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Volumn 13, Issue 1, 2010, Pages 36-44

PIP 3 controls synaptic function by maintaining AMPA receptor clustering at the postsynaptic membrane

Author keywords

[No Author keywords available]

Indexed keywords

AMPA RECEPTOR; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; PHOSPHATIDYLINOSITIDE; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE; POSTSYNAPTIC DENSITY PROTEIN 95; CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE II; CARRIER PROTEIN; DLGH4 PROTEIN, RAT; ENHANCED GREEN FLUORESCENT PROTEIN; ENZYME INHIBITOR; GREEN FLUORESCENT PROTEIN; GRIP1 PROTEIN, RAT; MEMBRANE PROTEIN; NERVE PROTEIN; PHOSPHATIDYLINOSITOL; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHATIDYLINOSITOL 3,4,5-TRIPHOSPHATE; POLYPHOSPHOINOSITIDE; SIGNAL PEPTIDE;

EID: 73949117548     PISSN: 10976256     EISSN: None     Source Type: Journal    
DOI: 10.1038/nn.2462     Document Type: Article
Times cited : (126)

References (48)
  • 1
    • 0037205048 scopus 로고    scopus 로고
    • The phosphoinositide 3-kinase pathway
    • Cantley, L.C. The phosphoinositide 3-kinase pathway. Science 296, 1655-1657 (2002).
    • (2002) Science , vol.296 , pp. 1655-1657
    • Cantley, L.C.1
  • 2
    • 33749836234 scopus 로고    scopus 로고
    • Phosphoinositides in cell regulation and membrane dynamics
    • Di Paolo, G. & De Camilli, P. Phosphoinositides in cell regulation and membrane dynamics. Nature 443, 651-657 (2006).
    • (2006) Nature , vol.443 , pp. 651-657
    • Di Paolo, G.1    De Camilli, P.2
  • 3
    • 2942623783 scopus 로고    scopus 로고
    • Protein-lipid interactions and phosphoinositide metabolism in membrane traffc: Insights from vesicle recycling in nerve terminals
    • Wenk, M.R. & De Camilli, P. Protein-lipid interactions and phosphoinositide metabolism in membrane traffc: insights from vesicle recycling in nerve terminals. Proc. Natl. Acad. Sci. USA 101, 8262-8269 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 8262-8269
    • Wenk, M.R.1    De Camilli, P.2
  • 4
    • 0036580702 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase is required for the expression but not for the induction or the maintenance of long-term potentiation in the hippocampal CA1 region
    • Sanna, P.P. et al. Phosphatidylinositol 3-kinase is required for the expression but not for the induction or the maintenance of long-term potentiation in the hippocampal CA1 region. J. Neurosci. 22, 3359-3365 (2002).
    • (2002) J. Neurosci. , vol.22 , pp. 3359-3365
    • Sanna, P.P.1
  • 5
    • 0037868947 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase regulates the induction of long-term potentiation through extracellular signal-related kinase-independent mechanisms
    • Opazo, P., Watabe, A.M., Grant, S.G. & O'Dell, T.J. Phosphatidylinositol 3-kinase regulates the induction of long-term potentiation through extracellular signal-related kinase-independent mechanisms. J. Neurosci. 23, 3679-3688 (2003).
    • (2003) J. Neurosci. , vol.23 , pp. 3679-3688
    • Opazo, P.1    Watabe, A.M.2    Grant, S.G.3    O'Dell, T.J.4
  • 6
    • 0037762556 scopus 로고    scopus 로고
    • Activation of PI3-kinase is required for AMPA receptor insertion during LTP of mEPSCs in cultured hippocampal neurons
    • Man, H.Y. et al. Activation of PI3-kinase is required for AMPA receptor insertion during LTP of mEPSCs in cultured hippocampal neurons. Neuron 38, 611-624 (2003).
