem 28:149-158.
    • (1977) J Neurochem , vol.28 , pp. 149-158
    • Berger, S.J.1    Carter, J.C.2    Lowry, O.H.3
  • 9
    • 0036582716 scopus 로고    scopus 로고
    • Functional stoichiometry of glutamate receptor desensitization
    • Bowie D, Lange GD (2002) Functional stoichiometry of glutamate receptor desensitization. J Neurosci 22:3392-3403.
    • (2002) J Neurosci , vol.22 , pp. 3392-3403
    • Bowie, D.1    Lange, G.D.2
  • 10
    • 0029082204 scopus 로고
    • Inward rectification of both AMPA and kainate subtype glutamate receptors generated by polyamine-mediated ion channel block
    • Bowie D, Mayer ML (1995) Inward rectification of both AMPA and kainate subtype glutamate receptors generated by polyamine-mediated ion channel block. Neuron 15:453-462.
    • (1995) Neuron , vol.15 , pp. 453-462
    • Bowie, D.1    Mayer, M.L.2
  • 11
    • 0036395239 scopus 로고    scopus 로고
    • Assembly and cell surface expression of homomeric and heteromeric 5-HT3 receptors: The role of oligomerization and chaperone proteins
    • Boyd GW, Low P, Dunlop JI, Robertson LA, Vardy A, Lambert JJ, Peters JA, Connolly CN (2002) Assembly and cell surface expression of homomeric and heteromeric 5-HT3 receptors: the role of oligomerization and chaperone proteins. Mol Cell Neurosci 21:38-50.
    • (2002) Mol Cell Neurosci , vol.21 , pp. 38-50
    • Boyd, G.W.1    Low, P.2    Dunlop, J.I.3    Robertson, L.A.4    Vardy, A.5    Lambert, J.J.6    Peters, J.A.7    Connolly, C.N.8
  • 13
    • 0034864511 scopus 로고    scopus 로고
    • Functional segregation of the highly conserved basic motifs within the third endoloop of the human secretin receptor
    • Chan KY, Pang RT, Chow BK (2001) Functional segregation of the highly conserved basic motifs within the third endoloop of the human secretin receptor. Endocrinology 142:3926-3934.
    • (2001) Endocrinology , vol.142 , pp. 3926-3934
    • Chan, K.Y.1    Pang, R.T.2    Chow, B.K.3
  • 14
    • 0036193888 scopus 로고    scopus 로고
    • Potassium channel ontogeny
    • Deutsch C (2002) Potassium channel ontogeny. Annu Rev Physiol 64:19-46.
    • (2002) Annu Rev Physiol , vol.64 , pp. 19-46
    • Deutsch, C.1
  • 15
    • 0141884309 scopus 로고    scopus 로고
    • The birth of a channel
    • Deutsch C (2003) The birth of a channel. Neuron 40:265-276.
    • (2003) Neuron , vol.40 , pp. 265-276
    • Deutsch, C.1
  • 17
    • 0037336295 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum
    • Ellgaard L, Helenius A (2003) Quality control in the endoplasmic reticulum. Nat Rev Mol Cell Biol 4:181-191.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 181-191
    • Ellgaard, L.1    Helenius, A.2
  • 18
    • 0033521072 scopus 로고    scopus 로고
    • Setting the standards: Quality control in the secretory pathway
    • Ellgaard L, Molinari M, Helenius A (1999) Setting the standards: quality control in the secretory pathway. Science 286:1882-1888.
    • (1999) Science , vol.286 , pp. 1882-1888
    • Ellgaard, L.1    Molinari, M.2    Helenius, A.3
  • 19
    • 0030729835 scopus 로고    scopus 로고
    • N-glycosylation is not a prerequisite for glutamate receptor function but is essential for lectin modulation
    • Everts I, Villmann C, Hollmann M (1997) N-glycosylation is not a prerequisite for glutamate receptor function but is essential for lectin modulation. Mol Pharmacol 52:861-873.
