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Volumn 728, Issue 1, 2014, Pages 183-187

Roles of subunit phosphorylation in regulating glutamate receptor function

Author keywords

AMPA; CaMKII; Cdk5; Excitatory amino acid; NMDA; PKA; PKC; Tyrosine kinase

Indexed keywords

AMPA RECEPTOR; CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE II; CYCLIC AMP DEPENDENT PROTEIN KINASE; CYCLIN DEPENDENT KINASE 5; FYN NON RECEPTOR TYROSINE KINASE; IONOTROPIC RECEPTOR; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; PROTEIN KINASE C; PROTEIN TYROSINE KINASE; SERINE; SRC NON RECEPTOR TYROSINE KINASE; THREONINE; TYROSINE; UNCLASSIFIED DRUG; PROTEIN SUBUNIT;

EID: 84897116585     PISSN: 00142999     EISSN: 18790712     Source Type: Journal    
DOI: 10.1016/j.ejphar.2013.11.019     Document Type: Article
Times cited : (78)

References (62)
  • 2
    • 0031283172 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent protein kinase II regulatory phosphorylation site in the α-amino-3-hydroxyl-5-methyl-4- isoxazole-propionate-type glutamate receptor
    • DOI 10.1074/jbc.272.52.32727
    • 2+/calmodulin-dependent protein kinase II regulatory phosphorylation site in the α-amino-3-hydroxyl-5-methyl-4-isoxazole-propionate-type glutamate receptor J. Biol. Chem. 272 1997 32727 32730 (Pubitemid 28023601)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.52 , pp. 32727-32730
    • Barria, A.1    Derkach, V.2    Soderling, T.3
  • 3
    • 33745927153 scopus 로고    scopus 로고
    • Synaptic Incorporation of AMPA Receptors during LTP Is Controlled by a PKC Phosphorylation Site on GluR1
    • DOI 10.1016/j.neuron.2006.06.013, PII S0896627306004673
    • J. Boehm, M.G. Kang, R.C. Johnson, J. Esteban, R.L. Huganir, and R. Malinow Synaptic incorporation of AMPA receptors during LTP is controlled by a PKC phosphorylation site on GluR1 Neuron 51 2006 213 225 (Pubitemid 44041865)
    • (2006) Neuron , vol.51 , Issue.2 , pp. 213-225
    • Boehm, J.1    Kang, M.-G.2    Johnson, R.C.3    Esteban, J.4    Huganir, R.L.5    Malinow, R.6
  • 5
    • 0033564041 scopus 로고    scopus 로고
    • Characterization of phosphorylation sites on the glutamate receptor 4 subunit of the AMPA receptors
    • A.L. Carvalho, K. Kameyama, and R.L. Huganir Characterization of phosphorylation sites on the glutamate receptor 4 subunit of the AMPA receptors J. Neurosci. 19 1999 4748 4754 (Pubitemid 29270110)
    • (1999) Journal of Neuroscience , vol.19 , Issue.12 , pp. 4748-4754
    • Carvalho, A.L.1    Kameyama, K.2    Huganir, R.L.3
  • 6
    • 8544232133 scopus 로고    scopus 로고
    • Regulation of the NMDA receptor complex and trafficking by activity-dependent phosphorylation of the NR2B subunit PDZ ligand
    • DOI 10.1523/JNEUROSCI.0546-04.2004
    • H.J. Chung, Y.H. Huang, L.F. Lau, and R.L. Huganir Regulation of the NMDA receptor complex and trafficking by activity-dependent phosphorylation of the NR2B subunit PDZ ligand J. Neurosci. 24 2004 10248 10259 (Pubitemid 39492052)
    • (2004) Journal of Neuroscience , vol.24 , Issue.45 , pp. 10248-10259
    • Hee, J.C.1    Yan, H.H.2    Lau, L.-F.3    Huganir, R.L.4
  • 7
    • 0034307444 scopus 로고    scopus 로고