    • (2003) Neuron , vol.38 , pp. 611-624
    • Man, H.Y.1
  • 7
    • 24344446859 scopus 로고    scopus 로고
    • State-dependent Ras signaling and AMPA receptor traffcking
    • Qin, Y. et al. State-dependent Ras signaling and AMPA receptor traffcking. Genes Dev. 19, 2000-2015 (2005).
    • (2005) Genes Dev. , vol.19 , pp. 2000-2015
    • Qin, Y.1
  • 8
    • 34047178403 scopus 로고    scopus 로고
    • Phospholipase C is required for changes in postsynaptic structure and function associated with NMDA receptor-dependent long-term depression
    • Horne, E.A. & Dell'Acqua, M.L. Phospholipase C is required for changes in postsynaptic structure and function associated with NMDA receptor-dependent long-term depression. J. Neurosci. 27, 3523-3534 (2007).
    • (2007) J. Neurosci. , vol.27 , pp. 3523-3534
    • Horne, E.A.1    Dell'Acqua, M.L.2
  • 9
    • 38149016966 scopus 로고    scopus 로고
    • The cell biology of synaptic plasticity: AMPA receptor traffcking
    • Shepherd, J.D. & Huganir, R.L. The cell biology of synaptic plasticity: AMPA receptor traffcking. Annu. Rev. Cell Dev. Biol. 23, 613-643 (2007).
    • (2007) Annu. Rev. Cell Dev. Biol. , vol.23 , pp. 613-643
    • Shepherd, J.D.1    Huganir, R.L.2
  • 10
    • 33748350045 scopus 로고    scopus 로고
    • Organelles and traffcking machinery for postsynaptic plasticity
    • Kennedy, M.J. & Ehlers, M.D. Organelles and traffcking machinery for postsynaptic plasticity. Annu. Rev. Neurosci. 29, 325-362 (2006).
    • (2006) Annu. Rev. Neurosci. , vol.29 , pp. 325-362
    • Kennedy, M.J.1    Ehlers, M.D.2
  • 11
    • 0034911881 scopus 로고    scopus 로고
    • Synthesis and function of 3-phosphorylated inositol lipids
    • Vanhaesebroeck, B. et al. Synthesis and function of 3-phosphorylated inositol lipids. Annu. Rev. Biochem. 70, 535-602 (2001).
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 535-602
    • Vanhaesebroeck, B.1
  • 12
    • 1842614409 scopus 로고    scopus 로고
    • PIP3 is involved in neuronal polarization and axon formation
    • Menager, C., Arimura, N., Fukata, Y. & Kaibuchi, K. PIP3 is involved in neuronal polarization and axon formation. J. Neurochem. 89, 109-118 (2004).
    • (2004) J. Neurochem. , vol.89 , pp. 109-118
    • Menager, C.1    Arimura, N.2    Fukata, Y.3    Kaibuchi, K.4
  • 13
    • 30544449810 scopus 로고    scopus 로고
    • Control of dendritic arborization by the phosphoinositide-3′- kinase-Akt-mammalian target of rapamycin pathway
    • Jaworski, J., Spangler, S., Seeburg, D.P., Hoogenraad, C.C. & Sheng, M. Control of dendritic arborization by the phosphoinositide-3′-kinase- Akt-mammalian target of rapamycin pathway. J. Neurosci. 25, 11300-11312 (2005).
    • (2005) J. Neurosci. , vol.25 , pp. 11300-11312
    • Jaworski, J.1    Spangler, S.2    Seeburg, D.P.3    Hoogenraad, C.C.4    Sheng, M.5
  • 14
    • 30544442753 scopus 로고    scopus 로고
    • Regulation of dendritic morphogenesis by Ras-PI3K-Akt-mTOR and Ras-MAPK signaling pathways
    • Kumar, V., Zhang, M.X., Swank, M.W., Kunz, J. & Wu, G.Y. Regulation of dendritic morphogenesis by Ras-PI3K-Akt-mTOR and Ras-MAPK signaling pathways. J. Neurosci. 25, 11288-11299 (2005).
