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Volumn 382, Issue 3, 2008, Pages 578-584

The Quaternary Structure of a Calcium-Permeable AMPA Receptor: Conservation of Shape and Symmetry across Functionally Distinct Subunit Assemblies

Author keywords

GluR2 AMPA receptor; ionotropic glutamate receptor; ligand gated ion channel; single particle electron microscopy; three dimensional structure

Indexed keywords

AMPA RECEPTOR; CALCIUM; PROTEIN SUBUNIT; UREA;

EID: 50149084710     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.07.021     Document Type: Article
Times cited : (31)

References (36)
  • 1
    • 0038022657 scopus 로고    scopus 로고
    • Functional studies and distribution define a family of transmembrane AMPA receptor regulatory proteins
    • Tomita S., Chen L., Kawasaki Y., Petralia R.S., Wenthold R.J., Nicoll R.A., and Bredt D.S. Functional studies and distribution define a family of transmembrane AMPA receptor regulatory proteins. J. Cell Biol. 161 (2003) 805-816
    • (2003) J. Cell Biol. , vol.161 , pp. 805-816
    • Tomita, S.1    Chen, L.2    Kawasaki, Y.3    Petralia, R.S.4    Wenthold, R.J.5    Nicoll, R.A.6    Bredt, D.S.7
  • 4
    • 0025879427 scopus 로고
    • Structural determinants of ion flow through recombinant glutamate receptor channels
    • Verdoorn T., Burnashev N., Monyer H., Seeburg P., and Sakmann B. Structural determinants of ion flow through recombinant glutamate receptor channels. Science 252 (1991) 1715-1718
    • (1991) Science , vol.252 , pp. 1715-1718
    • Verdoorn, T.1    Burnashev, N.2    Monyer, H.3    Seeburg, P.4    Sakmann, B.5
  • 5
    • 13444302564 scopus 로고    scopus 로고
    • Structure and different conformational states of native AMPA receptor complexes
    • Nakagawa T., Cheng Y., Ramm E., Sheng M., and Walz T. Structure and different conformational states of native AMPA receptor complexes. Nature 433 (2005) 545-549
    • (2005) Nature , vol.433 , pp. 545-549
    • Nakagawa, T.1    Cheng, Y.2    Ramm, E.3    Sheng, M.4    Walz, T.5
  • 6
    • 32344443866 scopus 로고    scopus 로고
    • Three-dimensional structure of an AMPA receptor without associated stargazin/TARP proteins
    • Nakagawa T., Cheng Y., Sheng M., and Walz T. Three-dimensional structure of an AMPA receptor without associated stargazin/TARP proteins. Biol. Chem. 387 (2006) 179-187
    • (2006) Biol. Chem. , vol.387 , pp. 179-187
    • Nakagawa, T.1    Cheng, Y.2    Sheng, M.3    Walz, T.4
  • 7
    • 7444240214 scopus 로고    scopus 로고
    • The three-dimensional structure of an ionotropic glutamate receptor reveals a dimer-of-dimers assembly
    • Tichelaar W., Safferling M., Keinänen K., Stark H., and Madden D. The three-dimensional structure of an ionotropic glutamate receptor reveals a dimer-of-dimers assembly. J. Mol. Biol. 344 (2004) 435-442
    • (2004) J. Mol. Biol. , vol.344 , pp. 435-442
    • Tichelaar, W.1    Safferling, M.2    Keinänen, K.3    Stark, H.4    Madden, D.5
  • 8
    • 0026543243 scopus 로고
    • Divalent ion permeability of AMPA receptor channels is dominated by the edited form of a single subunit
    • Burnashev N., Monyer H., Seeburg P.H., and Sakmann B. Divalent ion permeability of AMPA receptor channels is dominated by the edited form of a single subunit. Neuron 8 (1992) 189-198
    • (1992) Neuron , vol.8 , pp. 189-198
    • Burnashev, N.1    Monyer, H.2    Seeburg, P.H.3    Sakmann, B.4
  • 9