    • Phosphorylation of the AMPA receptor subunit GluR2 differentially regulates its interaction with PDZ domain-containing proteins
    • H.J. Chung, J. Xia, R.H. Scannevin, X. Zhang, and R.L. Huganir Phosphorylation of the AMPA receptor subunit GluR2 differentially regulates its interaction with PDZ domain-containing proteins J. Neurosci. 20 2000 7258 7267
    • (2000) J. Neurosci. , vol.20 , pp. 7258-7267
    • Chung, H.J.1    Xia, J.2    Scannevin, R.H.3    Zhang, X.4    Huganir, R.L.5
  • 10
    • 84856100434 scopus 로고    scopus 로고
    • Enhancement of AMPA currents and GluR1 membrane expression through PKA-coupled adenosine A(2A) receptors
    • R.B. Dias, J.A. Ribeiro, and A.M. Sebastiao Enhancement of AMPA currents and GluR1 membrane expression through PKA-coupled adenosine A(2A) receptors Hippocampus 22 2012 276 291
    • (2012) Hippocampus , vol.22 , pp. 276-291
    • Dias, R.B.1    Ribeiro, J.A.2    Sebastiao, A.M.3
  • 11
    • 0037312605 scopus 로고    scopus 로고
    • PKA phosphorylation of AMPA receptor subunits controls synaptic trafficking underlying plasticity
    • DOI 10.1038/nn997
    • J.A. Estaban, H. Shi, C. Wilson, M. Nuriya, R.L. Huganir, and R. Malinow PKA phosphorylation of AMPA receptor subunits controls synaptic trafficking underlying plasticity Nat. Neurosci. 6 2003 136 143 (Pubitemid 36182782)
    • (2003) Nature Neuroscience , vol.6 , Issue.2 , pp. 136-143
    • Esteban, J.A.1    Shi, S.-H.2    Wilson, C.3    Nuriya, M.4    Huganir, R.L.5    Malinow, R.6
  • 12
    • 84866411994 scopus 로고    scopus 로고
    • The balance between receptor recycling and trafficking toward lysosomes determines synaptic strength during long-term depression
    • M. Fernandez-Monreal, T.C. Brown, M. Royo, and J.A. Esteban The balance between receptor recycling and trafficking toward lysosomes determines synaptic strength during long-term depression J. Neurosci. 32 2012 13200 13205
    • (2012) J. Neurosci. , vol.32 , pp. 13200-13205
    • Fernandez-Monreal, M.1    Brown, T.C.2    Royo, M.3    Esteban, J.A.4
  • 13
    • 0035831431 scopus 로고    scopus 로고
    • Protein kinase C activation modulates alpha-calmodulin kinase II binding to NR2A subunit of N-mehtyl-d-aspartate receptor complex
    • F. Gardoni, C. Bellone, F. Cattabeni, and M. Di Luca Protein kinase C activation modulates alpha-calmodulin kinase II binding to NR2A subunit of N-mehtyl-d-aspartate receptor complex J. Biol. Chem. 276 2001 7609 7613
    • (2001) J. Biol. Chem. , vol.276 , pp. 7609-7613
    • Gardoni, F.1    Bellone, C.2    Cattabeni, F.3    Di Luca, M.4
  • 14
    • 84857879076 scopus 로고    scopus 로고
    • Mass spectrometrical identification of hippocampal NMDA receptor subunits NR1, NR2A-D and five phosphorylation sites on NR2A and NR2B
    • M. Ghafari, H. Hoger, S. Keihan Falsafi, N. Russo-Schlaff, A. Pollak, and G. Lubec Mass spectrometrical identification of hippocampal NMDA receptor subunits NR1, NR2A-D and five phosphorylation sites on NR2A and NR2B J. Proteome. Res. 11 2012 1891 1896
    • (2012) J. Proteome. Res. , vol.11 , pp. 1891-1896
    • Ghafari, M.1    Hoger, H.2    Keihan Falsafi, S.3    Russo-Schlaff, N.4    Pollak, A.5    Lubec, G.6
  • 15
    • 60349088785 scopus 로고    scopus 로고
