메뉴 건너뛰기




Volumn 23, Issue 3, 2003, Pages 798-806

Surface expression of GluR-D AMPA receptor is dependent on an interaction between its C-terminal domain and a 4.1 Protein

Author keywords

4.1 protein; AMPA receptor; GluR D; GluR4; Glutamate; Surface expression

Indexed keywords

AMPA RECEPTOR; GLUTAMATE RECEPTOR; GLUTATHIONE TRANSFERASE; PROTEIN SUBUNIT;

EID: 0037320813     PISSN: 02706474     EISSN: None     Source Type: Journal    
DOI: 10.1523/jneurosci.23-03-00798.2003     Document Type: Article
Times cited : (90)

References (43)
  • 1
    • 0032054473 scopus 로고    scopus 로고
    • Role of actin in anchoring postsynaptic receptors in cultured hippocampal neurons: Differential attachment of NMDA versus AMPA receptors
    • Allison DW, Gelfand VI, Spector I, Craig AM (1998) Role of actin in anchoring postsynaptic receptors in cultured hippocampal neurons: differential attachment of NMDA versus AMPA receptors. J Neurosci 18:2423-2436.
    • (1998) J Neurosci , vol.18 , pp. 2423-2436
    • Allison, D.W.1    Gelfand, V.I.2    Spector, I.3    Craig, A.M.4
  • 2
    • 0035238225 scopus 로고    scopus 로고
    • The postsynaptic spectrin/4.1 membrane protein "accumulation machine"
    • Baines AJ, Keating L, Phillips GW, Scott C (2001) The postsynaptic spectrin/4.1 membrane protein "accumulation machine". Cell Mol Biol Lett 6:691-702.
    • (2001) Cell Mol Biol Lett , vol.6 , pp. 691-702
    • Baines, A.J.1    Keating, L.2    Phillips, G.W.3    Scott, C.4
  • 3
    • 0033793869 scopus 로고    scopus 로고
    • Localization and stabilization of ionotropic glutamate receptors at synapses
    • Bolton MM, Blanpied TA, Ehlers MD (2000) Localization and stabilization of ionotropic glutamate receptors at synapses. Cell Mol Life Sci 57:1517-1525.
    • (2000) Cell Mol Life Sci , vol.57 , pp. 1517-1525
    • Bolton, M.M.1    Blanpied, T.A.2    Ehlers, M.D.3
  • 4
    • 0033564041 scopus 로고    scopus 로고
    • Characterization of phosphorylation sites on the glutamate receptor 4 subunit of the AMPA receptors
    • Carvalho AL, Kameyama K, Huganir RL (1999) Characterization of phosphorylation sites on the glutamate receptor 4 subunit of the AMPA receptors. J Neurosci 19:4748-4754.
    • (1999) J Neurosci , vol.19 , pp. 4748-4754
    • Carvalho, A.L.1    Kameyama, K.2    Huganir, R.L.3
  • 6
    • 0011727270 scopus 로고
    • Molecular cloning of protein 4.1, a major structural element of the human erythrocyte membrane skeleton
    • Conboy J, Kan YW, Shohet SB, Mohandas N (1986) Molecular cloning of protein 4.1, a major structural element of the human erythrocyte membrane skeleton. Proc Natl Acad Sci USA 83:9512-9516.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 9512-9516
    • Conboy, J.1    Kan, Y.W.2    Shohet, S.B.3    Mohandas, N.4
  • 7
    • 0033030234 scopus 로고    scopus 로고
    • The protein kinase C alpha binding protein PICK1 interacts with short but not long form alternative splice variants of AMPA receptor subunits
    • Dev KK, Nishimune A, Henley JM, Nakanishi S (1999) The protein kinase C alpha binding protein PICK1 interacts with short but not long form alternative splice variants of AMPA receptor subunits. Neuropharmacology 38:635-644.
    • (1999) Neuropharmacology , vol.38 , pp. 635-644
    • Dev, K.K.1    Nishimune, A.2    Henley, J.M.3    Nakanishi, S.4
  • 9
    • 0030900558 scopus 로고    scopus 로고
    • GRIP: A synaptic PDZ domain-containing protein that interacts with AMPA receptors
    • Dong H, O'Brien RJ, Fung ET, Lanahan AA, Worley PF, Huganir RL (1997) GRIP: a synaptic PDZ domain-containing protein that interacts with AMPA receptors. Nature 386:279-284.
    • (1997) Nature , vol.386 , pp. 279-284
    • Dong, H.1    O'Brien, R.J.2    Fung, E.T.3    Lanahan, A.A.4    Worley, P.F.5    Huganir, R.L.6
  • 10
    • 0033567072 scopus 로고    scopus 로고
    • Characterization of the glutamate receptor-interacting proteins GRIP1 and GRIP2
