메뉴 건너뛰기




Volumn 9, Issue 3, 2010, Pages 253-267

"Memory bytes" - Molecular match for CaMKII phosphorylation encoding of microtubule lattices

Author keywords

calmodulin kinase; dendrite; memory; Microtubule; neuron; phosphorylation

Indexed keywords

CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE II; POLYMER; SERINE; THREONINE; TUBULIN;

EID: 78249256322     PISSN: 02196352     EISSN: None     Source Type: Journal    
DOI: 10.1142/S0219635210002482     Document Type: Article
Times cited : (23)

References (51)
  • 1
    • 0034659732 scopus 로고    scopus 로고
    • Postsynaptic scaffolds of excitatory and inhibitory synapses in hippocampal neurons: Maintenance of core components independent of actin filaments and microtubules
    • Allison DW, Chervin AS, Gelfand VI, Craig AM, Postsynaptic scaffolds of excitatory and inhibitory synapses in hippocampal neurons: Maintenance of core components independent of actin filaments and microtubules, J Neurosci 20(12):4545-4554, 2000.
    • (2000) J. Neurosci. , vol.20 , Issue.12 , pp. 4545-4554
    • Allison, D.W.1    Chervin, A.S.2    Gelfand, V.I.3    Craig, A.M.4
  • 2
    • 0037884983 scopus 로고    scopus 로고
    • A prelude to long-term potentiation
    • Andersen P, A prelude to long-term potentiation, Philos Trans R Soc B 358(1432):613-615, 2003.
    • (2003) Philos. Trans. R Soc. B. , vol.358 , Issue.1432 , pp. 613-615
    • Andersen, P.1
  • 3
    • 0035859082 scopus 로고    scopus 로고
    • Interaction with the NMDA receptor locks CaMKII in an active conformation
    • Bayer KU, De Konick P, Leonard AS, Hell JW, Schulman H, Interaction with the NMDA receptor locks CaMKII in an active conformation, Nature 411:801-805, 2001.
    • (2001) Nature , vol.411 , pp. 801-805
    • Bayer, K.U.1    De Konick, P.2    Leonard, A.S.3    Hell, J.W.4    Schulman, H.5
  • 5
    • 0016270990 scopus 로고
    • The possible involvement of brain microtubules in memory fixation
    • Cronly-Dillon J, Carden D, Birks C, The possible involvement of brain microtubules in memory fixation, J Exp Biol 61:443-454, 1974.
    • (1974) J. Exp. Biol. , vol.61 , pp. 443-454
    • Cronly-Dillon, J.1    Carden, D.2    Birks, C.3
  • 6
    • 78249237310 scopus 로고    scopus 로고
    • DeLano Scientific LLC, Palo Alto, CA
    • DeLano W, PyMOL Release 0.99. DeLano Scientific LLC, Palo Alto, CA, 2002.
    • (2002) PyMOL Release 0.99
    • DeLano, W.1
  • 8
    • 39749165656 scopus 로고    scopus 로고
    • Differential regulation of dynein and kinesin motor proteins by tau
    • Dixit R, Ross JL, Goldman YE, Holzbaur EL, Differential regulation of dynein and kinesin motor proteins by tau, Science 319(5866):1086-1089, 2008.
    • (2008) Science , vol.319 , Issue.5866 , pp. 1086-1089
    • Dixit, R.1    Ross, J.L.2    Goldman, Y.E.3    Holzbaur, E.L.4
  • 11
    • 2142648724 scopus 로고    scopus 로고
    • CaMKII, an enzyme on the move: Regulation of temporospatial localization
    • Griffith LC, Lu CS, Sun XX, CaMKII, an enzyme on the move: Regulation of temporospatial localization, Molecular Interventions 3(7):386-403, 2003.
    • (2003) Molecular Interventions , vol.3 , Issue.7 , pp. 386-403
    • Griffith, L.C.1    Lu, C.S.2    Sun, X.X.3
  • 13
    • 0020407788 scopus 로고
    • Information processing in microtubules
