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Volumn 17, Issue 12, 2003, Pages 2521-2528

Bidirectional synaptic plasticity as a consequence of interdependent Ca2+-controlled phosphorylation and dephosphorylation pathways

Author keywords

AMPA receptor; CaMKII; LTD; LTP; PP1

Indexed keywords

AMPA RECEPTOR; CALCINEURIN; CALCIUM CHANNEL; CALCIUM ION; PHOSPHOPROTEIN PHOSPHATASE 1; PROTEIN KINASE (CALCIUM,CALMODULIN) II;

EID: 0037670369     PISSN: 0953816X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1460-9568.2003.02693.x     Document Type: Article
Times cited : (58)

References (42)
  • 1
    • 0030952362 scopus 로고    scopus 로고
    • Genetic demonstration of a role for PKA in the late phase of LTP and in hippocampus-based long-term memory
    • Abel, T., Nguyen, P.V., Barad, M., Deuel, T.A., Kandel, E.R. & Bourtchouladze, R. (1997) Genetic demonstration of a role for PKA in the late phase of LTP and in hippocampus-based long-term memory. Cell, 88, 615-626.
    • (1997) Cell , vol.88 , pp. 615-626
    • Abel, T.1    Nguyen, P.V.2    Barad, M.3    Deuel, T.A.4    Kandel, E.R.5    Bourtchouladze, R.6
  • 2
    • 0032565873 scopus 로고    scopus 로고
    • Modulation of AMPA receptor unitary conductance by synaptic activity
    • Benke, T.A., Luthi, A., Isaac, J.T. & Collingridge, G.L. (1998) Modulation of AMPA receptor unitary conductance by synaptic activity. Nature, 393, 793-797.
    • (1998) Nature , vol.393 , pp. 793-797
    • Benke, T.A.1    Luthi, A.2    Isaac, J.T.3    Collingridge, G.L.4
  • 3
    • 0033555859 scopus 로고    scopus 로고
    • Emergent properties of networks of biological signaling pathways
    • Bhalla, U.S. & Iyengar, R. (1999) Emergent properties of networks of biological signaling pathways. Science, 283, 381-387.
    • (1999) Science , vol.283 , pp. 381-387
    • Bhalla, U.S.1    Iyengar, R.2
  • 4
    • 0027476024 scopus 로고
    • A synaptic model of memory: Long-term potentiation in the hippocampus
    • Bliss, T.V. & Collingridge, G.L. (1993) A synaptic model of memory: long-term potentiation in the hippocampus. Nature, 361, 31-39.
    • (1993) Nature , vol.361 , pp. 31-39
    • Bliss, T.V.1    Collingridge, G.L.2
  • 5
    • 0035940469 scopus 로고    scopus 로고
    • A biophysical model of bidirectional synaptic plasticity: Dependence on AMPA and NMDA receptors
    • Castellani, G.C., Quinlan, E.M., Cooper, L.N. & Shouval, H.Z. (2001) A biophysical model of bidirectional synaptic plasticity: dependence on AMPA and NMDA receptors. Proc. Natl. Acad. Sci. USA, 98, 12,772-12,777.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 12772-712777
    • Castellani, G.C.1    Quinlan, E.M.2    Cooper, L.N.3    Shouval, H.Z.4
  • 6
    • 0035065721 scopus 로고    scopus 로고
    • Is persistent activity of calcium/calmodulin-dependent kinase required for the maintenance of LTP?
    • Chen, H.X., Otmakhov, N., Strack, S., Colbran, R.J. & Lisman, J.E. (2001) Is persistent activity of calcium/calmodulin-dependent kinase required for the maintenance of LTP? J. Neurophysiol., 85, 1368-1376.
    • (2001) J. Neurophysiol. , vol.85 , pp. 1368-1376
    • Chen, H.X.1    Otmakhov, N.2    Strack, S.3    Colbran, R.J.4    Lisman, J.E.5
  • 7
    • 0024397415 scopus 로고
    • The structure and regulation of protein phosphatases
    • Cohen, P. (1989) The structure and regulation of protein phosphatases. Annu. Rev. Biochem., 58, 453-508.
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 453-508
    • Cohen, P.1
  • 9
    • 0028949133 scopus 로고
    • Adenylyl cyclases and the interaction between calcium and cAMP signalling
    • Cooper, D.M., Mons, N. & Karpen, J.W. (1995) Adenylyl cyclases and the interaction between calcium and cAMP signalling. Nature, 374, 421-424.
    • (1995) Nature , vol.374 , pp. 421-424
    • Cooper, D.M.1    Mons, N.2    Karpen, J.W.3
  • 10
    • 0035176112 scopus 로고    scopus 로고
    • Bidirectional synaptic plasticity correlated with the magnitude of dendritic calcium transients above a threshold