    • Dong H, Zhang P, Song I, Petralia RS, Liao D, Huganir RL (1999) Characterization of the glutamate receptor-interacting proteins GRIP1 and GRIP2. J Neurosci 19:6930-6941.
    • (1999) J Neurosci , vol.19 , pp. 6930-6941
    • Dong, H.1    Zhang, P.2    Song, I.3    Petralia, R.S.4    Liao, D.5    Huganir, R.L.6
  • 11
    • 0022340978 scopus 로고
    • Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product
    • Evan GI, Lewis GK, Ramsay G, Bishop JM (1985) Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product. Mol Cell Biol 5:3610-3616.
    • (1985) Mol Cell Biol , vol.5 , pp. 3610-3616
    • Evan, G.I.1    Lewis, G.K.2    Ramsay, G.3    Bishop, J.M.4
  • 12
    • 0026612360 scopus 로고
    • Molecular cloning and development analysis of a new glutamate receptor subunit isoform in cerebellum
    • Gallo V, Upson LM, Hayes WP, Vyklicky L, Winters CA, Buonanno A (1992) Molecular cloning and development analysis of a new glutamate receptor subunit isoform in cerebellum. J Neurosci 12:1010-1023.
    • (1992) J Neurosci , vol.12 , pp. 1010-1023
    • Gallo, V.1    Upson, L.M.2    Hayes, W.P.3    Vyklicky, L.4    Winters, C.A.5    Buonanno, A.6
  • 13
    • 0001789834 scopus 로고
    • Transient production of proteins using an adenovirus transformed cell line
    • Gorman CM, Gies DR, McCray G (1990) Transient production of proteins using an adenovirus transformed cell line. DNA Prot Eng Tech 2:3-10.
    • (1990) DNA Prot Eng Tech , vol.2 , pp. 3-10
    • Gorman, C.M.1    Gies, D.R.2    McCray, G.3
  • 15
    • 0034708587 scopus 로고    scopus 로고
    • Driving AMPA receptors into synapses by LTP and CaMKII: Requirement for GluR1 and PDZ domain interaction
    • Hayashi Y, Shi SH, Esteban JA, Piccini A, Poncer JC, Malinow R (2000) Driving AMPA receptors into synapses by LTP and CaMKII: requirement for GluR1 and PDZ domain interaction, Science 287:2262-2267.
    • (2000) Science , vol.287 , pp. 2262-2267
    • Hayashi, Y.1    Shi, S.H.2    Esteban, J.A.3    Piccini, A.4    Poncer, J.C.5    Malinow, R.6
  • 17
    • 0034089870 scopus 로고    scopus 로고
    • The genetics of the protein 4.1 family: Organizers of the membrane and cytoskeleton
    • Hoover KB, Bryant PJ (2000) The genetics of the protein 4.1 family: organizers of the membrane and cytoskeleton. Curr Opin Cell Biol 12:229-234.
    • (2000) Curr Opin Cell Biol , vol.12 , pp. 229-234
    • Hoover, K.B.1    Bryant, P.J.2
  • 18
    • 0027401499 scopus 로고
    • Genomic structure of the locus encoding protein 4.1. Structural basis for complex combinational patterns of tissue-specific alternative RNA splicing
    • Huang JP, Tang CJ, Kou GH, Marchesi VT, Benz EJ, Tang TK (1993) Genomic structure of the locus encoding protein 4.1. Structural basis for complex combinational patterns of tissue-specific alternative RNA splicing, J Biol Chem 268:3758-3766.
    • (1993) J Biol Chem , vol.268 , pp. 3758-3766
    • Huang, J.P.1    Tang, C.J.2    Kou, G.H.3    Marchesi, V.T.4    Benz, E.J.5    Tang, T.K.6
  • 19
    • 0034093677 scopus 로고    scopus 로고
    • Use of proteoliposomes to generate phage antibodies against native AMPA receptor
    • Jespersen LK, Kuusinen A, Orellana A, Keiniinen K, Engberg J (2000) Use of proteoliposomes to generate phage antibodies against native AMPA receptor. Eur J Biochem 267:1382-1389,
    • (2000) Eur J Biochem , vol.267 , pp. 1382-1389
    • Jespersen, L.K.1    Kuusinen, A.2    Orellana, A.3    Keiniinen, K.4    Engberg, J.5
  • 20
    • 0035313084 scopus 로고    scopus 로고
    • In vitro eye-blink classical conditioning is NMDA receptor dependent and involves redistribution of AMPA receptor subunit GluR4
    • Keifer J (2001) In vitro eye-blink classical conditioning is NMDA receptor dependent and involves redistribution of AMPA receptor subunit GluR4. J Neurosci 21:2434-2441.
    • (2001) J Neurosci , vol.21 , pp. 2434-2441
    • Keifer, J.1