    • Hameroff SR, Watt RC, Information processing in microtubules, J Theor Biol 98:549-561, 1982.
    • (1982) J. Theor. Biol. , vol.98 , pp. 549-561
    • Hameroff, S.R.1    Watt, R.C.2
  • 15
    • 0030121458 scopus 로고    scopus 로고
    • Orchestrated reduction of quantum coherence in brain microtubules: A model for consciousness
    • Hameroff S, Penrose R, Orchestrated reduction of quantum coherence in brain microtubules: A model for consciousness, Math Comput Simulat 40:453-480, 1996.
    • (1996) Math. Comput. Simulat , vol.40 , pp. 453-480
    • Hameroff, S.1    Penrose, R.2
  • 16
    • 37549053317 scopus 로고    scopus 로고
    • Locally dynamic synaptic learning rules in pyramidal neuron dendrites
    • Harvey CD, Svoboda K, Locally dynamic synaptic learning rules in pyramidal neuron dendrites, Nature 450:1195-1200, 2007.
    • (2007) Nature , vol.450 , pp. 1195-1200
    • Harvey, C.D.1    Svoboda, K.2
  • 19
    • 0037097022 scopus 로고    scopus 로고
    • 2+/ calmodulindependent protein kinase II
    • 2+/calmodulindependent protein kinase II, Biochem J 364:593-611, 2002.
    • (2002) Biochem. J. , vol.364 , pp. 593-611
    • Hudmon, A.1    Schulman, H.2
  • 20
    • 0026040191 scopus 로고
    • Consensus sequences as substrate specificity determinants for protein kinases and protein phosphatases
    • Kennelly PJ, Krebs EG, Consensus sequences as substrate specificity determinants for protein kinases and protein phosphatases, J Biol Chem 266:15555-15558, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15555-15558
    • Kennelly, P.J.1    Krebs, E.G.2
  • 21
    • 62649108345 scopus 로고    scopus 로고
    • Activation of CaMKII in single dendritic spines during long-term potentiation
    • Lee S-JR, Escobedo-Lozoya Y, Szatmari EM, Yasuda R, Activation of CaMKII in single dendritic spines during long-term potentiation, Nature 458:299-304, 2009.
    • (2009) Nature , vol.458 , pp. 299-304
    • Lee, S.-J.R.1    Escobedo-Lozoya, Y.2    Szatmari, E.M.3    Yasuda, R.4
  • 22
    • 0023839373 scopus 로고
    • Two types of brain calmodulin-dependent protein kinase II: Morphological, biochemical and immunochemical properties
    • Levine H, Sahyoun NE, Two types of brain calmodulin-dependent protein kinase II: Morphological, biochemical and immunochemical properties, Brain Res 439 (1-2): 47-55, 1988.
    • (1988) Brain Res. , vol.439 , Issue.1-2 , pp. 47-55
    • Levine, H.1    Sahyoun, N.E.2
  • 24
    • 0010424768 scopus 로고
    • A mechanism for memory storage insensitive to molecular turnover: A bistable autophosphorylating kinase
    • Lisman JE, A mechanism for memory storage insensitive to molecular turnover: A bistable autophosphorylating kinase, Proc Natl Acad Sci USA 82:3055-3057, 1985.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 3055-3057
    • Lisman, J.E.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.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 5320-5324
    • Lisman, J.E.1    Goldring, M.A.2
  • 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 JE, Zhabotinsky AM, A model of synaptic memory, A CaMKII/PP1 switch that potentiates transmission by organizing an AMPA receptor anchoring assembly, Neuron 31:191-201, 2001.
    • (2001) Neuron , vol.31 , pp. 191-201