    • (2005) J. Neurosci. , vol.25 , pp. 11288-11299
    • Kumar, V.1    Zhang, M.X.2    Swank, M.W.3    Kunz, J.4    Wu, G.Y.5
  • 15
    • 0036305484 scopus 로고    scopus 로고
    • AMPA receptor traffcking and synaptic plasticity
    • Malinow, R. & Malenka, R.C. AMPA receptor traffcking and synaptic plasticity. Annu. Rev. Neurosci. 25, 103-126 (2002).
    • (2002) Annu. Rev. Neurosci. , vol.25 , pp. 103-126
    • Malinow, R.1    Malenka, R.C.2
  • 16
    • 33646123087 scopus 로고    scopus 로고
    • Dual role of the exocyst in AMPA receptor targeting and insertion into the postsynaptic membrane
    • Gerges, N.Z., Backos, D.S., Rupasinghe, C.N., Spaller, M.R. & Esteban, J.A. Dual role of the exocyst in AMPA receptor targeting and insertion into the postsynaptic membrane. EMBO J. 25, 1623-1634 (2006).
    • (2006) EMBO J. , vol.25 , pp. 1623-1634
    • Gerges, N.Z.1    Backos, D.S.2    Rupasinghe, C.N.3    Spaller, M.R.4    Esteban, J.A.5
  • 17
    • 0141737070 scopus 로고    scopus 로고
    • Direct imaging of lateral movements of AMPA receptors inside synapses
    • Tardin, C., Cognet, L., Bats, C., Lounis, B. & Choquet, D. Direct imaging of lateral movements of AMPA receptors inside synapses. EMBO J. 22, 4656-4665 (2003).
    • (2003) EMBO J. , vol.22 , pp. 4656-4665
    • Tardin, C.1    Cognet, L.2    Bats, C.3    Lounis, B.4    Choquet, D.5
  • 18
    • 0034693264 scopus 로고    scopus 로고
    • Distinct polyphosphoinositide binding selectivities for pleckstrin homology domains of GRP1-like proteins based on diglycine versus triglycine motifs
    • Klarlund, J.K., Tsiaras, W., Holik, J.J., Chawla, A. & Czech, M.P. Distinct polyphosphoinositide binding selectivities for pleckstrin homology domains of GRP1-like proteins based on diglycine versus triglycine motifs. J. Biol. Chem. 275, 32816-32821 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 32816-32821
    • Klarlund, J.K.1    Tsiaras, W.2    Holik, J.J.3    Chawla, A.4    Czech, M.P.5
  • 19
    • 28844462293 scopus 로고    scopus 로고
    • Phosphatidylinositol 3,4,5-trisphosphate mediates aldosterone stimulation of epithelial sodium channel (ENaC) and interacts with gamma-ENaC
    • Helms, M.N. et al. Phosphatidylinositol 3,4,5-trisphosphate mediates aldosterone stimulation of epithelial sodium channel (ENaC) and interacts with gamma-ENaC. J. Biol. Chem. 280, 40885-40891 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 40885-40891
    • Helms, M.N.1
  • 20
    • 27844469655 scopus 로고    scopus 로고
    • Selective cellular effects of overexpressed pleckstrin-homology domains that recognize PtdIns(3,4,5)P3 suggest their interaction with protein binding partners
    • Varnai, P. et al. Selective cellular effects of overexpressed pleckstrin-homology domains that recognize PtdIns(3,4,5)P3 suggest their interaction with protein binding partners. J. Cell Sci. 118, 4879-4888 (2005).
    • (2005) J. Cell Sci. , vol.118 , pp. 4879-4888
    • Varnai, P.1
  • 21
    • 0029943605 scopus 로고    scopus 로고
    • Membrane localization of phosphatidylinositol 3-kinase is suffcient to activate multiple signal-transducing kinase pathways
    • Klippel, A. et al. Membrane localization of phosphatidylinositol 3-kinase is suffcient to activate multiple signal-transducing kinase pathways. Mol. Cell. Biol. 16, 4117-4127 (1996).