  • 21
    • 0033152432 scopus 로고    scopus 로고
    • A role of actin filament in synaptic transmission and long-term potentiation
    • Kim CH, Lisman JE (1999) A role of actin filament in synaptic transmission and long-term potentiation, J Neurosci 19:4314-4324.
    • (1999) J Neurosci , vol.19 , pp. 4314-4324
    • Kim, C.H.1    Lisman, J.E.2
  • 22
    • 0028292005 scopus 로고
    • The organization of the gene for the functionally dominant alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptor subunit GluR-B
    • Kohler M, Kornau HC, Seeburg PH (1994) The organization of the gene for the functionally dominant alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptor subunit GluR-B. J Biol Chem 269:17367-17370.
    • (1994) J Biol Chem , vol.269 , pp. 17367-17370
    • Kohler, M.1    Kornau, H.C.2    Seeburg, P.H.3
  • 23
    • 0032878510 scopus 로고    scopus 로고
    • Oligomerization and ligand-binding properties of the ectodomain of the alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptor subunit GluRD
    • Kuusinen A, Abele R, Madden DR, Keinänen K (1999) Oligomerization and ligand-binding properties of the ectodomain of the alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptor subunit GluRD. J Biol Chem 274:28937-28943.
    • (1999) J Biol Chem , vol.274 , pp. 28937-28943
    • Kuusinen, A.1    Abele, R.2    Madden, D.R.3    Keinänen, K.4
  • 24
    • 0032584656 scopus 로고    scopus 로고
    • SAP97 is associated with the alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptor GluR1 subunit
    • Leonard AS, Davare MA, Horne MC, Garner CC, Hell JW (1998) SAP97 is associated with the alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptor GluR1 subunit. J Biol Chem 273:19518-19524.
    • (1998) J Biol Chem , vol.273 , pp. 19518-19524
    • Leonard, A.S.1    Davare, M.A.2    Horne, M.C.3    Garner, C.C.4    Hell, J.W.5
  • 25
    • 0038285449 scopus 로고    scopus 로고
    • Synaptic plasticity and dynamic modulation of the postsynaptic membrane
    • Luscher C, Nicoll RA, Malenka RC, Muller D (2000) Synaptic plasticity and dynamic modulation of the postsynaptic membrane. Nat Neurosci 3:545-550.
    • (2000) Nat Neurosci , vol.3 , pp. 545-550
    • Luscher, C.1    Nicoll, R.A.2    Malenka, R.C.3    Muller, D.4
  • 26
    • 0033793777 scopus 로고    scopus 로고
    • Intracellular trafficking of AMPA receptors in synaptic plasticity
    • Man HY, Ju W, Ahmadian G, Wang YT (2000) Intracellular trafficking of AMPA receptors in synaptic plasticity. Cell Mol Life Sci 57:1526-1534.
    • (2000) Cell Mol Life Sci , vol.57 , pp. 1526-1534
    • Man, H.Y.1    Ju, W.2    Ahmadian, G.3    Wang, Y.T.4
  • 28
    • 0000104067 scopus 로고    scopus 로고
    • Cloning and characterization of 4.1G (EPB41L2), a new member of the skeletal protein 4.1 (EPB41) gene family
    • Parra M, Gascard P, Walensky LD, Snyder SH, Mohandas N, Conboy JG (1998) Cloning and characterization of 4.1G (EPB41L2), a new member of the skeletal protein 4.1 (EPB41) gene family. Genomics 49:298-306.
    • (1998) Genomics , vol.49 , pp. 298-306
    • Parra, M.1    Gascard, P.2    Walensky, L.D.3    Snyder, S.H.4    Mohandas, N.5    Conboy, J.G.6
  • 31
    • 0030969931 scopus 로고    scopus 로고
    • Glutamate receptors are selectively targeted to postsynaptic sites in neurons
    • Rubio ME, Wenthold RJ (1997) Glutamate receptors are selectively targeted to postsynaptic sites in neurons. Neuron 18:939-950.
    • (1997) Neuron , vol.18 , pp. 939-950
    • Rubio, M.E.1    Wenthold, R.J.2
  • 32
    • 0035055799 scopus 로고    scopus 로고
    • Protein 4.1 in forebrain postsynaptic density preparations: Enrichment of 4.1 gene products and detection of 4.1R binding proteins
    • Scott C, Keating L, Bellamy M, Baines AJ (2001) Protein 4.1 in forebrain postsynaptic density preparations: enrichment of 4.1 gene products and detection of 4.1R binding proteins. Eur J Biochem 268:1084-1094.