    • Lisman, J.E.1    Zhabotinsky, A.M.2
  • 28
    • 0038222588 scopus 로고    scopus 로고
    • The discovery of long-term potentiation
    • Lømo T, The discovery of long-term potentiation, Phil Trans R Soc (Lond) 358:617-620, 2003.
    • (2003) Phil Trans. R Soc. (Lond) , vol.358 , pp. 617-620
    • Lømo, T.1
  • 29
    • 0035834521 scopus 로고    scopus 로고
    • Refined structure of αβ-tubulin at 3.5 Å resolution
    • Löwe J, Li H, Downing KH, Nogales E, Refined structure of αβ-tubulin at 3.5 Å resolution, J Mol Biol 313:1045-1057, 2001.
    • (2001) J. Mol. Biol. , vol.313 , pp. 1045-1057
    • Löwe, J.1    Li, H.2    Downing, K.H.3    Nogales, E.4
  • 30
    • 0022519298 scopus 로고
    • 2+-triggered molecular switch
    • 2+-triggered molecular switch, Cell 44(6):861-870, 1986.
    • (1986) Cell. , vol.44 , Issue.6 , pp. 861-870
    • Miller, S.G.1    Kennedy, M.B.2
  • 31
    • 33646187200 scopus 로고    scopus 로고
    • Unique features of action potential initiation in cortical neurons
    • Naundorf B, Wolf F, Volgushev M, Unique features of action potential initiation in cortical neurons, Nature 440(7087):1060-1063, 2006.
    • (2006) Nature , vol.440 , Issue.7087 , pp. 1060-1063
    • Naundorf, B.1    Wolf, F.2    Volgushev, M.3
  • 32
    • 0032495513 scopus 로고    scopus 로고
    • Structure of the αβ tubulin dimer by electron crystallography
    • Nogales E, Wolf SG, Downing KH, Structure of the αβ tubulin dimer by electron crystallography, Nature 39:199-203, 1998.
    • (1998) Nature , vol.39 , pp. 199-203
    • Nogales, E.1    Wolf, S.G.2    Downing, K.H.3
  • 33
    • 0026355413 scopus 로고
    • Protein kinase phosphorylation site sequences and consensus specificity motifs: Tabulations
    • Pearson RB, Kemp BE, Protein kinase phosphorylation site sequences and consensus specificity motifs: Tabulations, Methods Enzymol 200:62-81, 1991.
    • (1991) Methods Enzymol. , vol.200 , pp. 62-81
    • Pearson, R.B.1    Kemp, B.E.2
  • 36
    • 0000103011 scopus 로고
    • The Croonian lecture: La fine structure des centres nerveux
    • Ramon-y-Cajal SR, The Croonian lecture: La fine structure des centres nerveux, Proc R Soc Lond 55:444-468, 1894.
    • (1894) Proc. R Soc. Lond. , vol.55 , pp. 444-468
    • Ramon-y-Cajal, S.R.1
  • 37
    • 0000176851 scopus 로고
    • Computational connectionism within neurons: A model of cytoskeletal automata subserving neural networks
    • Rasmussen S, Karampurwala H, Vaidyanath R, Jensen KS, Hameroff S, Computational connectionism within neurons: A model of cytoskeletal automata subserving neural networks, Physica D 42:428-449, 1990.
    • (1990) Physica D , vol.42 , pp. 428-449
    • Rasmussen, S.1    Karampurwala, H.2    Vaidyanath, R.3    Jensen, K.S.4    Hameroff, S.5
  • 38
    • 59649091186 scopus 로고    scopus 로고
    • Heterosynaptic molecular dynamics: Locally induced propagating synaptic accumulation of CaM kinase II
    • Rose J, Jin S, Craig A, Heterosynaptic molecular dynamics: Locally induced propagating synaptic accumulation of CaM kinase II, Neuron 61(3):351-358, 2009.
    • (2009) Neuron , vol.61 , Issue.3 , pp. 351-358
    • Rose, J.1    Jin, S.2    Craig, A.3
  • 39
    • 28344445756 scopus 로고    scopus 로고