    • Phospho-regulation of synaptic and extrasynaptic N-methyl-d-aspartate receptors in adult hippocampal slices
    • S.M. Goebel-Goody, K.D. Davies, R.M. Alvestad Linger, R.K. Freund, and M.D. Browning Phospho-regulation of synaptic and extrasynaptic N-methyl-d-aspartate receptors in adult hippocampal slices Neuroscience 158 2009 1446 1459
    • (2009) Neuroscience , vol.158 , pp. 1446-1459
    • Goebel-Goody, S.M.1    Davies, K.D.2    Alvestad Linger, R.M.3    Freund, R.K.4    Browning, M.D.5
  • 17
    • 34247490214 scopus 로고    scopus 로고
    • PKC anchoring to GluR4 AMPA receptor subunit modulates PKC-driven receptor phosphorylation and surface expression
    • DOI 10.1111/j.1600-0854.2006.00521.x
    • A.R. Gomes, S.S. Correia, J.A. Esteban, C.B. Duarte, and A.L. Carvalho PKC anchoring to GluR4 AMPA receptor subunit modulates PKC-driven receptor phosphorylation and surface expression Traffic 8 2007 259 269 (Pubitemid 46656517)
    • (2007) Traffic , vol.8 , Issue.3 , pp. 259-269
    • Gomes, A.R.1    Correia, S.S.2    Esteban, J.A.3    Duarte, C.B.4    Carvalho, A.L.5
  • 19
    • 3042794099 scopus 로고    scopus 로고
    • Tyrosine phosphorylation and regulation of the AMPA receptor by Src family tyrosine kinases
    • DOI 10.1523/JNEUROSCI.0799-04.2004
    • T. Hayashi, and R.L. Huganir Tyrosine phosphorylation and regulation of the AMPA receptor by SRC family tyrosine kinases J. Neurosci. 24 2004 6152 6160 (Pubitemid 38891106)
    • (2004) Journal of Neuroscience , vol.24 , Issue.27 , pp. 6152-6160
    • Hayashi, T.1    Huganir, R.L.2
  • 21
    • 84877800482 scopus 로고    scopus 로고
    • The type II cGMP dependent protein kinase regulates GluA1 levels at the plasma membrane of developing cerebellar granule cells
    • S. Incontro, F. Ciruela, E. Ziff, F. Hormann, J. Sanchez-Prieto, and M. Torres The type II cGMP dependent protein kinase regulates GluA1 levels at the plasma membrane of developing cerebellar granule cells Biochim. Biophys 1833 2013 1820 1831
    • (2013) Biochim. Biophys , vol.1833 , pp. 1820-1831
    • Incontro, S.1    Ciruela, F.2    Ziff, E.3    Hormann, F.4    Sanchez-Prieto, J.5    Torres, M.6
  • 22
    • 84860346297 scopus 로고    scopus 로고
    • PKC phosphorylates GluA1-Ser831 to enhance AMPA receptor conductance
    • M.A. Jenkins, and S.F. Travnelis PKC phosphorylates GluA1-Ser831 to enhance AMPA receptor conductance Channels (Austin) 6 2012 60 64
    • (2012) Channels (Austin) , vol.6 , pp. 60-64
    • Jenkins, M.A.1    Travnelis, S.F.2
  • 23
    • 15244345046 scopus 로고    scopus 로고
    • PKC site mutations reveal differential modulation by insulin of NMDA receptors containing NR2A or NR2B subunits
    • DOI 10.1111/j.1471-4159.2004.02985.x
    • M.L. Jones, and J.P. Leonard PKC site mutations reveal differential modulation by insulin of NMDA receptors containing NR2A or NR2B subunits J. Neurochem. 92 2005 1431 1438 (Pubitemid 40389212)
    • (2005) Journal of Neurochemistry , vol.92 , Issue.6 , pp. 1431-1438
    • Jones, M.L.1    Leonard, J.P.2
  • 24
    • 84655165030 scopus 로고    scopus 로고
    • PI 3-kinase and PKCζ mediate insulin-induced potentiation of NMDA receptor currents in Xenopus oocytes
