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Volumn 104, Issue 3, 2008, Pages 596-610

Ca2+/calmodulin-dependent protein kinase IIα clusters are associated with stable lipid rafts and their formation traps PSD-95

Author keywords

Ca2+ calmodulin dependent protein kinase II cluster; Lipid raft; Post synaptic density; Post synaptic density 95

Indexed keywords

FLOTILLIN 1; GANGLIOSIDE GM1; IONOMYCIN; METHYL BETA CYCLODEXTRIN; POSTSYNAPTIC DENSITY PROTEIN 95; PROTEIN KINASE (CALCIUM,CALMODULIN) II; TRITON X 100; BETA CYCLODEXTRIN DERIVATIVE; CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE KINASE; DLGH4 PROTEIN, RAT; FLOTILLINS; GREEN FLUORESCENT PROTEIN; IONOPHORE; MEMBRANE PROTEIN; METHYL-BETA-CYCLODEXTRIN; OCTOXINOL; SIGNAL PEPTIDE; SURFACTANT; SYNAPTOPHYSIN; UNCLASSIFIED DRUG;

EID: 38049171259     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2007.05035.x     Document Type: Article
Times cited : (26)

References (55)
  • 2
    • 0035877299 scopus 로고    scopus 로고
    • Electron microscopic immunocytochemical detection of PSD-95, PSD-93, SAP-102, and SAP-97 at postsynaptic, presynaptic, and nonsynaptic sites of adult and neonatal rat visual cortex
    • Aoki C., Miko I., Oviedo H., Mikeladze-Dvali T., Alexandre L., Sweeney N. Bredt D. S. (2001) Electron microscopic immunocytochemical detection of PSD-95, PSD-93, SAP-102, and SAP-97 at postsynaptic, presynaptic, and nonsynaptic sites of adult and neonatal rat visual cortex. Synapse 40, 239 257.
    • (2001) Synapse , vol.40 , pp. 239-257
    • Aoki, C.1    Miko, I.2    Oviedo, H.3    Mikeladze-Dvali, T.4    Alexandre, L.5    Sweeney, N.6    Bredt, D.S.7
  • 3
    • 26944487610 scopus 로고    scopus 로고
    • NMDA receptor subunit composition controls synaptic plasticity by regulating binding to CaMKII
    • Barria A. Malinow R. (2005) NMDA receptor subunit composition controls synaptic plasticity by regulating binding to CaMKII. Neuron 48, 289 301.
    • (2005) Neuron , vol.48 , pp. 289-301
    • Barria, A.1    Malinow, R.2
  • 4
    • 22444434670 scopus 로고    scopus 로고
    • Amphotropic murine leukaemia virus envelope protein is associated with cholesterol-rich microdomains
    • Beer C., Pedersen L. Wirth M. (2005) Amphotropic murine leukaemia virus envelope protein is associated with cholesterol-rich microdomains. Virol. J. 2, 36 44.
    • (2005) Virol. J. , vol.2 , pp. 36-44
    • Beer, C.1    Pedersen, L.2    Wirth, M.3
  • 5
    • 0027226219 scopus 로고
    • Optimized survival of hippocampal neurons in B27-supplemented Neurobasal, a new serum-free medium combination
    • Brewer G. J., Torricelli J. R., Evege E. K. Price P. J. (1993) Optimized survival of hippocampal neurons in B27-supplemented Neurobasal, a new serum-free medium combination. J. Neurosci. Res. 35, 567 576.
    • (1993) J. Neurosci. Res. , vol.35 , pp. 567-576
    • Brewer, G.J.1    Torricelli, J.R.2    Evege, E.K.3    Price, P.J.4
  • 6
    • 0034625373 scopus 로고    scopus 로고
    • Structure and function of sphingolipid- and cholesterol-rich membrane rafts
    • Brown D. A. London E. (2000) Structure and function of sphingolipid- and cholesterol-rich membrane rafts. J. Biol. Chem. 275, 17221 17224.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17221-17224
    • Brown, D.A.1    London, E.2
  • 7
    • 0038439320 scopus 로고    scopus 로고
    • The role of receptor diffusion in the organization of the postsynaptic membrane
    • Choquet D. Triller A. (2003) The role of receptor diffusion in the organization of the postsynaptic membrane. Nat. Rev. Neurosci. 4, 251 265.