    • (1997) Mol Pharmacol , vol.52 , pp. 861-873
    • Everts, I.1    Villmann, C.2    Hollmann, M.3
  • 20
    • 0037442510 scopus 로고    scopus 로고
    • Amino-acid residues involved in glutamate receptor 6 kainate receptor gating and desensitization
    • Fleck MW, Cornell E, Mah SJ (2003) Amino-acid residues involved in glutamate receptor 6 kainate receptor gating and desensitization. J Neurosci 23:1219-1227.
    • (2003) J Neurosci , vol.23 , pp. 1219-1227
    • Fleck, M.W.1    Cornell, E.2    Mah, S.J.3
  • 21
    • 0038037859 scopus 로고    scopus 로고
    • Mechanisms of activation, inhibition and specificity: Crystal structures of the NMDA receptor NR1 ligand-binding core
    • Furukawa H, Gouaux E (2003) Mechanisms of activation, inhibition and specificity: crystal structures of the NMDA receptor NR1 ligand-binding core. EMBO J 22:2873-2885.
    • (2003) EMBO J , vol.22 , pp. 2873-2885
    • Furukawa, H.1    Gouaux, E.2
  • 22
    • 0002329664 scopus 로고    scopus 로고
    • Rat hippocampal neurons in low density culture
    • Banker G, Goslin K, eds, Cambridge, MA: MIT
    • Goslin K, Asumssen H, Banker G (1998) Rat hippocampal neurons in low density culture. In: Culturing nerve cells (Banker G, Goslin K, eds), pp 339-390. Cambridge, MA: MIT.
    • (1998) Culturing Nerve Cells , pp. 339-390
    • Goslin, K.1    Asumssen, H.2    Banker, G.3
  • 24
    • 1542509654 scopus 로고    scopus 로고
    • Mutations in the ligand-binding and pore domains control exit of glutamate receptors from the endoplasmic reticulum in C. elegans
    • Grunwald ME, Kaplan JM (2003) Mutations in the ligand-binding and pore domains control exit of glutamate receptors from the endoplasmic reticulum in C. elegans. Neuropharmacology 45:768-776.
    • (2003) Neuropharmacology , vol.45 , pp. 768-776
    • Grunwald, M.E.1    Kaplan, J.M.2
  • 25
    • 0033922136 scopus 로고    scopus 로고
    • Identification of molecular regions responsible for the membrane trafficking of Kir6.2
    • Hough E, Beech DJ, Sivaprasadarao A (2000) Identification of molecular regions responsible for the membrane trafficking of Kir6.2. Pflügers Arch 440:481-487.
    • (2000) Pflügers Arch , vol.440 , pp. 481-487
    • Hough, E.1    Beech, D.J.2    Sivaprasadarao, A.3
  • 26
    • 18744394305 scopus 로고    scopus 로고
    • Determinants of antagonist binding at the alpha-amino-3-hydroxy-5-methyl- 4-isoxazolepropionic acid receptor subunit, GluR-D. Role of the conserved arginine 507 and glutamate 727 residues
    • Jouppila A, Pentikainen OT, Settimo L, Nyronen T, Haapalahti JP, Lampinen M, Mottershead DG, Johnson MS, Keinanen K (2002) Determinants of antagonist binding at the alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor subunit, GluR-D. Role of the conserved arginine 507 and glutamate 727 residues. Eur J Biochem 269:6261-6270.
    • (2002) Eur J Biochem , vol.269 , pp. 6261-6270
    • Jouppila, A.1    Pentikainen, O.T.2    Settimo, L.3    Nyronen, T.4    Haapalahti, J.P.5    Lampinen, M.6    Mottershead, D.G.7    Johnson, M.S.8    Keinanen, K.9
  • 28
    • 0032521643 scopus 로고    scopus 로고
    • Characterization of the kainate-binding domain of the glutamate receptor GluR-6 subunit
    • Keinanen K, Jouppila A, Kuusinen A (1998) Characterization of the kainate-binding domain of the glutamate receptor GluR-6 subunit. Biochem J 330:1461-1467.