    • M.L. Jones, G.Y. Liao, R. Malecki, M. Li, N.M. Salazar, and J.P. Leonard PI 3-kinase and PKCζ mediate insulin-induced potentiation of NMDA receptor currents in Xenopus oocytes Brain Res. 1432 2012 7 14
    • (2012) Brain Res. , vol.1432 , pp. 7-14
    • Jones, M.L.1    Liao, G.Y.2    Malecki, R.3    Li, M.4    Salazar, N.M.5    Leonard, J.P.6
  • 25
    • 84874595643 scopus 로고    scopus 로고
    • The δ2 glutamate receptor gates long-term depression by coordinating interactions between two AMPA receptor phosphorylation sites
    • K. Kohda, W. Kakegawa, S. Matsuda, T. Yamamoto, H. Hirano, and M. Yuzaki The δ2 glutamate receptor gates long-term depression by coordinating interactions between two AMPA receptor phosphorylation sites Proc. Natl. Acad. Sci. USA 110 2013 E948 957
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 948-957
    • Kohda, K.1    Kakegawa, W.2    Matsuda, S.3    Yamamoto, T.4    Hirano, H.5    Yuzaki, M.6
  • 27
    • 0036236357 scopus 로고    scopus 로고
    • Calcineurin acts via the C-terminus of NR2A to modulate desensitization of NMDA receptors
    • DOI 10.1016/S0028-3908(02)00031-X, PII S002839080200031X
    • J.J. Krupp, B. Vissel, C.G. Thomas, S.F. Heinemann, and G.L. Westbrook Calciueurin acts via the C-terminus of NR2A to modulate desensitization of NMDA receptors Neuropharmacology 42 2002 593 602 (Pubitemid 34457739)
    • (2002) Neuropharmacology , vol.42 , Issue.5 , pp. 593-602
    • Krupp, J.J.1    Vissel, B.2    Thomas, C.G.3    Heinemann, S.F.4    Westbrook, G.L.5
  • 28
    • 0029093990 scopus 로고
    • Differential tyrosine phosphorylation of N-methyl-d-aspartate receptor subunits
    • L.F. Lau, and R.L. Huganir Differential tyrosine phosphorylation of N-methyl-d-aspartate receptor subunits J. Biol. Chem. 270 1995 20036 20041
    • (1995) J. Biol. Chem. , vol.270 , pp. 20036-20041
    • Lau, L.F.1    Huganir, R.L.2
  • 29
    • 33750013411 scopus 로고    scopus 로고
    • Synaptic plasticity and phosphorylation
    • H.K. Lee Synaptic plasticity and phosphorylation Pharmacol. Ther. 112 2006 810 832
    • (2006) Pharmacol. Ther. , vol.112 , pp. 810-832
    • Lee, H.K.1
  • 30
    • 34548480959 scopus 로고    scopus 로고
    • Identification and characterization of a novel phosphorylation site on the GluR1 subunit of AMPA receptors
    • DOI 10.1016/j.mcn.2007.06.003, PII S1044743107001455
    • H.K. Lee, K. Takamiya, K. Kameyama, K. He, S. Yu, L. Rossetti, D. Wilen, and R.L. Huganir Identification and characterization of a novel phosphorylation site on the GluR1 subunit of AMPA receptors Mol. Cell. Neurosci. 36 2007 86 94 (Pubitemid 47379556)
    • (2007) Molecular and Cellular Neuroscience , vol.36 , Issue.1 , pp. 86-94
    • Lee, H.-K.1    Takamiya, K.2    Kameyama, K.3    He, K.4    Yu, S.5    Rossetti, L.6    Wilen, D.7    Huganir, R.L.8
  • 31
    • 74049162430 scopus 로고    scopus 로고
    • Specific roles of AMPA receptor subunit GluR1 (GluA1) phosphorylation sites in regulating synaptic plasticity in the CA1 region of hippocampus
    • H.K. Lee, K. Takamiya, K. He, L. Song, and R.L. Huganir Specific roles of AMPA receptor subunit GluR1 (GluA1) phosphorylation sites in regulating synaptic plasticity in the CA1 region of hippocampus J. Neurophysiol. 103 2010 479 489
    • (2010) J. Neurophysiol. , vol.103 , pp. 479-489