    • (2003) Nat. Rev. Neurosci. , vol.4 , pp. 251-265
    • Choquet, D.1    Triller, A.2
  • 8
    • 0030695849 scopus 로고    scopus 로고
    • Use of cyclodextrins for manipulating cellular cholesterol content
    • Christian A. E., Haynes M. P., Phillips M. C. Rothblat G. H. (1997) Use of cyclodextrins for manipulating cellular cholesterol content. J. Lipid Res. 38, 2264 2272.
    • (1997) J. Lipid Res. , vol.38 , pp. 2264-2272
    • Christian, A.E.1    Haynes, M.P.2    Phillips, M.C.3    Rothblat, G.H.4
  • 9
    • 2942607447 scopus 로고    scopus 로고
    • Calcium/calmodulin-dependent protein kinase II and synaptic plasticity
    • Colbran R. J. Brown A. M. (2004) Calcium/calmodulin-dependent protein kinase II and synaptic plasticity. Curr. Opin. Neurobiol. 14, 318 327.
    • (2004) Curr. Opin. Neurobiol. , vol.14 , pp. 318-327
    • Colbran, R.J.1    Brown, A.M.2
  • 10
    • 0034193398 scopus 로고    scopus 로고
    • A novel particulate form of Ca(2+)/calmodulin-dependent [correction of Ca(2+)/CaMKII-dependent] protein kinase II in neurons
    • Dosemeci A., Reese T. S., Petersen J. Tao-Cheng J. H. (2000) A novel particulate form of Ca(2+)/calmodulin-dependent [correction of Ca(2+)/CaMKII-dependent] protein kinase II in neurons. J. Neurosci. 20, 3076 3084.
    • (2000) J. Neurosci. , vol.20 , pp. 3076-3084
    • Dosemeci, A.1    Reese, T.S.2    Petersen, J.3    Tao-Cheng, J.H.4
  • 12
    • 33746214631 scopus 로고    scopus 로고
    • Mechanisms for association of Ca2+/calmodulin-dependent protein kinase II with lipid rafts
    • Du F., Saitoh F., Tian Q. B., Miyazawa S., Endo S. Suzuki T. (2006) Mechanisms for association of Ca2+/calmodulin-dependent protein kinase II with lipid rafts. Biochem. Biophys. Res. Commun. 347, 814 820.
    • (2006) Biochem. Biophys. Res. Commun. , vol.347 , pp. 814-820
    • Du, F.1    Saitoh, F.2    Tian, Q.B.3    Miyazawa, S.4    Endo, S.5    Suzuki, T.6
  • 13
    • 0034627757 scopus 로고    scopus 로고
    • Dual palmitoylation of PSD-95 mediates its vesiculotubular sorting, postsynaptic targeting, and ion channel clustering
    • El-Husseini A. E., Craven S. E., Chetkovich D. M., Firestein B. L., Schnell E., Aoki C. Bredt D. S. (2000) Dual palmitoylation of PSD-95 mediates its vesiculotubular sorting, postsynaptic targeting, and ion channel clustering. J. Cell Biol. 148, 159 172.
    • (2000) J. Cell Biol. , vol.148 , pp. 159-172
    • El-Husseini, A.E.1    Craven, S.E.2    Chetkovich, D.M.3    Firestein, B.L.4    Schnell, E.5    Aoki, C.6    Bredt, D.S.7
  • 14
    • 0037016687 scopus 로고    scopus 로고
    • Parkin and CASK/LIN-2 associate via a PDZ-mediated interaction and are co-localized in lipid rafts and postsynaptic densities in brain
    • Fallon L., Moreau F., Croft B. G., Labib N., Gu W. J. Fon E. A. (2002) Parkin and CASK/LIN-2 associate via a PDZ-mediated interaction and are co-localized in lipid rafts and postsynaptic densities in brain. J. Biol. Chem. 277, 486 491.