    • (1998) Biochem J , vol.330 , pp. 1461-1467
    • Keinanen, K.1    Jouppila, A.2    Kuusinen, A.3
  • 29
    • 0035947642 scopus 로고    scopus 로고
    • Adjacent basic amino acid residues recognized by the COP I complex and ubiquitination govern endoplasmic reticulum to cell surface trafficking of the nicotinic acetylcholine receptor alpha-subunit
    • Keller SH, Lindstrom J, Ellisman M, Taylor P (2001) Adjacent basic amino acid residues recognized by the COP I complex and ubiquitination govern endoplasmic reticulum to cell surface trafficking of the nicotinic acetylcholine receptor alpha-subunit. J Biol Chem 276:18384-18391.
    • (2001) J Biol Chem , vol.276 , pp. 18384-18391
    • Keller, S.H.1    Lindstrom, J.2    Ellisman, M.3    Taylor, P.4
  • 30
    • 0032432673 scopus 로고    scopus 로고
    • Endocrinopathies in the family of endoplasmic reticulum (ER) storage diseases: Disorders of protein trafficking and the role of ER molecular chaperones
    • Kim PS, Arvan P (1998) Endocrinopathies in the family of endoplasmic reticulum (ER) storage diseases: disorders of protein trafficking and the role of ER molecular chaperones. Endocr Rev 19:173-202.
    • (1998) Endocr Rev , vol.19 , pp. 173-202
    • Kim, P.S.1    Arvan, P.2
  • 31
    • 0032541434 scopus 로고    scopus 로고
    • AMPA receptors and bacterial periplasmic amino-acid binding proteins share the ionic mechanism of ligand recognition
    • Lampinen M, Pentikainen O, Johnson MS, Keinanen K (1998) AMPA receptors and bacterial periplasmic amino-acid binding proteins share the ionic mechanism of ligand recognition. EMBO J 17:4704-4711.
    • (1998) EMBO J , vol.17 , pp. 4704-4711
    • Lampinen, M.1    Pentikainen, O.2    Johnson, M.S.3    Keinanen, K.4
  • 32
    • 0036830592 scopus 로고    scopus 로고
    • Discrimination between agonists and antagonists by the a-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid-selective glutamate receptor. A mutation analysis of the ligand-binding domain of GIuR-D subunit
    • Lampinen M, Settimo L, Pentikainen OT, Jouppila A, Mottershead DG, Johnson MS, Keinanen K (2002) Discrimination between agonists and antagonists by the a-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid-selective glutamate receptor. A mutation analysis of the ligand-binding domain of GIuR-D subunit. J Biol Chem 277:41940-41947.
    • (2002) J Biol Chem , vol.277 , pp. 41940-41947
    • Lampinen, M.1    Settimo, L.2    Pentikainen, O.T.3    Jouppila, A.4    Mottershead, D.G.5    Johnson, M.S.6    Keinanen, K.7
  • 33
    • 0030991790 scopus 로고    scopus 로고
    • Molecular determinants of agonist discrimination by NMDA receptor subunits: Analysis of the glutamate binding site on the NR2B subunit
    • Laube B, Hirai H, Sturgess M, Betz H, Kuhse J (1997) Molecular determinants of agonist discrimination by NMDA receptor subunits: analysis of the glutamate binding site on the NR2B subunit. Neuron 18:493-503.
    • (1997) Neuron , vol.18 , pp. 493-503
    • Laube, B.1    Hirai, H.2    Sturgess, M.3    Betz, H.4    Kuhse, J.5
  • 34
    • 0038380386 scopus 로고    scopus 로고
    • Roles and rules of kainate receptors in synaptic transmission
    • Lerma J (2003) Roles and rules of kainate receptors in synaptic transmission. Nat Rev Neurosci 4:481-495.
    • (2003) Nat Rev Neurosci , vol.4 , pp. 481-495
    • Lerma, J.1
  • 35
    • 0029077048 scopus 로고
    • Steric masking of a dilysine endoplasmic reticulum retention motif during assembly of the human high affinity receptor for immunoglobulin E
    • Letourneur F, Hennecke S, Demolliere C, Cosson P (1995) Steric masking of a dilysine endoplasmic reticulum retention motif during assembly of the human high affinity receptor for immunoglobulin E. J Cell Biol 129:971-978.