    • Structure of the autoinhibited kinase domain of CaMKII and SAXS analysis of the holoenzyme
    • Rosenberg OS, Deindl S, Sung RJ, Nairn AC, Kuriyan J, Structure of the autoinhibited kinase domain of CaMKII and SAXS analysis of the holoenzyme, Cell 123:849-860, 2005.
    • (2005) Cell. , vol.123 , pp. 849-860
    • Rosenberg, O.S.1    Deindl, S.2    Sung, R.J.3    Nairn, A.C.4    Kuriyan, J.5
  • 40
    • 0141634366 scopus 로고    scopus 로고
    • The physical basis of microtubule structure and stability
    • Sept D, Baker NA, McCammon JA, The physical basis of microtubule structure and stability, Protein Science 12(10):2257-2261, 2003.
    • (2003) Protein Science , vol.12 , Issue.10 , pp. 2257-2261
    • Sept, D.1    Baker, N.A.2    McCammon, J.A.3
  • 41
    • 0023424860 scopus 로고
    • Tubulin phosphorylation by casein kinase II is similar to that found in vivo
    • Serrano L, Díaz-Nido J, Wandosell E, Avila J, Tubulin phosphorylation by casein kinase II is similar to that found in vivo, J Cell Biol 105:1731-1739, 1987.
    • (1987) J. Cell. Biol. , vol.105 , pp. 1731-1739
    • Serrano, L.1    Díaz-Nido, J.2    Wandosell, E.3    Avila, J.4
  • 42
    • 0032148396 scopus 로고    scopus 로고
    • CaMKII β functions as an f-actin targeting module that localizes CaMKII α/β heterooligomers to dendritic spines
    • Shen K, Teruel MN, Subramanian K, Meyer T, CaMKII β functions as an f-actin targeting module that localizes CaMKII α/β heterooligomers to dendritic spines, Neuron 21:593-606, 1998.
    • (1998) Neuron , vol.21 , pp. 593-606
    • Shen, K.1    Teruel, M.N.2    Subramanian, K.3    Meyer, T.4
  • 43
    • 0033515884 scopus 로고    scopus 로고
    • Dynamic control of CaMKII translocation and localization in hippocampal neurons by NMDA receptor stimulation
    • Shen K, Meyer T, Dynamic control of CaMKII translocation and localization in hippocampal neurons by NMDA receptor stimulation, Science 284:162-167, 1999.
    • (1999) Science , vol.284 , pp. 162-167
    • Shen, K.1    Meyer, T.2
  • 47
    • 0022827893 scopus 로고
    • Phosphorylation of tubulin by a calmodulin-dependent protein kinase
    • Wandosell F, Serrano L, Hernández MA, Avila J, Phosphorylation of tubulin by a calmodulin-dependent protein kinase, J Biol Chem 261:10332-10339, 1986.
    • (1986) J. Biol. Chem. , vol.261 , pp. 10332-10339
    • Wandosell, F.1    Serrano, L.2    Hernández, M.A.3    Avila, J.4
  • 48
    • 0034734813 scopus 로고    scopus 로고
    • 2+/calmodulin- dependent protein kinase II translocated to the postsynaptic density
    • 2+/calmodulin-dependent protein kinase II translocated to the postsynaptic density, Mol Brain Res 81:118-128, 2000.
    • (2000) Mol. Brain Res. , vol.81 , pp. 118-128
    • Yoshimura, Y.1    Aoi, C.2    Yamauchi, T.3
  • 50
    • 50149095303 scopus 로고    scopus 로고
    • Optical induction of plasticity at single synapses reveals input-specific accumulation of α CaMKII
    • Zhang Y-P, Holbro N, Oertner TG, Optical induction of plasticity at single synapses reveals input-specific accumulation of α CaMKII, Proc Natl Acad Sci USA 105(33):12039-12044, 2008.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , Issue.33 , pp. 12039-12044
    • Zhang, Y.-P.1    Holbro, N.2    Oertner, T.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.