    • Lee, H.K.1    Takamiya, K.2    He, K.3    Song, L.4    Huganir, R.L.5
  • 33
    • 0035040079 scopus 로고    scopus 로고
    • Evidence for direct protein kinase-C mediated modulation of N-methyl-D-aspartate receptor current
    • G.Y. Liao, D.A. Wagner, M.H. Hsu, and J.P. Leonard Evidence for direct protein kinase-C mediated modulation of N-methyl-d-aspartate receptor current Mol. Pharmacol. 59 2001 960 964 (Pubitemid 32381573)
    • (2001) Molecular Pharmacology , vol.59 , Issue.5 , pp. 960-964
    • Liao, G.-Y.1    Wagner, D.A.2    Hsu, M.H.3    Leonard, J.P.4
  • 34
    • 67649800746 scopus 로고    scopus 로고
    • Regulation of AMPA receptor extrasynaptic insertion by 4.1N, phosphorylation and palmitoylation
    • D.T. Lin, Y. Makino, K. Sharma, T. Hayashi, R. Neve, K. Takamiya, and R.L. Huganir Regulation of AMPA receptor extrasynaptic insertion by 4.1N, phosphorylation and palmitoylation Nat. Neurosci. 12 2009 879 887
    • (2009) Nat. Neurosci. , vol.12 , pp. 879-887
    • Lin, D.T.1    Makino, Y.2    Sharma, K.3    Hayashi, T.4    Neve, R.5    Takamiya, K.6    Huganir, R.L.7
  • 35
    • 84863496238 scopus 로고    scopus 로고
    • Posttranslational regulation of AMPA receptor trafficking and function
    • W. Lu, and K.W. Roche Posttranslational regulation of AMPA receptor trafficking and function Curr. Opin. Neurobiol. 22 2012 470 479
    • (2012) Curr. Opin. Neurobiol. , vol.22 , pp. 470-479
    • Lu, W.1    Roche, K.W.2
  • 36
    • 84876920736 scopus 로고    scopus 로고
    • Two serine residues on GluN2A C-terminal tails control NMDA receptor current decay times
    • B.A. Maki, R. Cole, and G.K. Popescu Two serine residues on GluN2A C-terminal tails control NMDA receptor current decay times Channels (Austin) 7 2013 126 132
    • (2013) Channels (Austin) , vol.7 , pp. 126-132
    • Maki, B.A.1    Cole, R.2    Popescu, G.K.3
  • 37
    • 79957715137 scopus 로고    scopus 로고
    • Enhanced synaptic plasticity in mice with phosphomimetic mutation of the GluA1 AMPA receptor
    • Y. Makino, R.C. Johnson, Y. Yu, K. Takamiya, and R.L. Huganir Enhanced synaptic plasticity in mice with phosphomimetic mutation of the GluA1 AMPA receptor Proc. Natl. Acad. Sci. USA 108 2011 8450 8455
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 8450-8455
    • Makino, Y.1    Johnson, R.C.2    Yu, Y.3    Takamiya, K.4    Huganir, R.L.5
  • 38
    • 0031435496 scopus 로고    scopus 로고
    • Phosphorylation of the α-amino-3-hydroxy-5-methylisoxazole-4- propionic Acid receptor GluR1 subunit by calcium/calmodulin-dependent kinase II
    • DOI 10.1074/jbc.272.51.32528
    • A.L. Mammen, K. Kameyama, K.W. Roche, and R.L. Huganir Phosphorylation of the alpha-amino-3-hydroxy-5-methylisoxazole4-propionic acid receptor GluR1 subunit by calcium/calmodulin-dependent kinase II J. Biol. Chem. 272 1997 32528 32533 (Pubitemid 28011939)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.51 , pp. 32528-32533
    • Mammen, A.L.1    Kameyama, K.2    Roche, K.W.3    Huganir, R.L.4
  • 39
  • 40
    • 0032823580 scopus 로고    scopus 로고
    • Phosphorylation of serine-880 in GluR2 by protein kinase C prevents its C terminus from binding with glutamate receptor-interacting protein