    • (1995) J Cell Biol , vol.129 , pp. 971-978
    • Letourneur, F.1    Hennecke, S.2    Demolliere, C.3    Cosson, P.4
  • 36
    • 0033546277 scopus 로고    scopus 로고
    • Subtype-specific assembly of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptor subunits is mediated by their N-terminal domains
    • Leuschner WD, Hoch W (1999) Subtype-specific assembly of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptor subunits is mediated by their N-terminal domains. J Biol Chem 274:16907-16916.
    • (1999) J Biol Chem , vol.274 , pp. 16907-16916
    • Leuschner, W.D.1    Hoch, W.2
  • 37
    • 0036606360 scopus 로고    scopus 로고
    • ER transport signals and trafficking of potassium channels and receptors
    • Ma D, Jan LY (2002) ER transport signals and trafficking of potassium channels and receptors. Curr Opin Neurobiol 12:287-292.
    • (2002) Curr Opin Neurobiol , vol.12 , pp. 287-292
    • Ma, D.1    Jan, L.Y.2
  • 38
    • 0029899637 scopus 로고    scopus 로고
    • A Venus flytrap mechanism for activation and desensitization of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptors
    • Mano I, Lamed Y, Teichberg VI (1996) A Venus flytrap mechanism for activation and desensitization of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptors. J Biol Chem 271:15299-15302.
    • (1996) J Biol Chem , vol.271 , pp. 15299-15302
    • Mano, I.1    Lamed, Y.2    Teichberg, V.I.3
  • 41
    • 0024822411 scopus 로고
    • Light and electron microscopic localization of glutamate immunoreactivity in the supraoptic nucleus of the rat hypothalamus
    • Meeker RB, Swanson DJ, Hayward JN (1989) Light and electron microscopic localization of glutamate immunoreactivity in the supraoptic nucleus of the rat hypothalamus. Neuroscience 33:157-167.
    • (1989) Neuroscience , vol.33 , pp. 157-167
    • Meeker, R.B.1    Swanson, D.J.2    Hayward, J.N.3
  • 43
    • 0033568842 scopus 로고    scopus 로고
    • Alternative splicing of the C-terminal domain regulates cell surface expression of the NMDA receptor NR1 subunit
    • Okabe S, Miwa A, Okado H (1999) Alternative splicing of the C-terminal domain regulates cell surface expression of the NMDA receptor NR1 subunit. J Neurosci 19:7781-7792.
    • (1999) J Neurosci , vol.19 , pp. 7781-7792
    • Okabe, S.1    Miwa, A.2    Okado, H.3
  • 44
    • 17144450204 scopus 로고    scopus 로고
    • Identification of the amino acid subsets accounting for the ligand binding specificity of a glutamate receptor
    • Paas Y, Eisenstein M, Medevielle F, Teichberg VI, Devillers-Thiery A (1996) Identification of the amino acid subsets accounting for the ligand binding specificity of a glutamate receptor. Neuron 17:979-990.
    • (1996) Neuron , vol.17 , pp. 979-990
    • Paas, Y.1    Eisenstein, M.2    Medevielle, F.3    Teichberg, V.I.4    Devillers-Thiery, A.5
  • 46
    • 0037007201 scopus 로고    scopus 로고
    • Ligands act as pharmacological chaperones and increase the efficiency of delta opioid receptor maturation
    • Petaja-Repo UE, Hogue M, Bhalla S, Laperriere A, Morello JP, Bouvier M (2002) Ligands act as pharmacological chaperones and increase the efficiency of delta opioid receptor maturation. EMBO J 21:1628-1637.
    • (2002) EMBO J , vol.21 , pp. 1628-1637
    • Petaja-Repo, U.E.1    Hogue, M.2    Bhalla, S.3    Laperriere, A.4    Morello, J.P.5    Bouvier, M.6
  • 47
    • 1642398017 scopus 로고    scopus 로고
    • NMDA receptors: Subunit assembly and trafficking to the synapse
    • Prybylowski K, Wenthold RJ (2004) NMDA receptors: subunit assembly and trafficking to the synapse. J Biol Chem 279:9673-9676.
    • (2004) J Biol Chem , vol.279 , pp. 9673-9676
    • Prybylowski, K.1    Wenthold, R.J.2
  • 48
    • 0032128150 scopus 로고    scopus 로고
    • Assembly, sorting, and exit of oligomeric proteins from the endoplasmic reticulum
    • Reddy PS, Corley RB (1998) Assembly, sorting, and exit of oligomeric proteins from the endoplasmic reticulum. BioEssays 20:546-554.