    • Cormier, R.J., Greenwood, A.C. & Connor, J.A. (2001) Bidirectional synaptic plasticity correlated with the magnitude of dendritic calcium transients above a threshold. J. Neurophysiol., 85, 399-406.
    • (2001) J. Neurophysiol. , vol.85 , pp. 399-406
    • Cormier, R.J.1    Greenwood, A.C.2    Connor, J.A.3
  • 11
    • 0032588030 scopus 로고    scopus 로고
    • 2+/calmodulin-kinase II enhances channel conductance of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionate type glutamate receptors
    • 2+/calmodulin-kinase II enhances channel conductance of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionate type glutamate receptors. Proc. Natl. Acad. Sci. USA, 96, 3269-3274.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 3269-3274
    • Derkach, V.1    Barria, A.2    Soderling, T.R.3
  • 12
    • 0033639083 scopus 로고    scopus 로고
    • Reinsertion or degradation of AMPA receptors determined by activity-dependent endocytic sorting
    • Ehlers, M.D. (2000) Reinsertion or degradation of AMPA receptors determined by activity-dependent endocytic sorting. Neuron, 28, 511-525.
    • (2000) Neuron , vol.28 , pp. 511-525
    • Ehlers, M.D.1
  • 13
    • 0032527118 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent protein kinase II from hog gastric mucosa using a protein-protein affinity chromatographic technique
    • 2+/calmodulin-dependent protein kinase II from hog gastric mucosa using a protein-protein affinity chromatographic technique. Eur. J. Biochem., 255, 516-525.
    • (1998) Eur. J. Biochem. , vol.255 , pp. 516-525
    • Fahrmann, M.1    Mohlig, M.2    Schatz, H.3    Pfeiffer, A.4
  • 14
    • 0028306195 scopus 로고
    • Dual role of calmodulin in autophosphorylation of multifunctional CaM kinase may underlie decoding of calcium signals
    • Hanson, P.I., Meyer, T., Stryer, L. & Schulman, H. (1994) Dual role of calmodulin in autophosphorylation of multifunctional CaM kinase may underlie decoding of calcium signals. Neuron, 12, 943-956.
    • (1994) Neuron , vol.12 , pp. 943-956
    • Hanson, P.I.1    Meyer, T.2    Stryer, L.3    Schulman, H.4
  • 15
    • 0034708587 scopus 로고    scopus 로고
    • Driving AMPA receptors into synapses by LTP and CaMKII: Requirement for GluR1 and PDZ domain interaction
    • Hayashi, Y., Shi, S.H., Esteban, J.A., Piccini, A., Poncer, J.C. & Malinow, R. (2000) Driving AMPA receptors into synapses by LTP and CaMKII: requirement for GluR1 and PDZ domain interaction. Science, 287, 2262-2267.
    • (2000) Science , vol.287 , pp. 2262-2267
    • Hayashi, Y.1    Shi, S.H.2    Esteban, J.A.3    Piccini, A.4    Poncer, J.C.5    Malinow, R.6
  • 16
    • 0034116677 scopus 로고    scopus 로고
    • Models of calmodulin trapping and CaM kinase II activation in a dendritic spine
    • Holmes, W.R. (2000) Models of calmodulin trapping and CaM kinase II activation in a dendritic spine. J. Comput. Neurosci., 8, 65-85.
    • (2000) J. Comput. Neurosci. , vol.8 , pp. 65-85
    • Holmes, W.R.1
  • 17
    • 0020641117 scopus 로고
    • The protein phosphatases involved in cellular regulation. 6. Measurement of type-1 and type-2 protein phosphatases in extracts of mammalian tissues; an assessment of their physiological roles
    • Ingebritsen, T.S., Stewart, A.A. & Cohen, P. (1983) The protein phosphatases involved in cellular regulation. 6. Measurement of type-1 and type-2 protein phosphatases in extracts of mammalian tissues; an assessment of their physiological roles. Eur. J. Biochem., 132, 297-307.
    • (1983) Eur. J. Biochem. , vol.132 , pp. 297-307
    • Ingebritsen, T.S.1    Stewart, A.A.2    Cohen, P.3
  • 18
    • 0020307706 scopus 로고
    • Quantitative determinations of calmodulin in the supernatant and particulate fractions of mammalian tissues
    • Kakiuchi, S., Yasuda, S., Yamazaki, R., Teshima, Y., Kanda, K., Kakiuchi, R. & Sobue, K. (1982) Quantitative determinations of calmodulin in the supernatant and particulate fractions of mammalian tissues. J. Biochem. (Tokyo), 92, 1041-1048.
    • (1982) J. Biochem. (Tokyo) , vol.92 , pp. 1041-1048
