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Volumn 89, Issue 6, 2016, Pages 1264-1276

Distinct Structural Pathways Coordinate the Activation of AMPA Receptor-Auxiliary Subunit Complexes

Author keywords

[No Author keywords available]

Indexed keywords

GLUTAMATE RECEPTOR 1; GLUTAMATE RECEPTOR 2; AMPA RECEPTOR; GLUTAMIC ACID; LITHIUM; PROTEIN SUBUNIT;

EID: 84960802301     PISSN: 08966273     EISSN: 10974199     Source Type: Journal    
DOI: 10.1016/j.neuron.2016.01.038     Document Type: Article
Times cited : (56)

References (58)
  • 2
    • 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. Mechanisms for activation and antagonism of an AMPA-sensitive glutamate receptor: crystal structures of the GluR2 ligand binding core. Neuron 2000, 28:165-181.
    • (2000) Neuron , vol.28 , pp. 165-181
    • Armstrong, N.1    Gouaux, E.2
  • 3
    • 84874626300 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of new 2,4-syn-functionalized (S)-glutamate analogues and structure-activity relationship studies at ionotropic glutamate receptors and excitatory amino acid transporters
    • Assaf Z., Larsen A.P., Venskutonyte˙ R., Han L., Abrahamsen B., Nielsen B., Gajhede M., Kastrup J.S., Jensen A.A., Pickering D.S., et al. Chemoenzymatic synthesis of new 2,4-syn-functionalized (S)-glutamate analogues and structure-activity relationship studies at ionotropic glutamate receptors and excitatory amino acid transporters. J. Med. Chem. 2013, 56:1614-1628.
    • (2013) J. Med. Chem. , vol.56 , pp. 1614-1628
    • Assaf, Z.1    Larsen, A.P.2    Venskutonyte, R.3    Han, L.4    Abrahamsen, B.5    Nielsen, B.6    Gajhede, M.7    Kastrup, J.S.8    Jensen, A.A.9    Pickering, D.S.10
  • 5
    • 0037088834 scopus 로고    scopus 로고
    • External anions and cations distinguish between AMPA and kainate receptor gating mechanisms
    • Bowie D. External anions and cations distinguish between AMPA and kainate receptor gating mechanisms. J. Physiol. 2002, 539:725-733.
    • (2002) J. Physiol. , vol.539 , pp. 725-733
    • Bowie, D.1
  • 6
    • 73549084285 scopus 로고    scopus 로고
    • Ion-dependent gating of kainate receptors
    • Bowie D. Ion-dependent gating of kainate receptors. J. Physiol. 2010, 588:67-81.
    • (2010) J. Physiol. , vol.588 , pp. 67-81
    • Bowie, D.1
  • 7
    • 84912135616 scopus 로고    scopus 로고
    • Mapping the interaction sites between AMPA receptors and TARPs reveals a role for the receptor N-terminal domain in channel gating
    • Cais O., Herguedas B., Krol K., Cull-Candy S.G., Farrant M., Greger I.H. Mapping the interaction sites between AMPA receptors and TARPs reveals a role for the receptor N-terminal domain in channel gating. Cell Rep. 2014, 9:728-740.
    • (2014) Cell Rep. , vol.9 , pp. 728-740
    • Cais, O.1    Herguedas, B.2    Krol, K.3    Cull-Candy, S.G.4    Farrant, M.5    Greger, I.H.6
  • 9
    • 0042856419 scopus 로고    scopus 로고
    • Stargazin differentially controls the trafficking of alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionate and kainate receptors
    • Chen L., El-Husseini A., Tomita S., Bredt D.S., Nicoll R.A. Stargazin differentially controls the trafficking of alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionate and kainate receptors. Mol. Pharmacol. 2003, 64:703-706.
    • (2003) Mol. Pharmacol. , vol.64 , pp. 703-706
    • Chen, L.1    El-Husseini, A.2    Tomita, S.3    Bredt, D.S.4    Nicoll, R.A.5
  • 10
    • 34548552563 scopus 로고    scopus 로고
    • Two families of TARP isoforms that have distinct effects on the kinetic properties of AMPA receptors and synaptic currents
    • Cho C.H., St-Gelais F., Zhang W., Tomita S., Howe J.R. Two families of TARP isoforms that have distinct effects on the kinetic properties of AMPA receptors and synaptic currents. Neuron 2007, 55:890-904.
    • (2007) Neuron , vol.55 , pp. 890-904
    • Cho, C.H.1    St-Gelais, F.2    Zhang, W.3    Tomita, S.4    Howe, J.R.5