    • (1998) BioEssays , vol.20 , pp. 546-554
    • Reddy, P.S.1    Corley, R.B.2
  • 49
    • 0032486422 scopus 로고    scopus 로고
    • The tetrameric structure of a glutamate receptor channel
    • Rosenmund C, Stern-Bach Y, Stevens CF (1998) The tetrameric structure of a glutamate receptor channel. Science 280:1596-1599.
    • (1998) Science , vol.280 , pp. 1596-1599
    • Rosenmund, C.1    Stern-Bach, Y.2    Stevens, C.F.3
  • 50
    • 0035341508 scopus 로고    scopus 로고
    • An NMDA receptor ER retention signal regulated by phosphorylation and alternative splicing
    • Scott DB, Blanpied TA, Swanson GT, Zhang C, Ehlers MD (2001) An NMDA receptor ER retention signal regulated by phosphorylation and alternative splicing. J Neurosci 21:3063-3072.
    • (2001) J Neurosci , vol.21 , pp. 3063-3072
    • Scott, D.B.1    Blanpied, T.A.2    Swanson, G.T.3    Zhang, C.4    Ehlers, M.D.5
  • 51
    • 0027234701 scopus 로고
    • The TINS/TiPS Lecture. The molecular biology of mammalian glutamate receptor channels
    • Seeburg PH (1993) The TINS/TiPS Lecture. The molecular biology of mammalian glutamate receptor channels. Trends Neurosci 16:359-365.
    • (1993) Trends Neurosci , vol.16 , pp. 359-365
    • Seeburg, P.H.1
  • 52
    • 0032077722 scopus 로고    scopus 로고
    • RNA editing of brain glutamate receptor channels: Mechanism and physiology
    • Seeburg PH, Higuchi M, Sprengel R (1998) RNA editing of brain glutamate receptor channels: mechanism and physiology. Brain Res Brain Res Rev 26:217-229.
    • (1998) Brain Res Brain Res Rev , vol.26 , pp. 217-229
    • Seeburg, P.H.1    Higuchi, M.2    Sprengel, R.3
  • 53
    • 85052772258 scopus 로고
    • Glutamate as a neurotransmitter
    • Kvamme E, ed, Boca Raton, FL: CRC
    • Shank RP, Aprison MH (1988) Glutamate as a neurotransmitter. In: Glutamine and glutamate in mammals, VoI II (Kvamme E, ed), pp 3-19. Boca Raton, FL: CRC.
    • (1988) Glutamine and Glutamate in Mammals , vol.2 , pp. 3-19
    • Shank, R.P.1    Aprison, M.H.2
  • 54
    • 0033623299 scopus 로고    scopus 로고
    • Concentration-dependent substrate behavior of native AMPA receptors
    • Smith TC, Howe JR (2000) Concentration-dependent substrate behavior of native AMPA receptors. Nat Neurosci 3:992-997.
    • (2000) Nat Neurosci , vol.3 , pp. 992-997
    • Smith, T.C.1    Howe, J.R.2
  • 56
    • 0034520590 scopus 로고    scopus 로고
    • PDZ domain suppression of an ER retention signal in NMDA receptor NR1 splice variants
    • Standley S, Roche KW, McCallum J, Sans N, Wenthold RJ (2000) PDZ domain suppression of an ER retention signal in NMDA receptor NR1 splice variants. Neuron 28:887-898.
    • (2000) Neuron , vol.28 , pp. 887-898
    • Standley, S.1    Roche, K.W.2    McCallum, J.3    Sans, N.4    Wenthold, R.J.5
  • 57
    • 0028559605 scopus 로고
    • Agonist selectivity of glutamate receptors is specified by two domains structurally related to bacterial amino acid-binding proteins
    • Stern-Bach Y, Bettler B, Hartley M, Sheppard PO, O'Hara PJ, Heinemann SF (1994) Agonist selectivity of glutamate receptors is specified by two domains structurally related to bacterial amino acid-binding proteins. Neuron 13:1345-1357.