    • 0037198702 scopus 로고    scopus 로고
    • RNA editing at Arg607 controls AMPA receptor exit from the endoplasmic reticulum
    • Greger I., Khatri L., and Ziff E. RNA editing at Arg607 controls AMPA receptor exit from the endoplasmic reticulum. Neuron 34 (2002) 759-772
    • (2002) Neuron , vol.34 , pp. 759-772
    • Greger, I.1    Khatri, L.2    Ziff, E.3
  • 10
    • 0031015614 scopus 로고    scopus 로고
    • Single-channel properties of recombinant AMPA receptors depend on RNA editing, splice variation, and subunit composition
    • Swanson G., Kamboj S., and Cull-Candy S. Single-channel properties of recombinant AMPA receptors depend on RNA editing, splice variation, and subunit composition. J. Neurosci. 17 (1997) 58-69
    • (1997) J. Neurosci. , vol.17 , pp. 58-69
    • Swanson, G.1    Kamboj, S.2    Cull-Candy, S.3
  • 11
    • 33847125205 scopus 로고    scopus 로고
    • 2 +-permeable AMPA receptors in synaptic plasticity and neuronal death
    • 2 +-permeable AMPA receptors in synaptic plasticity and neuronal death. Trends Neurosci. 30 (2007) 126-134
    • (2007) Trends Neurosci. , vol.30 , pp. 126-134
    • Liu, S.1    Zukin, R.2
  • 13
    • 0032514408 scopus 로고    scopus 로고
    • Calcium-permeable AMPA receptors mediate long-term potentiation in interneurons in the amygdala
    • Mahanty N.K., and Sah P. Calcium-permeable AMPA receptors mediate long-term potentiation in interneurons in the amygdala. Nature 394 (1998) 683-687
    • (1998) Nature , vol.394 , pp. 683-687
    • Mahanty, N.K.1    Sah, P.2
  • 14
    • 0036732391 scopus 로고    scopus 로고
    • Blockage of Ca(2 +)-permeable AMPA receptors suppresses migration and induces apoptosis in human glioblastoma cells
    • Ishiuchi S., Tsuzuki K., Yoshida Y., Yamada N., Hagimura N., Okado H., et al. Blockage of Ca(2 +)-permeable AMPA receptors suppresses migration and induces apoptosis in human glioblastoma cells. Nat. Med. 8 (2002) 971-978
    • (2002) Nat. Med. , vol.8 , pp. 971-978
    • Ishiuchi, S.1    Tsuzuki, K.2    Yoshida, Y.3    Yamada, N.4    Hagimura, N.5    Okado, H.6
  • 15
    • 0026452868 scopus 로고
    • Switch in glutamate receptor subunit gene expression in CA1 subfield of hippocampus following global ischemia in rats
    • Pellegrini-Giampietro D.E., Zukin R.S., Bennett M.V., Cho S., and Pulsinelli W.A. Switch in glutamate receptor subunit gene expression in CA1 subfield of hippocampus following global ischemia in rats. Proc. Natl Acad. Sci. U. S. A. 89 (1992) 10499-10503
    • (1992) Proc. Natl Acad. Sci. U. S. A. , vol.89 , pp. 10499-10503
    • Pellegrini-Giampietro, D.E.1    Zukin, R.S.2    Bennett, M.V.3    Cho, S.4    Pulsinelli, W.A.5
  • 16
    • 1542378930 scopus 로고    scopus 로고
    • Glutamate receptors: RNA editing and death of motor neurons
    • Kawahara Y., Ito K., Sun H., Aizawa H., Kanazawa I., and Kwak S. Glutamate receptors: RNA editing and death of motor neurons. Nature 427 (2004) 801
    • (2004) Nature , vol.427 , pp. 801
    • Kawahara, Y.1    Ito, K.2    Sun, H.3    Aizawa, H.4    Kanazawa, I.5    Kwak, S.6
  • 17
    • 2342462388 scopus 로고    scopus 로고
    • Structure and function of glutamate receptor ion channels
    • Mayer M., and Armstrong N. Structure and function of glutamate receptor ion channels. Annu. Rev. Physiol. 66 (2004) 161-181
    • (2004) Annu. Rev. Physiol. , vol.66 , pp. 161-181
    • Mayer, M.1    Armstrong, N.2
  • 18