    • (2002) J. Biol. Chem. , vol.277 , pp. 486-491
    • Fallon, L.1    Moreau, F.2    Croft, B.G.3    Labib, N.4    Gu, W.J.5    Fon, E.A.6
  • 15
    • 2142648724 scopus 로고    scopus 로고
    • CaMKII, an enzyme on the move: Regulation of temporospatial localization
    • Griffith L. C., Lu C. S. Sun X. X. (2003) CaMKII, an enzyme on the move: regulation of temporospatial localization. Mol. Interv. 3, 386 403.
    • (2003) Mol. Interv. , vol.3 , pp. 386-403
    • Griffith, L.C.1    Lu, C.S.2    Sun, X.X.3
  • 16
    • 0037996880 scopus 로고    scopus 로고
    • Lipid rafts in the maintenance of synapses, dendritic spines, and surface AMPA receptor stability
    • Hering H., Lin C. C. Sheng M. (2003) Lipid rafts in the maintenance of synapses, dendritic spines, and surface AMPA receptor stability. J. Neurosci. 23, 3262 3271.
    • (2003) J. Neurosci. , vol.23 , pp. 3262-3271
    • Hering, H.1    Lin, C.C.2    Sheng, M.3
  • 17
    • 3242690769 scopus 로고    scopus 로고
    • Secretory trafficking in neuronal dendrites
    • Horton A. C. Ehlers M. D. (2004) Secretory trafficking in neuronal dendrites. Nat. Cell Biol. 6, 585 591.
    • (2004) Nat. Cell Biol. , vol.6 , pp. 585-591
    • Horton, A.C.1    Ehlers, M.D.2
  • 18
    • 0029882409 scopus 로고    scopus 로고
    • Inactivation and self-association of Ca2+/calmodulin-dependent protein kinase II during autophosphorylation
    • Hudmon A., Aronowski J., Kolb S. J. Waxham M. N. (1996) Inactivation and self-association of Ca2+/calmodulin-dependent protein kinase II during autophosphorylation. J. Biol. Chem. 271, 8800 8808.
    • (1996) J. Biol. Chem. , vol.271 , pp. 8800-8808
    • Hudmon, A.1    Aronowski, J.2    Kolb, S.J.3    Waxham, M.N.4
  • 19
    • 0035095802 scopus 로고    scopus 로고
    • Light scattering and transmission electron microscopy studies reveal a mechanism for calcium/calmodulin-dependent protein kinase II self-association
    • Hudmon A., Kim S. A., Kolb S. J., Stoops J. K. Waxham M. N. (2001) Light scattering and transmission electron microscopy studies reveal a mechanism for calcium/calmodulin-dependent protein kinase II self-association. J. Neurochem. 76, 1364 1375.
    • (2001) J. Neurochem. , vol.76 , pp. 1364-1375
    • Hudmon, A.1    Kim, S.A.2    Kolb, S.J.3    Stoops, J.K.4    Waxham, M.N.5
  • 20
    • 23044493437 scopus 로고    scopus 로고
    • A mechanism for Ca2+/calmodulin-dependent protein kinase II clustering at synaptic and nonsynaptic sites based on self-association
    • Hudmon A., Lebel E., Roy H., Sik A., Schulman H., Waxham M. N. De Koninck P. (2005) A mechanism for Ca2+/calmodulin-dependent protein kinase II clustering at synaptic and nonsynaptic sites based on self-association. J. Neurosci. 25, 6971 6983.
    • (2005) J. Neurosci. , vol.25 , pp. 6971-6983
    • Hudmon, A.1    Lebel, E.2    Roy, H.3    Sik, A.4    Schulman, H.5    Waxham, M.N.6    De Koninck, P.7
  • 21
    • 28344440027 scopus 로고    scopus 로고
    • CaMKII structure - An elegant design
    • Hunter T. Schulman H. (2005) CaMKII structure - an elegant design. Cell 123, 765 767.