    • (1994) Neuron , vol.13 , pp. 1345-1357
    • Stern-Bach, Y.1    Bettler, B.2    Hartley, M.3    Sheppard, P.O.4    O'Hara, P.J.5    Heinemann, S.F.6
  • 59
    • 0029778556 scopus 로고    scopus 로고
    • Signal-mediated sorting of membrane proteins between the endoplasmic reticulum and the Golgi apparatus
    • Teasdale RD, Jackson MR (1996) Signal-mediated sorting of membrane proteins between the endoplasmic reticulum and the Golgi apparatus. Annu Rev Cell Dev Biol 12:27-54.
    • (1996) Annu Rev Cell Dev Biol , vol.12 , pp. 27-54
    • Teasdale, R.D.1    Jackson, M.R.2
  • 60
    • 0344393021 scopus 로고    scopus 로고
    • Quality control and protein folding in the secretory pathway
    • Trombetta ES, Parodi AJ (2003) Quality control and protein folding in the secretory pathway. Annu Rev Cell Dev Biol 19:649-676.
    • (2003) Annu Rev Cell Dev Biol , vol.19 , pp. 649-676
    • Trombetta, E.S.1    Parodi, A.J.2
  • 62
    • 0026686125 scopus 로고
    • Mutations in a putative agonist binding region of the AMPA-selective glutamate receptor channel
    • Uchino S, Sakimura K, Nagahari K, Mishina M (1992) Mutations in a putative agonist binding region of the AMPA-selective glutamate receptor channel. FEES Lett 308:253-257.
    • (1992) FEES Lett , vol.308 , pp. 253-257
    • Uchino, S.1    Sakimura, K.2    Nagahari, K.3    Mishina, M.4
  • 63
    • 14044254241 scopus 로고    scopus 로고
    • Ligand binding is a critical requirement for plasma membrane expression of heteromeric kainate receptors
    • Valluru L, Xu J, Zhu Y, Yan S, Contractor A, Swanson GT (2005) Ligand binding is a critical requirement for plasma membrane expression of heteromeric kainate receptors. J Biol Chem, 280:6085-6093.
    • (2005) J Biol Chem , vol.280 , pp. 6085-6093
    • Valluru, L.1    Xu, J.2    Zhu, Y.3    Yan, S.4    Contractor, A.5    Swanson, G.T.6
  • 65
    • 0033601326 scopus 로고    scopus 로고
    • Cysteine mutagenesis and homology modeling of the ligand-binding site of a kainate-binding protein
    • Wo ZG, Chohan KK, Chen H, Sutcliffe MJ, Oswald RE (1999) Cysteine mutagenesis and homology modeling of the ligand-binding site of a kainate-binding protein. J Biol Chem 274:37210-37208.
    • (1999) J Biol Chem , vol.274 , pp. 37210-137208
    • Wo, Z.G.1    Chohan, K.K.2    Chen, H.3    Sutcliffe, M.J.4    Oswald, R.E.5
  • 66
    • 1642565240 scopus 로고    scopus 로고
    • Sulfonylureas correct trafficking defects of ATP-sensitive potassium channels caused by mutations in the sulfonylurea receptor
    • Yan F, Lin CW, Weisiger E, Cartier EA, Taschenberger G, Shyng SL (2004) Sulfonylureas correct trafficking defects of ATP-sensitive potassium channels caused by mutations in the sulfonylurea receptor. J Biol Chem 279:11096-11105.
    • (2004) J Biol Chem , vol.279 , pp. 11096-11105
    • Yan, F.1    Lin, C.W.2    Weisiger, E.3    Cartier, E.A.4    Taschenberger, G.5    Shyng, S.L.6
  • 68
    • 0033103174 scopus 로고    scopus 로고
    • A new ER trafficking signal regulates the subunit stoichiometry of plasma membrane K(ATP) channels
    • Zerangue N, Schwappach B, Jan YN, Jan LY (1999) A new ER trafficking signal regulates the subunit stoichiometry of plasma membrane K(ATP) channels. Neuron 22:537-548.
    • (1999) Neuron , vol.22 , pp. 537-548
    • Zerangue, N.1    Schwappach, B.2    Jan, Y.N.3    Jan, L.Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.