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4117-4127
    • Klippel, A.1
  • 23
    • 2542448005 scopus 로고    scopus 로고
    • + channel by phosphatidylinositol 3,4,5-trisphosphate and phosphatidylinositol 3,4-bisphosphate produced by phosphoinositide 3-OH kinase
    • + channel by phosphatidylinositol 3,4,5-trisphosphate and phosphatidylinositol 3,4-bisphosphate produced by phosphoinositide 3-OH kinase. J. Biol. Chem. 279, 22654-22663 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 22654-22663
    • Tong, Q.1    Gamper, N.2    Medina, J.L.3    Shapiro, M.S.4    Stockand, J.D.5
  • 24
    • 0029977616 scopus 로고    scopus 로고
    • Evidence for multiple AMPA receptor complexes in hippocampal CA1/CA2 neurons
    • Wenthold, R.J., Petralia, R.S., Blahos, J. II & Niedzielski, A.S. Evidence for multiple AMPA receptor complexes in hippocampal CA1/CA2 neurons. J. Neurosci. 16, 1982-1989 (1996).
    • (1996) J. Neurosci. , vol.16 , pp. 1982-1989
    • Wenthold, R.J.1    Petralia, R.S.2    Blahos, I.I.J.3    Niedzielski, A.S.4
  • 26
  • 27
    • 65249185511 scopus 로고    scopus 로고
    • Subunit composition of synaptic AMPA receptors revealed by a single-cell genetic approach
    • Lu, W. et al. Subunit composition of synaptic AMPA receptors revealed by a single-cell genetic approach. Neuron 62, 254-268 (2009).
    • (2009) Neuron , vol.62 , pp. 254-268
    • Lu, W.1
  • 28
    • 0035805143 scopus 로고    scopus 로고
    • Subunit-specifc rules governing AMPA receptor traffcking to synapses in hippocampal pyramidal neurons
    • Shi, S., Hayashi, Y., Esteban, J.A. & Malinow, R. Subunit-specifc rules governing AMPA receptor traffcking to synapses in hippocampal pyramidal neurons. Cell 105, 331-343 (2001).
    • (2001) Cell , vol.105 , pp. 331-343
    • Shi, S.1    Hayashi, Y.2    Esteban, J.A.3    Malinow, R.4
  • 29
    • 0034708587 scopus 로고    scopus 로고
    • Driving AMPA receptors into synapses by LTP and CaMKII: Requirement for GluR1 and PDZ domain interaction
    • Hayashi, Y. et al. Driving AMPA receptors into synapses by LTP and CaMKII: requirement for GluR1 and PDZ domain interaction. Science 287, 2262-2267 (2000).
    • (2000) Science , vol.287 , pp. 2262-2267
    • Hayashi, Y.1
  • 30
    • 33847162742 scopus 로고    scopus 로고
    • The interaction between Stargazin and PSD-95 regulates AMPA receptor surface traffcking
    • Bats, C., Groc, L. & Choquet, D. The interaction between Stargazin and PSD-95 regulates AMPA receptor surface traffcking. Neuron 53, 719-734 (2007).
    • (2007) Neuron , vol.53 , pp. 719-734
    • Bats, C.1    Groc, L.2    Choquet, D.3
  • 31
    • 0037109042 scopus 로고    scopus 로고
    • Direct interactions between PSD-95 and stargazin control synaptic AMPA receptor number
    • Schnell, E. et al. Direct interactions between PSD-95 and stargazin control synaptic AMPA receptor number. Proc. Natl. Acad. Sci. USA 99, 13902-13907 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 13902-13907
    • Schnell, E.1
  • 32
    • 0742322856 scopus 로고    scopus 로고
    • Postsynaptic density 95 controls AMPA receptor incorporation during long-term potentiation and experience-driven synaptic plasticity
    • Ehrlich, I. & Malinow, R. Postsynaptic density 95 controls AMPA receptor incorporation during long-term potentiation and experience-driven synaptic plasticity. J. Neurosci. 24, 916-927 (2004).