    • DOI 10.1046/j.1471-4159.1999.731765.x
    • S. Matsuda, S. Mikawa, and H. Hirai Phosphorylation of serine-880 in GluR2 by protein kinase C prevents its C terminus from binding with glutamate receptor-interacting protein J. Neurochem. 73 1999 1765 1768 (Pubitemid 29440182)
    • (1999) Journal of Neurochemistry , vol.73 , Issue.4 , pp. 1765-1768
    • Matsuda, S.1    Mikawa, S.2    Hirai, H.3
  • 41
    • 0034660060 scopus 로고    scopus 로고
    • Disruption of AMPA receptor GluR2 clusters following long-term depression induction in cerebellar Purkinje neurons
    • S. Matsuda, T. Launey, S. Mikawa, and H. Hirai Disruption of AMPA receptor GluR2 clusters following long-term depression induction in cerebellar Purkinje neurons EMBO J. 19 2000 2765 2774 (Pubitemid 30386749)
    • (2000) EMBO Journal , vol.19 , Issue.12 , pp. 2765-2774
    • Matsuda, S.1    Launey, T.2    Mikawa, S.3    Hirai, H.4
  • 42
    • 0035808467 scopus 로고    scopus 로고
    • Characterization of Fyn-mediated tyrosine phosphorylation sites on GluRε2 (NR2B) subunit of the N-methyl-D-aspartate receptor
    • DOI 10.1074/jbc.M008085200
    • T. Nakazawa, S. Komai, T. Tezuka, C. Hisatsune, H. Umemori, K. Semba, M. Mishina, T. Manabe, and T. Yamamoto Characterization of Fyn-mediated tyrosine phosphorylation sites on GluR epsilon 2 (NR2B) subunit of the N-methyl-d-aspartate receptor J. Biol. Chem. 276 2001 693 699 (Pubitemid 32050862)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.1 , pp. 693-699
    • Nakazawa, T.1    Komai, S.2    Tezuka, T.3    Hisatsune, C.4    Umemori, H.5    Semba, K.6    Mishina, M.7    Manabe, T.8    Yamamoto, T.9
  • 43
    • 33644851262 scopus 로고    scopus 로고
    • Extrasynaptic membrane trafficking regulated by GluR1 serine 845 phosphorylation primes AMPA receptors for long-term potentiation
    • M.C. Oh, V.A. Derkach, E.S. Guire, and T.R. Soderling Extrasynaptic membrane trafficking regulated by GluR1 serine 845 phosphorylation primes AMPA receptors for long-term potentiation J. Biol. Chem. 281 2006 752 758
    • (2006) J. Biol. Chem. , vol.281 , pp. 752-758
    • Oh, M.C.1    Derkach, V.A.2    Guire, E.S.3    Soderling, T.R.4
  • 44
    • 0029905992 scopus 로고    scopus 로고
    • Identification of a phosphorylation site for calcium/calmodulin- dependent protein kinase II in the NR2B subunit of the N-methyl-D-aspartate receptor
    • DOI 10.1074/jbc.271.49.31670
    • R.V. Omkumar, O. Melinda, M.J. Kiely, A.J. Rosenstein, K.T. Min, and M.B. Kennedy Identification of a phosphorylation site for calcium/calmodulin- dependent protein kinase II in the NR2B subunit of the N-methyl-d-aspartate receptor J. Biol. Chem. 271 1996 31670 31678 (Pubitemid 26408631)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.49 , pp. 31670-31678
    • Omkumar, R.V.1    Kiely, M.J.2    Rosenstein, A.J.3    Min, K.-T.4    Kennedy, M.B.5
  • 45
    • 84878658398 scopus 로고    scopus 로고
    • PKCλ is critical in AMPA receptor phosphorylation and synaptic incorporation during LTP
    • S.Q. Ren, J.Z. Yan, X.Y. Zhang, Y.F. Bu, W.W. Pan, W. Yao, T. Tian, and W. Lu PKCλ is critical in AMPA receptor phosphorylation and synaptic incorporation during LTP EMBO J 32 2013 1365 1380
    • (2013) EMBO J , vol.32 , pp. 1365-1380