    • (2005) Cell , vol.123 , pp. 765-767
    • Hunter, T.1    Schulman, H.2
  • 22
    • 0032532271 scopus 로고    scopus 로고
    • Effects of cholesterol depletion by cyclodextrin on the sphingolipid microdomains of the plasma membrane
    • Ilangumaran S. Hoessli D. C. (1998) Effects of cholesterol depletion by cyclodextrin on the sphingolipid microdomains of the plasma membrane. Biochem. J. 335 (Pt. 2 433 440.
    • (1998) Biochem. J. , vol.335 , Issue.2 , pp. 433-440
    • Ilangumaran, S.1    Hoessli, D.C.2
  • 23
    • 3042662329 scopus 로고    scopus 로고
    • Brain-specific potential guanine nucleotide exchange factor for Arf, synArfGEF (Po), is localized to postsynaptic density
    • Inaba Y., Tian Q. B., Okano A. et al. (2004) Brain-specific potential guanine nucleotide exchange factor for Arf, synArfGEF (Po), is localized to postsynaptic density. J. Neurochem. 89, 1347 1357.
    • (2004) J. Neurochem. , vol.89 , pp. 1347-1357
    • Inaba, Y.1    Tian, Q.B.2    Okano, A.3
  • 24
    • 12244260817 scopus 로고    scopus 로고
    • The postsynaptic density and dendritic raft localization of PSD-Zip70, which contains an N-myristoylation sequence and leucine-zipper motifs
    • Konno D., Ko J. A., Usui S. et al. (2002) The postsynaptic density and dendritic raft localization of PSD-Zip70, which contains an N-myristoylation sequence and leucine-zipper motifs. J. Cell Sci. 115, 4695 4706.
    • (2002) J. Cell Sci. , vol.115 , pp. 4695-4706
    • Konno, D.1    Ko, J.A.2    Usui, S.3
  • 25
    • 29144483525 scopus 로고    scopus 로고
    • Toward understanding the dynamics of membrane-raft-based molecular interactions
    • Kusumi A. Suzuki K. (2005) Toward understanding the dynamics of membrane-raft-based molecular interactions. Biochim. Biophys. Acta 1746, 234 251.
    • (2005) Biochim. Biophys. Acta , vol.1746 , pp. 234-251
    • Kusumi, A.1    Suzuki, K.2
  • 27
    • 0038673369 scopus 로고    scopus 로고
    • Ligand-dependent recruitment of the ErbB4 signaling complex into neuronal lipid rafts
    • Ma L., Huang Y. Z., Pitcher G. M. et al. (2003) Ligand-dependent recruitment of the ErbB4 signaling complex into neuronal lipid rafts. J. Neurosci. 23, 3164 3175.
    • (2003) J. Neurosci. , vol.23 , pp. 3164-3175
    • Ma, L.1    Huang, Y.Z.2    Pitcher, G.M.3
  • 28
    • 0033067455 scopus 로고    scopus 로고
    • Glycolipid-enriched caveolae and caveolae-like domains in the nervous system
    • Masserini M., Palestini P. Pitto M. (1999) Glycolipid-enriched caveolae and caveolae-like domains in the nervous system. J. Neurochem. 73, 1 11.
    • (1999) J. Neurochem. , vol.73 , pp. 1-11
    • Masserini, M.1    Palestini, P.2    Pitto, M.3
  • 29
    • 3242672694 scopus 로고    scopus 로고
    • Calcium/calmodulin-dependent protein kinase II phosphorylation drives synapse-associated protein 97 into spines
    • Mauceri D., Cattabeni F., Di Luca M. Gardoni F. (2004) Calcium/calmodulin-dependent protein kinase II phosphorylation drives synapse-associated protein 97 into spines. J. Biol. Chem. 279, 23813 23821.