    • (2004) J. Neurosci. , vol.24 , pp. 916-927
    • Ehrlich, I.1    Malinow, R.2
  • 33
    • 0038045645 scopus 로고    scopus 로고
    • Postsynaptic density-95 mimics and occludes hippocampal long-term potentiation and enhances long-term depression
    • Stein, V., House, D.R., Bredt, D.S. & Nicoll, R.A. Postsynaptic density-95 mimics and occludes hippocampal long-term potentiation and enhances long-term depression. J. Neurosci. 23, 5503-5506 (2003).
    • (2003) J. Neurosci. , vol.23 , pp. 5503-5506
    • Stein, V.1    House, D.R.2    Bredt, D.S.3    Nicoll, R.A.4
  • 34
    • 33644560354 scopus 로고    scopus 로고
    • Glutamate receptor exocytosis and spine enlargement during chemically induced long-term potentiation
    • Kopec, C.D., Li, B., Wei, W., Boehm, J. & Malinow, R. Glutamate receptor exocytosis and spine enlargement during chemically induced long-term potentiation. J. Neurosci. 26, 2000-2009 (2006).
    • (2006) J. Neurosci. , vol.26 , pp. 2000-2009
    • Kopec, C.D.1    Li, B.2    Wei, W.3    Boehm, J.4    Malinow, R.5
  • 35
    • 0038022657 scopus 로고    scopus 로고
    • Functional studies and distribution defne a family of transmembrane AMPA receptor regulatory proteins
    • Tomita, S. et al. Functional studies and distribution defne a family of transmembrane AMPA receptor regulatory proteins. J. Cell Biol. 161, 805-816 (2003).
    • (2003) J. Cell Biol. , vol.161 , pp. 805-816
    • Tomita, S.1
  • 36
    • 0026734317 scopus 로고
    • Three-dimensional structure of dendritic spines and synapses in rat hippocampus (CA1) at postnatal day 15 and adult ages: Implications for the maturation of synaptic physiology and long-term potentiation
    • Harris, K.M., Jensen, F.E. & Tsao, B. Three-dimensional structure of dendritic spines and synapses in rat hippocampus (CA1) at postnatal day 15 and adult ages: implications for the maturation of synaptic physiology and long-term potentiation. J. Neurosci. 12, 2685-2705 (1992).
    • (1992) J. Neurosci. , vol.12 , pp. 2685-2705
    • Harris, K.M.1    Jensen, F.E.2    Tsao, B.3
  • 38
    • 0028051595 scopus 로고
    • The glutamate uptake inhibitor L-trans-pyrrolidine-2,4-dicarboxylate depresses excitatory synaptic transmission via a presynaptic mechanism in cultured hippocampal neurons
    • Maki, R., Robinson, M.B. & Dichter, M.A. The glutamate uptake inhibitor L-trans-pyrrolidine-2,4-dicarboxylate depresses excitatory synaptic transmission via a presynaptic mechanism in cultured hippocampal neurons. J. Neurosci. 14, 6754-6762 (1994).
    • (1994) J. Neurosci. , vol.14 , pp. 6754-6762
    • Maki, R.1    Robinson, M.B.2    Dichter, M.A.3
  • 39
    • 67249087641 scopus 로고    scopus 로고
    • Soluble oligomers of amyloid β protein facilitate hippocampal long-term depression by disrupting neuronal glutamate uptake
    • Li, S. et al. Soluble oligomers of amyloid β protein facilitate hippocampal long-term depression by disrupting neuronal glutamate uptake. Neuron 62, 788-801 (2009).
    • (2009) Neuron , vol.62 , pp. 788-801
    • Li, S.1
  • 40
    • 0027369524 scopus 로고
    • The uptake inhibitor L-trans-PDC enhances responses to glutamate but fails to alter the kinetics of excitatory synaptic currents in the hippocampus
    • Isaacson, J.S. & Nicoll, R.A. The uptake inhibitor L-trans-PDC enhances responses to glutamate but fails to alter the kinetics of excitatory synaptic currents in the hippocampus. J. Neurophysiol. 70, 2187-2191 (1993).