    • Ren, S.Q.1    Yan, J.Z.2    Zhang, X.Y.3    Bu, Y.F.4    Pan, W.W.5    Yao, W.6    Tian, T.7    Lu, W.8
  • 46
    • 0030175899 scopus 로고    scopus 로고
    • Characterization of multiple phosphorylation sites on the AMPA receptor GluR1 subunit
    • DOI 10.1016/S0896-6273(00)80144-0
    • K.W. Roche, R.J. O'Brien, A.L. Mammen, J. Bernhardt, and R.L. Huganir Characterization of multiple phosphorylation sites on the AMPA receptor GluR1 subunit Neuron 16 1996 1179 1188 (Pubitemid 26227239)
    • (1996) Neuron , vol.16 , Issue.6 , pp. 1179-1188
    • Roche, K.W.1    O'Brien, R.J.2    Mammen, A.L.3    Bernhardt, J.4    Huganir, R.L.5
  • 47
    • 20544432404 scopus 로고    scopus 로고
    • Serines 890 and 896 of the NMDA receptor subunit NR1 are differentially phosphorylated by protein kinase C isoforms
    • DOI 10.1016/j.neuint.2005.04.011, PII S0197018605000963
    • A.M. Sanchez-Perez, and V. Felipo Serines 890 and 896 of the NMDA receptor subunit NR1 are differentially phosphorylated by protein kinase C isoforms Neurochem. Int. 47 2005 84 91 (Pubitemid 40848697)
    • (2005) Neurochemistry International , vol.47 , Issue.1-2 SPEC. ISS. , pp. 84-91
    • Sanchez-Perez, A.M.1    Felipo, V.2
  • 49
    • 84875808267 scopus 로고    scopus 로고
    • Activated CaMKII couples GluN2B and casein kinase 2 to control synaptic NMDA receptors
    • A. Sanz-Clemente, J.A. Gray, K.A. Ogilvie, R.A. Nicoll, and K.W. Roche Activated CaMKII couples GluN2B and casein kinase 2 to control synaptic NMDA receptors Cell Rep. 3 2013 607 614
    • (2013) Cell Rep. , vol.3 , pp. 607-614
    • Sanz-Clemente, A.1    Gray, J.A.2    Ogilvie, K.A.3    Nicoll, R.A.4    Roche, K.W.5
  • 50
    • 77956998216 scopus 로고    scopus 로고
    • Casein kinase 2 regulates the NR2 subunit composition of synaptic NMDA receptors
    • A. Sanz-Clemente, J.A. Matta, J.T. Isaac, and K.W. Roche Casein kinase 2 regulates the NR2 subunit composition of synaptic NMDA receptors Neuron 67 2010 984 996
    • (2010) Neuron , vol.67 , pp. 984-996
    • Sanz-Clemente, A.1    Matta, J.A.2    Isaac, J.T.3    Roche, K.W.4
  • 51
    • 84871558287 scopus 로고    scopus 로고
    • Diversity in NMDA receptor composition: Many regulators, many consequences
    • A. Sanz-Clemente, R.A. Nicoll, and K.W. Roche Diversity in NMDA receptor composition: many regulators, many consequences Neuroscientist 19 2013 62 75
    • (2013) Neuroscientist , vol.19 , pp. 62-75
    • Sanz-Clemente, A.1    Nicoll, R.A.2    Roche, K.W.3
  • 52
    • 0035341508 scopus 로고    scopus 로고
    • An NMDA receptor ER retention signal regulated by phosphorylation and alternative splicing
    • D.B. Scott, T.A. Blanpied, G.T. Swanson, C. Zhang, and M.D. Ehlers An NMDA receptor ER retention signal regulated by phosphorylation and alternative splicing J. Neurosci. 21 2001 3063 3072 (Pubitemid 32323488)
    • (2001) Journal of Neuroscience , vol.21 , Issue.9 , pp. 3063-3072
    • Scott, D.B.1    Blanpied, T.A.2    Swanson, G.T.3    Zhang, C.4    Ehlers, M.D.5
  • 53
    • 0141919571 scopus 로고    scopus 로고
    • Glutamate receptor subunit 2 serine 880 phosphorylation modulates synaptic transmission and mediates plasticity in CA1 pyramidal cells