    • (2004) J. Biol. Chem. , vol.279 , pp. 23813-23821
    • Mauceri, D.1    Cattabeni, F.2    Di Luca, M.3    Gardoni, F.4
  • 30
    • 0037044851 scopus 로고    scopus 로고
    • Proteomic analysis of a detergent-resistant membrane skeleton from neutrophil plasma membranes
    • Nebl T., Pestonjamasp K. N., Leszyk J. D., Crowley J. L., Oh S. W. Luna E. J. (2002) Proteomic analysis of a detergent-resistant membrane skeleton from neutrophil plasma membranes. J. Biol. Chem. 277, 43399 43409.
    • (2002) J. Biol. Chem. , vol.277 , pp. 43399-43409
    • Nebl, T.1    Pestonjamasp, K.N.2    Leszyk, J.D.3    Crowley, J.L.4    Oh, S.W.5    Luna, E.J.6
  • 31
    • 1642271441 scopus 로고    scopus 로고
    • Membrane and raft association of reggie-1/flotillin-2: Role of myristoylation, palmitoylation and oligomerization and induction of filopodia by overexpression
    • Neumann-Giesen C., Falkenbach B., Beicht P., Claasen S., Luers G., Stuermer C. A., Herzog V. Tikkanen R. (2004) Membrane and raft association of reggie-1/flotillin-2: role of myristoylation, palmitoylation and oligomerization and induction of filopodia by overexpression. Biochem. J. 378, 509 518.
    • (2004) Biochem. J. , vol.378 , pp. 509-518
    • Neumann-Giesen, C.1    Falkenbach, B.2    Beicht, P.3    Claasen, S.4    Luers, G.5    Stuermer, C.A.6    Herzog, V.7    Tikkanen, R.8
  • 32
    • 0344837802 scopus 로고    scopus 로고
    • Huntingtin-interacting protein-1-related protein of rat (rHIP1R) is localized in the postsynaptic regions
    • Okano A., Usuda N., Furihata K., Nakayama K., Bao Tian Q., Okamoto T. Suzuki T. (2003) Huntingtin-interacting protein-1-related protein of rat (rHIP1R) is localized in the postsynaptic regions. Brain Res. 967, 210 225.
    • (2003) Brain Res. , vol.967 , pp. 210-225
    • Okano, A.1    Usuda, N.2    Furihata, K.3    Nakayama, K.4    Bao Tian, Q.5    Okamoto, T.6    Suzuki, T.7
  • 33
    • 0033607680 scopus 로고    scopus 로고
    • Glycosphingolipids are not essential for formation of detergent-resistant membrane rafts in melanoma cells. Methyl-β-cyclodextrin does not affect cell surface transport of a GPI-anchored protein
    • Ostermeyer A. G., Beckrich B. T., Ivarson K. A., Grove K. E. Brown D. A. (1999) Glycosphingolipids are not essential for formation of detergent-resistant membrane rafts in melanoma cells. Methyl-β-cyclodextrin does not affect cell surface transport of a GPI-anchored protein. J. Biol. Chem. 274, 34459 34466.
    • (1999) J. Biol. Chem. , vol.274 , pp. 34459-34466
    • Ostermeyer, A.G.1    Beckrich, B.T.2    Ivarson, K.A.3    Grove, K.E.4    Brown, D.A.5
  • 34
    • 7044270772 scopus 로고    scopus 로고
    • Persistent accumulation of calcium/calmodulin-dependent protein kinase II in dendritic spines after induction of NMDA receptor-dependent chemical long-term potentiation
    • Otmakhov N., Tao-Cheng J. H., Carpenter S., Asrican B., Dosemeci A., Reese T. S. Lisman J. (2004) Persistent accumulation of calcium/calmodulin- dependent protein kinase II in dendritic spines after induction of NMDA receptor-dependent chemical long-term potentiation. J. Neurosci. 24, 9324 9331.
    • (2004) J. Neurosci. , vol.24 , pp. 9324-9331
    • Otmakhov, N.1    Tao-Cheng, J.H.2    Carpenter, S.3    Asrican, B.4    Dosemeci, A.5    Reese, T.S.6    Lisman, J.7
  • 35
    • 0032545181 scopus 로고    scopus 로고
    • The N-terminal PDZ-containing region of postsynaptic density-95 mediates association with caveolar-like lipid domains
    • Perez A. S. Bredt D. S. (1998) The N-terminal PDZ-containing region of postsynaptic density-95 mediates association with caveolar-like lipid domains. Neurosci. Lett. 258, 121 123.