    • Kakiuchi, S.1    Yasuda, S.2    Yamazaki, R.3    Teshima, Y.4    Kanda, K.5    Kakiuchi, R.6    Sobue, K.7
  • 19
    • 0030972388 scopus 로고    scopus 로고
    • Characterization of the interaction between DARPP-32 and protein phosphatase 1 (PP-1): DARPP-32 peptides antagonize the interaction of PP-1 with binding proteins
    • Kwon, Y.G., Huang, H.B., Desdouits, F., Girault, J.A., Greengard, P. & Nairn, A.C. (1997) Characterization of the interaction between DARPP-32 and protein phosphatase 1 (PP-1): DARPP-32 peptides antagonize the interaction of PP-1 with binding proteins. Proc. Natl. Acad. Sci. USA, 94, 3536-3541.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3536-3541
    • Kwon, Y.G.1    Huang, H.B.2    Desdouits, F.3    Girault, J.A.4    Greengard, P.5    Nairn, A.C.6
  • 20
    • 0034702259 scopus 로고    scopus 로고
    • Regulation of distinct AMPA receptor phosphorylation sites during bidirectional synaptic plasticity
    • Lee, H.K., Barbarosie, M., Kameyama, K., Bear, M.F. & Huganir, R.L. (2000) Regulation of distinct AMPA receptor phosphorylation sites during bidirectional synaptic plasticity. Nature, 405, 955-959.
    • (2000) Nature , vol.405 , pp. 955-959
    • Lee, H.K.1    Barbarosie, M.2    Kameyama, K.3    Bear, M.F.4    Huganir, R.L.5
  • 22
    • 0025823438 scopus 로고
    • Calcium binding to calmodulin and its globular domains
    • Linse, S., Helmersson, A. & Forsen, S. (1991) Calcium binding to calmodulin and its globular domains. J. Biol. Chem., 266, 8050-8054.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8050-8054
    • Linse, S.1    Helmersson, A.2    Forsen, S.3
  • 23
    • 0024341227 scopus 로고
    • A mechanism for the Hebb and the anti-Hebb processes underlying learning and memory
    • Lisman, J. (1989) A mechanism for the Hebb and the anti-Hebb processes underlying learning and memory. Proc. Natl. Acad. Sci. USA, 86, 9574-9578.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 9574-9578
    • Lisman, J.1
  • 24
    • 0028031221 scopus 로고
    • The CaM kinase II hypothesis for the storage of synaptic memory
    • Lisman, J. (1994) The CaM kinase II hypothesis for the storage of synaptic memory. Trends Neurosci., 17, 406-412.
    • (1994) Trends Neurosci. , vol.17 , pp. 406-412
    • Lisman, J.1
  • 25
    • 0024043858 scopus 로고
    • 2+/calmodulin-dependent protein kinase molecules of the postsynaptic density
    • 2+/calmodulin-dependent protein kinase molecules of the postsynaptic density. Proc. Natl. Acad. Sci. USA, 85, 5320-5324.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 5320-5324
    • Lisman, J.E.1    Goldring, M.A.2
  • 26
    • 0036513485 scopus 로고    scopus 로고
    • The molecular basis of CaMKII function in synaptic and behavioural memory
    • Lisman, J., Schulman, H. & Cline, H. (2002) The molecular basis of CaMKII function in synaptic and behavioural memory. Nature Rev. Neurosci., 3, 175-190.
    • (2002) Nature Rev. Neurosci. , vol.3 , pp. 175-190
    • Lisman, J.1    Schulman, H.2    Cline, H.3
  • 27
    • 0035797491 scopus 로고    scopus 로고
    • A model of synaptic memory: A CaMKII/PP1 switch that potentiates transmission by organizing an AMPA receptor anchoring assembly
    • Lisman, J.E. & Zhabotinsky, A.M. (2001) A model of synaptic memory: a CaMKII/PP1 switch that potentiates transmission by organizing an AMPA receptor anchoring assembly. Neuron, 31, 191-201.
    • (2001) Neuron , vol.31 , pp. 191-201
    • Lisman, J.E.1    Zhabotinsky, A.M.2
  • 28
    • 0028880861 scopus 로고
    • Calcium/calmodulin-dependent kinase II and long-term potentiation enhance synaptic transmission by the same mechanism
    • Lledo, P.M., Hjelmstad, G.O., Mukherji, S., Soderling, T.R., Malenka, R.C. & Nicoll, R.A. (1995) Calcium/calmodulin-dependent kinase II and long-term potentiation enhance synaptic transmission by the same mechanism. Proc. Natl. Acad. Sci. USA, 92, 11,175-11,179.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 11175-11179