    • 36148942092 scopus 로고    scopus 로고
    • Breaking the bottleneck: eukaryotic membrane protein expression for high-resolution structural studies
    • Midgett C.R., and Madden D.R. Breaking the bottleneck: eukaryotic membrane protein expression for high-resolution structural studies. J. Struct. Biol. 160 (2007) 265-274
    • (2007) J. Struct. Biol. , vol.160 , pp. 265-274
    • Midgett, C.R.1    Madden, D.R.2
  • 19
    • 0035923431 scopus 로고    scopus 로고
    • First images of a glutamate receptor ion channel: oligomeric state and molecular dimensions of GluRB homomers
    • Safferling M., Tichelaar W., Kümmerle G., Jouppila A., Kuusinen A., Keinänen K., and Madden D. First images of a glutamate receptor ion channel: oligomeric state and molecular dimensions of GluRB homomers. Biochemistry 40 (2001) 13948-13953
    • (2001) Biochemistry , vol.40 , pp. 13948-13953
    • Safferling, M.1    Tichelaar, W.2    Kümmerle, G.3    Jouppila, A.4    Kuusinen, A.5    Keinänen, K.6    Madden, D.7
  • 20
    • 33847297686 scopus 로고    scopus 로고
    • Baculoviral expression of an integral membrane protein for structural studies
    • Madden D.R., and Safferling M. Baculoviral expression of an integral membrane protein for structural studies. Methods Mol. Biol. 363 (2007) 39-57
    • (2007) Methods Mol. Biol. , vol.363 , pp. 39-57
    • Madden, D.R.1    Safferling, M.2
  • 21
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: semiautomated software for high-resolution single-particle reconstructions
    • Ludtke S.J., Baldwin P.R., and Chiu W. EMAN: semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol. 128 (1999) 82-97
    • (1999) J. Struct. Biol. , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 22
    • 50149102266 scopus 로고
    • Automatic classification-clustering techniques used with principal axes methods
    • Berry E.M. (Ed), John Wiley and Sons, New York
    • Lebart L., Morineau A., and Warwick K.M. Automatic classification-clustering techniques used with principal axes methods. In: Berry E.M. (Ed). Multivariate Descriptive Statistical Analysis (1984), John Wiley and Sons, New York 109-145
    • (1984) Multivariate Descriptive Statistical Analysis , pp. 109-145
    • Lebart, L.1    Morineau, A.2    Warwick, K.M.3
  • 23
    • 0035940689 scopus 로고    scopus 로고
    • A 11.5 A single particle reconstruction of GroEL using EMAN
    • Ludtke S.J., Jakana J., Song J.L., Chuang D.T., and Chiu W. A 11.5 A single particle reconstruction of GroEL using EMAN. J. Mol. Biol. 314 (2001) 253-262
    • (2001) J. Mol. Biol. , vol.314 , pp. 253-262
    • Ludtke, S.J.1    Jakana, J.2    Song, J.L.3    Chuang, D.T.4    Chiu, W.5
  • 24
    • 3142538754 scopus 로고    scopus 로고
    • Seeing GroEL at 6 A resolution by single particle electron cryomicroscopy
    • Ludtke S.J., Chen D.H., Song J.L., Chuang D.T., and Chiu W. Seeing GroEL at 6 A resolution by single particle electron cryomicroscopy. Structure 12 (2004) 1129-1136
    • (2004) Structure , vol.12 , pp. 1129-1136
    • Ludtke, S.J.1    Chen, D.H.2    Song, J.L.3    Chuang, D.T.4    Chiu, W.5
  • 26
    • 0034093677 scopus 로고    scopus 로고
    • Use of proteoliposomes to generate phage antibodies against native AMPA receptor
    • Jespersen L.K., Kuusinen A., Orellana A., Keinänen K., and Engberg J. Use of proteoliposomes to generate phage antibodies against native AMPA receptor. Eur. J. Biochem. 267 (2000) 1382-1389