    • (1998) Neurosci. Lett. , vol.258 , pp. 121-123
    • Perez, A.S.1    Bredt, D.S.2
  • 36
    • 0348010289 scopus 로고    scopus 로고
    • Distribution of postsynaptic density (PSD)-95 and Ca2+/calmodulin- dependent protein kinase II at the PSD
    • Petersen J. D., Chen X., Vinade L., Dosemeci A., Lisman J. E. Reese T. S. (2003) Distribution of postsynaptic density (PSD)-95 and Ca2+/calmodulin- dependent protein kinase II at the PSD. J. Neurosci. 23, 11270 11278.
    • (2003) J. Neurosci. , vol.23 , pp. 11270-11278
    • Petersen, J.D.1    Chen, X.2    Vinade, L.3    Dosemeci, A.4    Lisman, J.E.5    Reese, T.S.6
  • 38
    • 28244489857 scopus 로고    scopus 로고
    • Differential modulation of Ca2+/calmodulin-dependent protein kinase II activity by regulated interactions with N-methyl-D-aspartate receptor NR2B subunits and alpha-actinin
    • Robison A. J., Bartlett R. K., Bass M. A. Colbran R. J. (2005a) Differential modulation of Ca2+/calmodulin-dependent protein kinase II activity by regulated interactions with N-methyl-D-aspartate receptor NR2B subunits and alpha-actinin. J. Biol. Chem. 280, 39316 39323.
    • (2005) J. Biol. Chem. , vol.280 , pp. 39316-39323
    • Robison, A.J.1    Bartlett, R.K.2    Bass, M.A.3    Colbran, R.J.4
  • 39
    • 27444434998 scopus 로고    scopus 로고
    • Multivalent interactions of calcium/calmodulin-dependent protein kinase II with the postsynaptic density proteins NR2B, densin-180, and alpha-actinin-2
    • Robison A. J., Bass M. A., Jiao Y., MacMillan L. B., Carmody L. C., Bartlett R. K. Colbran R. J. (2005b) Multivalent interactions of calcium/calmodulin-dependent protein kinase II with the postsynaptic density proteins NR2B, densin-180, and alpha-actinin-2. J. Biol. Chem. 280, 35329 35336.
    • (2005) J. Biol. Chem. , vol.280 , pp. 35329-35336
    • Robison, A.J.1    Bass, M.A.2    Jiao, Y.3    MacMillan, L.B.4    Carmody, L.C.5    Bartlett, R.K.6    Colbran, R.J.7
  • 40
    • 3142727963 scopus 로고    scopus 로고
    • NIDD, a novel DHHC-containing protein, targets neuronal nitric-oxide synthase (nNOS) to the synaptic membrane through a PDZ-dependent interaction and regulates nNOS activity
    • Saitoh F., Tian Q. B., Okano A., Sakagami H., Kondo H. Suzuki T. (2004) NIDD, a novel DHHC-containing protein, targets neuronal nitric-oxide synthase (nNOS) to the synaptic membrane through a PDZ-dependent interaction and regulates nNOS activity. J. Biol. Chem. 279, 29461 29468.
    • (2004) J. Biol. Chem. , vol.279 , pp. 29461-29468
    • Saitoh, F.1    Tian, Q.B.2    Okano, A.3    Sakagami, H.4    Kondo, H.5    Suzuki, T.6
  • 41
    • 0031964607 scopus 로고    scopus 로고
    • Cholesterol and sphingolipid enhance the Triton X-100 insolubility of glycosylphosphatidylinositol-anchored proteins by promoting the formation of detergent-insoluble ordered membrane domains
    • Schroeder R. J., Ahmed S. N., Zhu Y., London E. Brown D. A. (1998) Cholesterol and sphingolipid enhance the Triton X-100 insolubility of glycosylphosphatidylinositol-anchored proteins by promoting the formation of detergent-insoluble ordered membrane domains. J. Biol. Chem. 273, 1150 1157.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1150-1157
    • Schroeder, R.J.1    Ahmed, S.N.2    Zhu, Y.3    London, E.4    Brown, D.A.5
  • 42
    • 0033515884 scopus 로고    scopus 로고
    • Dynamic control of CaMKII translocation and localization in hippocampal neurons by NMDA receptor stimulation
    • Shen K. Meyer T. (1999) Dynamic control of CaMKII translocation and localization in hippocampal neurons by NMDA receptor stimulation. Science 284, 162 166.