  • 13
    • 84920125558 scopus 로고    scopus 로고
    • Retour aux sources: defining the structural basis of glutamate receptor activation
    • Dawe G.B., Aurousseau M.R., Daniels B.A., Bowie D. Retour aux sources: defining the structural basis of glutamate receptor activation. J. Physiol. 2015, 593:97-110.
    • (2015) J. Physiol. , vol.593 , pp. 97-110
    • Dawe, G.B.1    Aurousseau, M.R.2    Daniels, B.A.3    Bowie, D.4
  • 17
    • 84920177233 scopus 로고    scopus 로고
    • Assembly of AMPA receptors: mechanisms and regulation
    • Gan Q., Salussolia C.L., Wollmuth L.P. Assembly of AMPA receptors: mechanisms and regulation. J. Physiol. 2015, 593:39-48.
    • (2015) J. Physiol. , vol.593 , pp. 39-48
    • Gan, Q.1    Salussolia, C.L.2    Wollmuth, L.P.3
  • 18
    • 77958163995 scopus 로고    scopus 로고
    • Lithium acts as a potentiator of AMPAR currents in hippocampal CA1 cells by selectively increasing channel open probability
    • Gebhardt C., Cull-Candy S.G. Lithium acts as a potentiator of AMPAR currents in hippocampal CA1 cells by selectively increasing channel open probability. J. Physiol. 2010, 588:3933-3941.
    • (2010) J. Physiol. , vol.588 , pp. 3933-3941
    • Gebhardt, C.1    Cull-Candy, S.G.2
  • 19
    • 84920194240 scopus 로고    scopus 로고
    • The multifaceted subunit interfaces of ionotropic glutamate receptors
    • Green T., Nayeem N. The multifaceted subunit interfaces of ionotropic glutamate receptors. J. Physiol. 2015, 593:73-81.
    • (2015) J. Physiol. , vol.593 , pp. 73-81
    • Green, T.1    Nayeem, N.2
  • 20
    • 33745493837 scopus 로고    scopus 로고
    • Developmentally regulated, combinatorial RNA processing modulates AMPA receptor biogenesis
    • Greger I.H., Akamine P., Khatri L., Ziff E.B. Developmentally regulated, combinatorial RNA processing modulates AMPA receptor biogenesis. Neuron 2006, 51:85-97.
    • (2006) Neuron , vol.51 , pp. 85-97
    • Greger, I.H.1    Akamine, P.2    Khatri, L.3    Ziff, E.B.4
  • 21
    • 34447648920 scopus 로고    scopus 로고
    • Molecular determinants of AMPA receptor subunit assembly
    • Greger I.H., Ziff E.B., Penn A.C. Molecular determinants of AMPA receptor subunit assembly. Trends Neurosci. 2007, 30:407-416.
    • (2007) Trends Neurosci. , vol.30 , pp. 407-416
    • Greger, I.H.1    Ziff, E.B.2    Penn, A.C.3
  • 22
    • 84912070404 scopus 로고    scopus 로고
    • Auxiliary subunits: shepherding AMPA receptors to the plasma membrane
    • Haering S.C., Tapken D., Pahl S., Hollmann M. Auxiliary subunits: shepherding AMPA receptors to the plasma membrane. Membranes (Basel) 2014, 4:469-490.
    • (2014) Membranes (Basel) , vol.4 , pp. 469-490
    • Haering, S.C.1    Tapken, D.2    Pahl, S.3    Hollmann, M.4
  • 25
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • Hess B., Kutzner C., van der Spoel D., Lindahl E. GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation. J. Chem. Theory Comput. 2008, 4:435-447.
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    van der Spoel, D.3    Lindahl, E.4
  • 26
    • 1242293631 scopus 로고    scopus 로고
    • Regulation of AMPA receptor gating by ligand binding core dimers
    • Horning M.S., Mayer M.L. Regulation of AMPA receptor gating by ligand binding core dimers. Neuron 2004, 41:379-388.
    • (2004) Neuron , vol.41 , pp. 379-388
    • Horning, M.S.1    Mayer, M.L.2
  • 27
    • 84920180634 scopus 로고    scopus 로고
    • Modulation of non-NMDA receptor gating by auxiliary subunits
    • Howe J.R. Modulation of non-NMDA receptor gating by auxiliary subunits. J. Physiol. 2015, 593:61-72.
    • (2015) J. Physiol. , vol.593 , pp. 61-72
    • Howe, J.R.1
  • 28
    • 84920157296 scopus 로고    scopus 로고
    • Glutamate receptor pores
    • Huettner J.E. Glutamate receptor pores. J. Physiol. 2015, 593:49-59.
    • (2015) J. Physiol. , vol.593 , pp. 49-59
    • Huettner, J.E.1
  • 30
    • 79955089674 scopus 로고    scopus 로고