    • K.J. Seidenman, J.P. Steinberg, R.L. Huganir, and R. Malinow Glutamate receptor subunit 2 Serine 880 phosphorylation modulates synaptic transmission and mediates plasticity in CA1 pyramidal cells J. Neurosci. 23 2003 9220 9228 (Pubitemid 37243823)
    • (2003) Journal of Neuroscience , vol.23 , Issue.27 , pp. 9220-9228
    • Seidenman, K.J.1    Steinberg, J.P.2    Huganir, R.3    Malinow, R.4
  • 56
    • 0031040615 scopus 로고    scopus 로고
    • Characterization of protein kinase A and protein kinase C phosphorylation of the N-methyl-D-aspartate receptor NR1 subunit using phosphorylation site-specific antibodies
    • DOI 10.1074/jbc.272.8.5157
    • W.G. Tingley, M.D. Ehlers, K. Kameyama, C. Doherty, J.B. Ptak, C.T. Riley, and R.L. Huganir Characterization of protein kinase A and protein kinase C phosphorylation of the N-methyl-D-aspartate receptor NR1 subunit using phosphorylation site-specific antibodies J. Biol. Chem. 272 1997 5157 5166 (Pubitemid 27090073)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.8 , pp. 5157-5166
    • Tingley, W.G.1    Ehlers, M.D.2    Kameyama, K.3    Doherty, C.4    Ptak, J.B.5    Riley, C.T.6    Huganir, R.L.7
  • 58
    • 83655192092 scopus 로고    scopus 로고
    • Regulation of NMDA receptors by the tyrosine kinase Fyn
    • C.H. Trepanier, M.F. Jackson, and J.F. MacDonald Regulation of NMDA receptors by the tyrosine kinase Fyn FEBS. J. 279 2012 12 19
    • (2012) FEBS. J. , vol.279 , pp. 12-19
    • Trepanier, C.H.1    Jackson, M.F.2    Macdonald, J.F.3
  • 59
    • 0034986665 scopus 로고    scopus 로고
    • A use-dependent tyrosine dephosphorylation of NMDA receptors is independent of ion flux
    • DOI 10.1038/88404
    • B. Vissel, J.J. Krupp, S.F. Heinemann, and G.L. Westbrook A use-dependent tyrosine dephosphorylation of NMDA receptors is independent of ion flux Nat. Neurosci. 4 2001 587 596 (Pubitemid 32507372)
    • (2001) Nature Neuroscience , vol.4 , Issue.6 , pp. 587-596
    • Vissel, B.1    Krupp, J.J.2    Heinemann, S.F.3    Westbrook, G.L.4
  • 60
    • 34547105826 scopus 로고    scopus 로고
    • Fyn-mediated phosphorylation of NR2B Tyr-1336 controls calpain-mediated NR2B cleavage in neurons and heterologous systems
    • DOI 10.1074/jbc.M700624200
    • H.Y. Wu, F.C. Hsu, A.J. Gleichman, I. Baconguis, D.A. Coulter, and D.R. Lynch Fyn-mediated phosphorylation of NR2B Tyr-1336 controls calpain-mediated NR2B cleavage in neurons and heterologous systems J. Biol. Chem. 282 2007 20075 20087 (Pubitemid 47100033)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.28 , pp. 20075-20087
    • Wu, H.-Y.1    Hsu, F.-C.2    Gleichman, A.J.3    Baconguis, I.4    Coulter, D.A.5    Lynch, D.R.6
  • 62
    • 0035050819 scopus 로고    scopus 로고
    • Identification of mouse NMDA receptor subunit NR2A C-terminal tyrosine sites phosphorylated by coexpression with v-Src
    • DOI 10.1046/j.1471-4159.2001.00255.x
    • M. Yang, and J.P. Leonard Identification of mouse NMDA receptor subunit NR2A C-terminal tyrosine sites phosphorylated by coexpression with v-Src J. Neurochem. 77 2001 580 588 (Pubitemid 32298752)
    • (2001) Journal of Neurochemistry , vol.77 , Issue.2 , pp. 580-588
    • Yang, M.1    Leonard, J.P.2


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