    • (1999) Science , vol.284 , pp. 162-166
    • Shen, K.1    Meyer, T.2
  • 43
    • 0141828502 scopus 로고    scopus 로고
    • Use of detergents to study membrane rafts: The good, the bad, and the ugly
    • Shogomori H. Brown D. A. (2003) Use of detergents to study membrane rafts: the good, the bad, and the ugly. Biol. Chem. 384, 1259 1263.
    • (2003) Biol. Chem. , vol.384 , pp. 1259-1263
    • Shogomori, H.1    Brown, D.A.2
  • 44
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K. Ikonen E. (1997) Functional rafts in cell membranes. Nature 387, 569 572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 45
    • 0031023590 scopus 로고    scopus 로고
    • Three-dimensional organization of smooth endoplasmic reticulum in hippocampal CA1 dendrites and dendritic spines of the immature and mature rat
    • Spacek J. Harris K. M. (1997) Three-dimensional organization of smooth endoplasmic reticulum in hippocampal CA1 dendrites and dendritic spines of the immature and mature rat. J. Neurosci. 17, 190 203.
    • (1997) J. Neurosci. , vol.17 , pp. 190-203
    • Spacek, J.1    Harris, K.M.2
  • 46
    • 0036768289 scopus 로고    scopus 로고
    • Lipid rafts at postsynaptic sites: Distribution, function and linkage to postsynaptic density
    • Suzuki T. (2002) Lipid rafts at postsynaptic sites: distribution, function and linkage to postsynaptic density. Neurosci. Res. 44, 1 9.
    • (2002) Neurosci. Res. , vol.44 , pp. 1-9
    • Suzuki, T.1
  • 47
    • 0028111814 scopus 로고
    • Rapid translocation of cytosolic Ca2+/calmodulin-dependent protein kinase II into postsynaptic density after decapitation
    • Suzuki T., Okumura-Noji K., Tanaka R. Tada T. (1994) Rapid translocation of cytosolic Ca2+/calmodulin-dependent protein kinase II into postsynaptic density after decapitation. J. Neurochem. 63, 1529 1537.
    • (1994) J. Neurochem. , vol.63 , pp. 1529-1537
    • Suzuki, T.1    Okumura-Noji, K.2    Tanaka, R.3    Tada, T.4
  • 48
    • 0035906258 scopus 로고    scopus 로고
    • Biochemical evidence for localization of AMPA-type glutamate receptor subunits in the dendritic raft
    • Suzuki T., Ito J., Takagi H., Saitoh F., Nawa H. Shimizu H. (2001) Biochemical evidence for localization of AMPA-type glutamate receptor subunits in the dendritic raft. Brain Res. Mol. Brain Res. 89, 20 28.
    • (2001) Brain Res. Mol. Brain Res. , vol.89 , pp. 20-28
    • Suzuki, T.1    Ito, J.2    Takagi, H.3    Saitoh, F.4    Nawa, H.5    Shimizu, H.6
  • 49
    • 13444301322 scopus 로고    scopus 로고
    • A novel scaffold protein, TANC, possibly a rat homolog of Drosophila rolling pebbles (rols), forms a multiprotein complex with various postsynaptic density proteins
    • Suzuki T., Li W., Zhang J. P., Tian Q. B., Sakagami H., Usuda N., Kondo H., Fujii T. Endo S. (2005) A novel scaffold protein, TANC, possibly a rat homolog of Drosophila rolling pebbles (rols), forms a multiprotein complex with various postsynaptic density proteins. Eur. J. Neurosci. 21, 339 350.