    • The expanding social network of ionotropic glutamate receptors: TARPs and other transmembrane auxiliary subunits
    • Jackson A.C., Nicoll R.A. The expanding social network of ionotropic glutamate receptors: TARPs and other transmembrane auxiliary subunits. Neuron 2011, 70:178-199.
    • (2011) Neuron , vol.70 , pp. 178-199
    • Jackson, A.C.1    Nicoll, R.A.2
  • 31
    • 0029912748 scopus 로고    scopus 로고
    • Development and testing of the OPLS all-atom force field on conformational energetics and properties of organic liquids
    • Jorgensen W.L., Maxwell D.S., Tirado-Rives J. Development and testing of the OPLS all-atom force field on conformational energetics and properties of organic liquids. J. Am. Chem. Soc. 1996, 118:11225-11236.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 11225-11236
    • Jorgensen, W.L.1    Maxwell, D.S.2    Tirado-Rives, J.3
  • 32
    • 73549093121 scopus 로고    scopus 로고
    • SynDIG1: an activity-regulated, AMPA- receptor-interacting transmembrane protein that regulates excitatory synapse development
    • Kalashnikova E., Lorca R.A., Kaur I., Barisone G.A., Li B., Ishimaru T., Trimmer J.S., Mohapatra D.P., Díaz E. SynDIG1: an activity-regulated, AMPA- receptor-interacting transmembrane protein that regulates excitatory synapse development. Neuron 2010, 65:80-93.
    • (2010) Neuron , vol.65 , pp. 80-93
    • Kalashnikova, E.1    Lorca, R.A.2    Kaur, I.3    Barisone, G.A.4    Li, B.5    Ishimaru, T.6    Trimmer, J.S.7    Mohapatra, D.P.8    Díaz, E.9
  • 33
    • 0035913529 scopus 로고    scopus 로고
    • Evaluation and reparametrization of the OPLS-AA force field for proteins via comparison with accurate quantum chemical calculations on peptides
    • Kaminski G.A., Friesner R.A., Tirado-Rives J., Jorgensen W.L. Evaluation and reparametrization of the OPLS-AA force field for proteins via comparison with accurate quantum chemical calculations on peptides. J. Phys. Chem. B 2001, 105:6474-6487.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 6474-6487
    • Kaminski, G.A.1    Friesner, R.A.2    Tirado-Rives, J.3    Jorgensen, W.L.4
  • 34
    • 0032692897 scopus 로고    scopus 로고
    • Lithium modulates desensitization of the glutamate receptor subtype gluR3 in Xenopus oocytes
    • Karkanias N.B., Papke R.L. Lithium modulates desensitization of the glutamate receptor subtype gluR3 in Xenopus oocytes. Neurosci. Lett. 1999, 277:153-156.
    • (1999) Neurosci. Lett. , vol.277 , pp. 153-156
    • Karkanias, N.B.1    Papke, R.L.2
  • 35
    • 84903393500 scopus 로고    scopus 로고
    • Mechanical coupling maintains the fidelity of NMDA receptor-mediated currents
    • Kazi R., Dai J., Sweeney C., Zhou H.X., Wollmuth L.P. Mechanical coupling maintains the fidelity of NMDA receptor-mediated currents. Nat. Neurosci. 2014, 17:914-922.
    • (2014) Nat. Neurosci. , vol.17 , pp. 914-922
    • Kazi, R.1    Dai, J.2    Sweeney, C.3    Zhou, H.X.4    Wollmuth, L.P.5
  • 39
  • 41
    • 13444302564 scopus 로고    scopus 로고
    • Structure and different conformational states of native AMPA receptor complexes
    • Nakagawa T., Cheng Y., Ramm E., Sheng M., Walz T. Structure and different conformational states of native AMPA receptor complexes. Nature 2005, 433:545-549.
    • (2005) Nature , vol.433 , pp. 545-549
    • Nakagawa, T.1    Cheng, Y.2    Ramm, E.3    Sheng, M.4    Walz, T.5
  • 42
    • 79951985476 scopus 로고    scopus 로고
    • Conformational flexibility of the ligand-binding domain dimer in kainate receptor gating and desensitization
    • Nayeem N., Mayans O., Green T. Conformational flexibility of the ligand-binding domain dimer in kainate receptor gating and desensitization. J. Neurosci. 2011, 31:2916-2924.
    • (2011) J. Neurosci. , vol.31 , pp. 2916-2924
    • Nayeem, N.1    Mayans, O.2    Green, T.3
  • 43
    • 33646260450 scopus 로고    scopus 로고
    • Optimal description of a protein structure in terms of multiple groups undergoing TLS motion