    • Lledo, P.M.1    Hjelmstad, G.O.2    Mukherji, S.3    Soderling, T.R.4    Malenka, R.C.5    Nicoll, R.A.6
  • 29
  • 30
    • 0027941257 scopus 로고
    • Synaptic plasticity in the hippocampus: LTP and LTD
    • Malenka, R.C. (1994) Synaptic plasticity in the hippocampus: LTP and LTD. Cell, 78, 535-538.
    • (1994) Cell , vol.78 , pp. 535-538
    • Malenka, R.C.1
  • 31
    • 0033578855 scopus 로고    scopus 로고
    • Long-term potentiation - A decade of progress?
    • Malenka, R.C. & Nicoll, R.A. (1999) Long-term potentiation - a decade of progress? Science, 285, 1870-1874.
    • (1999) Science , vol.285 , pp. 1870-1874
    • Malenka, R.C.1    Nicoll, R.A.2
  • 33
    • 0026718175 scopus 로고
    • Calmodulin trapping by calcium-calmodulin-dependent protein kinase
    • Meyer, T., Hanson, P.I., Stryer, L. & Schulman, H. (1992) Calmodulin trapping by calcium-calmodulin-dependent protein kinase. Science, 256, 1199-1202.
    • (1992) Science , vol.256 , pp. 1199-1202
    • Meyer, T.1    Hanson, P.I.2    Stryer, L.3    Schulman, H.4
  • 34
    • 0028176087 scopus 로고
    • Involvement of a calcineurin/inhibitor-1 phosphatase cascade in hippocampal long-term depression
    • Mulkey, R.M., Endo, S., Shenolikar, S. & Malenka, R.C. (1994) Involvement of a calcineurin/inhibitor-1 phosphatase cascade in hippocampal long-term depression. Nature, 369, 486-488.
    • (1994) Nature , vol.369 , pp. 486-488
    • Mulkey, R.M.1    Endo, S.2    Shenolikar, S.3    Malenka, R.C.4
  • 36
    • 0036006169 scopus 로고    scopus 로고
    • A fresh look at the role of CaMKII in hippocampal synaptic plasticity and memory
    • Rongo, C. (2002) A fresh look at the role of CaMKII in hippocampal synaptic plasticity and memory. Bioessays, 24, 223-233.
    • (2002) Bioessays , vol.24 , pp. 223-233
    • Rongo, C.1
  • 37
    • 0028222312 scopus 로고
    • Dual calcium ion regulation of calcineurin by calmodulin and calcineurin B
    • Stemmer, P.M. & Klee, C.B. (1994) Dual calcium ion regulation of calcineurin by calmodulin and calcineurin B. Biochemistry, 33, 6859-6866.
    • (1994) Biochemistry , vol.33 , pp. 6859-6866
    • Stemmer, P.M.1    Klee, C.B.2
  • 38
    • 0020540684 scopus 로고
    • 2+/ calmodulin-dependent protein phosphatase (2B) from rabbit skeletal muscle
    • 2+/ calmodulin-dependent protein phosphatase (2B) from rabbit skeletal muscle. Eur. J. Biochem., 132, 289-295.
    • (1983) Eur. J. Biochem. , vol.132 , pp. 289-295
    • Stewart, A.A.1    Ingebritsen, T.S.2    Cohen, P.3
  • 39
    • 0030946102 scopus 로고    scopus 로고
    • Translocation of autophosphorylated calcium/calmodulin-dependent protein kinase II to the postsynaptic density
    • Strack, S., Choi, S., Lovinger, D.M. & Colbran, R.J. (1997) Translocation of autophosphorylated calcium/calmodulin-dependent protein kinase II to the postsynaptic density. J. Biol. Chem., 272, 13,467-13,470.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13467-13470
    • Strack, S.1    Choi, S.2    Lovinger, D.M.3    Colbran, R.J.4
  • 40
    • 0037092436 scopus 로고    scopus 로고
    • Regulation of GluR1 by the A-kinase anchoring protein 79 (AKAP79) signaling complex shares properties with long-term depression
    • Tavalin, S.J., Colledge, M., Hell, J.W., Langeberg, L.K., Huganir, R.L. & Scott, J.D. (2002) Regulation of GluR1 by the A-kinase anchoring protein 79 (AKAP79) signaling complex shares properties with long-term depression. J. Neurosci., 22, 3044-3051.
    • (2002) J. Neurosci. , vol.22 , pp. 3044-3051
    • Tavalin, S.J.1    Colledge, M.2    Hell, J.W.3    Langeberg, L.K.4    Huganir, R.L.5    Scott, J.D.6
  • 41
    • 0035407298 scopus 로고    scopus 로고
    • Roles of serine/threonine phosphatases in hippocampal synaptic plasticity
    • Winder, D.G. & Sweatt, J.D. (2001) Roles of serine/threonine phosphatases in hippocampal synaptic plasticity. Nature Rev. Neurosci., 2, 461-474.
    • (2001) Nature Rev. Neurosci. , vol.2 , pp. 461-474
    • Winder, D.G.1    Sweatt, J.D.2


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