    • (2005) Eur. J. Neurosci. , vol.21 , pp. 339-350
    • Suzuki, T.1    Li, W.2    Zhang, J.P.3    Tian, Q.B.4    Sakagami, H.5    Usuda, N.6    Kondo, H.7    Fujii, T.8    Endo, S.9
  • 50
    • 3042552565 scopus 로고    scopus 로고
    • Secretagogue-induced translocation of CRHSP-28 within an early apical endosomal compartment in acinar cells
    • Thomas D. D., Weng N. Groblewski G. E. (2004) Secretagogue-induced translocation of CRHSP-28 within an early apical endosomal compartment in acinar cells. Am. J. Physiol. Gastrointest. Liver Physiol. 287, G253 G263.
    • (2004) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.287
    • Thomas, D.D.1    Weng, N.2    Groblewski, G.E.3
  • 51
    • 33745071526 scopus 로고    scopus 로고
    • Interaction of LDL receptor-related protein 4 (LRP4) with postsynaptic scaffold proteins via its C-terminal PDZ domain-binding motif, and its regulation by Ca/calmodulin-dependent protein kinase II
    • Tian Q. B., Suzuki T., Yamauchi T. et al. (2006) Interaction of LDL receptor-related protein 4 (LRP4) with postsynaptic scaffold proteins via its C-terminal PDZ domain-binding motif, and its regulation by Ca/calmodulin- dependent protein kinase II. Eur. J. Neurosci. 23, 2864 2876.
    • (2006) Eur. J. Neurosci. , vol.23 , pp. 2864-2876
    • Tian, Q.B.1    Suzuki, T.2    Yamauchi, T.3
  • 52
    • 0031932282 scopus 로고    scopus 로고
    • N-terminal palmitoylation of PSD-95 regulates association with cell membranes and interaction with K+ channel Kv1.4
    • Topinka J. R. Bredt D. S. (1998) N-terminal palmitoylation of PSD-95 regulates association with cell membranes and interaction with K+ channel Kv1.4. Neuron 20, 125 134.
    • (1998) Neuron , vol.20 , pp. 125-134
    • Topinka, J.R.1    Bredt, D.S.2
  • 53
    • 13244252410 scopus 로고    scopus 로고
    • BAALC 1-6-8 protein is targeted to postsynaptic lipid rafts by its N-terminal myristoylation and palmitoylation, and interacts with alpha, but not beta, subunit of Ca/calmodulin-dependent protein kinase II
    • Wang X., Tian Q. B., Okano A., Sakagami H., Moon I. S., Kondo H., Endo S. Suzuki T. (2005) BAALC 1-6-8 protein is targeted to postsynaptic lipid rafts by its N-terminal myristoylation and palmitoylation, and interacts with alpha, but not beta, subunit of Ca/calmodulin-dependent protein kinase II. J. Neurochem. 92, 647 659.
    • (2005) J. Neurochem. , vol.92 , pp. 647-659
    • Wang, X.1    Tian, Q.B.2    Okano, A.3    Sakagami, H.4    Moon, I.S.5    Kondo, H.6    Endo, S.7    Suzuki, T.8
  • 54
    • 0347052880 scopus 로고    scopus 로고
    • Differential recruitment of Kv1.4 and Kv4.2 to lipid rafts by PSD-95
    • Wong W. Schlichter L. C. (2004) Differential recruitment of Kv1.4 and Kv4.2 to lipid rafts by PSD-95. J. Biol. Chem. 279, 444 452.
    • (2004) J. Biol. Chem. , vol.279 , pp. 444-452
    • Wong, W.1    Schlichter, L.C.2
  • 55
    • 0037012847 scopus 로고    scopus 로고
    • Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells
    • Zacharias D. A., Violin J. D., Newton A. C. Tsien R. Y. (2002) Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells. Science 296, 913 916.
    • (2002) Science , vol.296 , pp. 913-916
    • Zacharias, D.A.1    Violin, J.D.2    Newton, A.C.3    Tsien, R.Y.4


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