    • (1993) J. Neurophysiol. , vol.70 , pp. 2187-2191
    • Isaacson, J.S.1    Nicoll, R.A.2
  • 41
    • 33745215607 scopus 로고    scopus 로고
    • Signalling mechanisms mediated by the phosphoinositide 3-kinase/Akt cascade in synaptic plasticity and memory in the rat
    • Horwood, J.M., Dufour, F., Laroche, S. & Davis, S. Signalling mechanisms mediated by the phosphoinositide 3-kinase/Akt cascade in synaptic plasticity and memory in the rat. Eur. J. Neurosci. 23, 3375-3384 (2006).
    • (2006) Eur. J. Neurosci. , vol.23 , pp. 3375-3384
    • Horwood, J.M.1    Dufour, F.2    Laroche, S.3    Davis, S.4
  • 42
    • 0036724203 scopus 로고    scopus 로고
    • Activity-dependent NMDA receptor-mediated activation of protein kinase B/Akt in cortical neuronal cultures
    • Sutton, G. & Chandler, L.J. Activity-dependent NMDA receptor-mediated activation of protein kinase B/Akt in cortical neuronal cultures. J. Neurochem. 82, 1097-1105 (2002).
    • (2002) J. Neurochem. , vol.82 , pp. 1097-1105
    • Sutton, G.1    Chandler, L.J.2
  • 43
    • 33749648798 scopus 로고    scopus 로고
    • Synapse-specifc and developmentally regulated targeting of AMPA receptors by a family of MAGUK scaffolding proteins
    • Elias, G.M. et al. Synapse-specifc and developmentally regulated targeting of AMPA receptors by a family of MAGUK scaffolding proteins. Neuron 52, 307-320 (2006).
    • (2006) Neuron , vol.52 , pp. 307-320
    • Elias, G.M.1
  • 44
    • 33748313081 scopus 로고    scopus 로고
    • The prevalence and signifcance of PDZ domain-phosphoinositide interactions
    • Zimmermann, P. The prevalence and signifcance of PDZ domain- phosphoinositide interactions. Biochim. Biophys. Acta 1761, 947-956 (2006).
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 947-956
    • Zimmermann, P.1
  • 45
    • 33845313646 scopus 로고    scopus 로고
    • PI(3,4,5)P3 and PI(4,5)P2 lipids target proteins with polybasic clusters to the plasma membrane
    • Heo, W.D. et al. PI(3,4,5)P3 and PI(4,5)P2 lipids target proteins with polybasic clusters to the plasma membrane. Science 314, 1458-1461 (2006).
    • (2006) Science , vol.314 , pp. 1458-1461
    • Heo, W.D.1
  • 46
    • 33644854568 scopus 로고    scopus 로고
    • Lipid binding regulates synaptic targeting of PICK1 AMPA receptor traffcking and synaptic plasticity
    • Jin, W. et al. Lipid binding regulates synaptic targeting of PICK1, AMPA receptor traffcking, and synaptic plasticity. J. Neurosci. 26, 2380-2390 (2006).
    • (2006) J. Neurosci. , vol.26 , pp. 2380-2390
    • Jin, W.1
  • 47
    • 0037062424 scopus 로고    scopus 로고
    • A monomeric red fuorescent protein
    • Campbell, R.E. et al. A monomeric red fuorescent protein. Proc. Natl. Acad. Sci. USA 99, 7877-7882 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 7877-7882
    • Campbell, R.E.1
  • 48
    • 0028987110 scopus 로고
    • An osmium-free method of epon embedment that preserves both ultrastructure and antigenicity for post-embedding immunocytochemistry
    • Phend, K.D., Rustioni, A. & Weinberg, R.J. An osmium-free method of epon embedment that preserves both ultrastructure and antigenicity for post-embedding immunocytochemistry. J. Histochem. Cytochem. 43, 283-292 (1995).
    • (1995) J. Histochem. Cytochem. , vol.43 , pp. 283-292
    • Phend, K.D.1    Rustioni, A.2    Weinberg, R.J.3


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