    • (2000) Eur. J. Biochem. , vol.267 , pp. 1382-1389
    • Jespersen, L.K.1    Kuusinen, A.2    Orellana, A.3    Keinänen, K.4    Engberg, J.5
  • 27
    • 0028965140 scopus 로고
    • Unraveling the modular design of glutamate-gated ion channels
    • Wo Z.G., and Oswald R.E. Unraveling the modular design of glutamate-gated ion channels. Trends Neurosci. 18 (1995) 161-168
    • (1995) Trends Neurosci. , vol.18 , pp. 161-168
    • Wo, Z.G.1    Oswald, R.E.2
  • 28
    • 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., and Gouaux E. Mechanisms for activation and antagonism of an AMPA-sensitive glutamate receptor: crystal structures of the GluR2 ligand binding core. Neuron 28 (2000) 165-181
    • (2000) Neuron , vol.28 , pp. 165-181
    • Armstrong, N.1    Gouaux, E.2
  • 29
    • 17644417156 scopus 로고    scopus 로고
    • Two regions in the N-terminal domain of ionotropic glutamate receptor 3 form the subunit oligomerization interfaces that control subtype-specific receptor assembly
    • Ayalon G., Segev E., Elgavish S., and Stern-Bach Y. Two regions in the N-terminal domain of ionotropic glutamate receptor 3 form the subunit oligomerization interfaces that control subtype-specific receptor assembly. J. Biol. Chem. 280 (2005) 15053-15060
    • (2005) J. Biol. Chem. , vol.280 , pp. 15053-15060
    • Ayalon, G.1    Segev, E.2    Elgavish, S.3    Stern-Bach, Y.4
  • 31
    • 0034884750 scopus 로고    scopus 로고
    • Functional assembly of AMPA and kainate receptors is mediated by several discrete protein-protein interactions
    • Ayalon G., and Stern-Bach Y. Functional assembly of AMPA and kainate receptors is mediated by several discrete protein-protein interactions. Neuron 31 (2001) 103-113
    • (2001) Neuron , vol.31 , pp. 103-113
    • Ayalon, G.1    Stern-Bach, Y.2
  • 32
    • 0035819074 scopus 로고    scopus 로고
    • Heteromeric AMPA receptors assemble with a preferred subunit stoichiometry and spatial arrangement
    • Mansour M., Nagarajan N., Nehring R., Clements J., and Rosenmund C. Heteromeric AMPA receptors assemble with a preferred subunit stoichiometry and spatial arrangement. Neuron 32 (2001) 841-853
    • (2001) Neuron , vol.32 , pp. 841-853
    • Mansour, M.1    Nagarajan, N.2    Nehring, R.3    Clements, J.4    Rosenmund, C.5
  • 33
    • 0037442813 scopus 로고    scopus 로고
    • Studies of NMDA receptor function and stoichiometry with truncated and tandem subunits
    • Schorge S., and Colquhoun D. Studies of NMDA receptor function and stoichiometry with truncated and tandem subunits. J. Neurosci. 23 (2003) 1151-1158
    • (2003) J. Neurosci. , vol.23 , pp. 1151-1158
    • Schorge, S.1    Colquhoun, D.2
  • 34
    • 1242293628 scopus 로고    scopus 로고
    • The outer pore of the glutamate receptor channel has 2-fold rotational symmetry
    • Sobolevsky A., Yelshansky M., and Wollmuth L. The outer pore of the glutamate receptor channel has 2-fold rotational symmetry. Neuron 41 (2004) 367-378
    • (2004) Neuron , vol.41 , pp. 367-378
    • Sobolevsky, A.1    Yelshansky, M.2    Wollmuth, L.3
  • 35
    • 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 D.R., and Keinänen K. 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 (1999) 28937-28943
    • (1999) J. Biol. Chem. , vol.274 , pp. 28937-28943
    • Kuusinen, A.1    Abele, R.2    Madden, D.R.3    Keinänen, K.4


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