    • (2001) Eur J Biochem , vol.268 , pp. 1084-1094
    • Scott, C.1    Keating, L.2    Bellamy, M.3    Baines, A.J.4
  • 33
    • 0034332508 scopus 로고    scopus 로고
    • Regulation of AMPA receptor GluR1 subunit surface expression by a 4.1N-linked actin cytoskeletal association
    • Shen L, Liang F, Walensky LD, Huganir RL (2000) Regulation of AMPA receptor GluR1 subunit surface expression by a 4.1N-linked actin cytoskeletal association, J Neurosci 20:7932-7940.
    • (2000) J Neurosci , vol.20 , pp. 7932-7940
    • Shen, L.1    Liang, F.2    Walensky, L.D.3    Huganir, R.L.4
  • 34
    • 0034916230 scopus 로고    scopus 로고
    • PDZ domains and the organization of supramolecular complexes
    • Sheng M, Sala C (2001) PDZ domains and the organization of supramolecular complexes. Annu Rev Neurosci 24:1-29.
    • (2001) Annu Rev Neurosci , vol.24 , pp. 1-29
    • Sheng, M.1    Sala, C.2
  • 36
    • 0032143945 scopus 로고    scopus 로고
    • Interaction of the N-ethylmaleimide-sensitive factor with AMPA receptors
    • Song I, Kamboj S, Xia J, Dong H, Liao D, Huganir RL (1998) Interaction of the N-ethylmaleimide-sensitive factor with AMPA receptors. Neuron 21:393-400.
    • (1998) Neuron , vol.21 , pp. 393-400
    • Song, I.1    Kamboj, S.2    Xia, J.3    Dong, H.4    Liao, D.5    Huganir, R.L.6
  • 38
    • 0032489868 scopus 로고    scopus 로고
    • The 13-kD FK506 binding protein, FKBP13, interacts with a novel homologue of the erythrocyte membrane cytoskeletal protein 4.1
    • Walensky LD, Gascard P, Fields ME, Blackshaw S, Conboy JG, Mohandas N, Snyder SH (1998) The 13-kD FK506 binding protein, FKBP13, interacts with a novel homologue of the erythrocyte membrane cytoskeletal protein 4.1. J Cell Biol 141:143-153.
    • (1998) J Cell Biol , vol.141 , pp. 143-153
    • Walensky, L.D.1    Gascard, P.2    Fields, M.E.3    Blackshaw, S.4    Conboy, J.G.5    Mohandas, N.6    Snyder, S.H.7
  • 40
    • 0032907948 scopus 로고    scopus 로고
    • Clustering of AMPA of AMPA receptors by the synaptic PDZ domain-containing protein PICK1
    • Xia J, Zhang X, Staudinger J, Huganir RL (1999) Clustering of AMPA of AMPA receptors by the synaptic PDZ domain-containing protein PICK1. Neuron 22:179-187.
    • (1999) Neuron , vol.22 , pp. 179-187
    • Xia, J.1    Zhang, X.2    Staudinger, J.3    Huganir, R.L.4
  • 41
    • 0034595322 scopus 로고    scopus 로고
    • Comparison of mRNA and protein levels of four members of the protein 4.1 family: The type II brain 4.1/4.1B/KIAA0987 is the most predominant member of the protein 4.1 family in rat brain
    • Yamakawa H, Ohara O (2000) Comparison of mRNA and protein levels of four members of the protein 4.1 family: the type II brain 4.1/4.1B/KIAA0987 is the most predominant member of the protein 4.1 family in rat brain. Gene 248:137-145.
    • (2000) Gene , vol.248 , pp. 137-145
    • Yamakawa, H.1    Ohara, O.2
  • 42
    • 0033017916 scopus 로고    scopus 로고
    • Molecular characterization of a new member of the protein 4.1 family (brain 4.1) in rat brain
    • Yamakawa H, Ohara R, Nakajima D, Nakayama M, Ohara O (1999) Molecular characterization of a new member of the protein 4.1 family (brain 4.1) in rat brain. Brain Res Mol Brain Res 70: 197-209.
    • (1999) Brain Res Mol Brain Res , vol.70 , pp. 197-209
    • Yamakawa, H.1    Ohara, R.2    Nakajima, D.3    Nakayama, M.4    Ohara, O.5
  • 43
    • 0033773869 scopus 로고    scopus 로고
    • Postnatal synaptic potentiation: Delivery of GluR4-containing AMPA receptors by spontaneous activity
    • Zhu JJ, Esteban JA, Hayashi Y, Malinow R (2000) Postnatal synaptic potentiation: delivery of GluR4-containing AMPA receptors by spontaneous activity. Nat Neurosci 3:1098-1106.
    • (2000) Nat Neurosci , vol.3 , pp. 1098-1106
    • Zhu, J.J.1    Esteban, J.A.2    Hayashi, Y.3    Malinow, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.