    • Painter J., Merritt E.A. Optimal description of a protein structure in terms of multiple groups undergoing TLS motion. Acta Crystallogr. D Biol. Crystallogr. 2006, 62:439-450.
    • (2006) Acta Crystallogr. D Biol. Crystallogr. , vol.62 , pp. 439-450
    • Painter, J.1    Merritt, E.A.2
  • 44
    • 44649169115 scopus 로고    scopus 로고
    • Molecular basis of kainate receptor modulation by sodium
    • Plested A.J., Vijayan R., Biggin P.C., Mayer M.L. Molecular basis of kainate receptor modulation by sodium. Neuron 2008, 58:720-735.
    • (2008) Neuron , vol.58 , pp. 720-735
    • Plested, A.J.1    Vijayan, R.2    Biggin, P.C.3    Mayer, M.L.4
  • 45
    • 14944366485 scopus 로고    scopus 로고
    • Stargazin reduces desensitization and slows deactivation of the AMPA-type glutamate receptors
    • Priel A., Kolleker A., Ayalon G., Gillor M., Osten P., Stern-Bach Y. Stargazin reduces desensitization and slows deactivation of the AMPA-type glutamate receptors. J. Neurosci. 2005, 25:2682-2686.
    • (2005) J. Neurosci. , vol.25 , pp. 2682-2686
    • Priel, A.1    Kolleker, A.2    Ayalon, G.3    Gillor, M.4    Osten, P.5    Stern-Bach, Y.6
  • 49
    • 72049124287 scopus 로고    scopus 로고
    • X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate receptor
    • Sobolevsky A.I., Rosconi M.P., Gouaux E. X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate receptor. Nature 2009, 462:745-756.
    • (2009) Nature , vol.462 , pp. 745-756
    • Sobolevsky, A.I.1    Rosconi, M.P.2    Gouaux, E.3
  • 50
    • 34748849546 scopus 로고    scopus 로고
    • Stargazin attenuates intracellular polyamine block of calcium-permeable AMPA receptors
    • Soto D., Coombs I.D., Kelly L., Farrant M., Cull-Candy S.G. Stargazin attenuates intracellular polyamine block of calcium-permeable AMPA receptors. Nat. Neurosci. 2007, 10:1260-1267.
    • (2007) Nat. Neurosci. , vol.10 , pp. 1260-1267
    • Soto, D.1    Coombs, I.D.2    Kelly, L.3    Farrant, M.4    Cull-Candy, S.G.5
  • 52
    • 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., Bredt D.S. Functional studies and distribution define a family of transmembrane AMPA receptor regulatory proteins. J. Cell Biol. 2003, 161:805-816.
    • (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
  • 54
    • 84921381426 scopus 로고    scopus 로고
    • Subcellular localization of K+ channels in mammalian brain neurons: remarkable precision in the midst of extraordinary complexity
    • Trimmer J.S. Subcellular localization of K+ channels in mammalian brain neurons: remarkable precision in the midst of extraordinary complexity. Neuron 2015, 85:238-256.
    • (2015) Neuron , vol.85 , pp. 238-256
    • Trimmer, J.S.1
  • 55
    • 23744486903 scopus 로고    scopus 로고
    • Stargazin modulates native AMPA receptor functional properties by two distinct mechanisms
    • Turetsky D., Garringer E., Patneau D.K. Stargazin modulates native AMPA receptor functional properties by two distinct mechanisms. J. Neurosci. 2005, 25:7438-7448.
    • (2005) J. Neurosci. , vol.25 , pp. 7438-7448
    • Turetsky, D.1    Garringer, E.2    Patneau, D.K.3
  • 57
    • 33744973079 scopus 로고    scopus 로고
    • External ions are coactivators of kainate receptors
    • Wong A.Y., Fay A.M., Bowie D. External ions are coactivators of kainate receptors. J. Neurosci. 2006, 26:5750-5755.
    • (2006) J. Neurosci. , vol.26 , pp. 5750-5755
    • Wong, A.Y.1    Fay, A.M.2    Bowie, D.3
  • 58
    • 84898726082 scopus 로고    scopus 로고
    • Auxiliary proteins promote modal gating of AMPA- and kainate-type glutamate receptors
    • Zhang W., Devi S.P., Tomita S., Howe J.R. Auxiliary proteins promote modal gating of AMPA- and kainate-type glutamate receptors. Eur. J. Neurosci. 2014, 39:1138-1147.
    • (2014) Eur. J. Neurosci. , vol.39 , pp. 1138-1147
    • Zhang, W.1    Devi, S.P.2    Tomita, S.3    Howe, J.R.4


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