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Volumn 24, Issue 9, 2004, Pages 2304-2312

Phosphorylation of Tau by Fyn: Implications for Alzheimer's Disease

Author keywords

Alzheimer's disease; Fyn; Neurofibrillary tangles; Phosphospecific antibodies; Tau; Tyrosine phosphorylation

Indexed keywords

PROTEIN KINASE FYN; SERINE; TAU PROTEIN; THREONINE;

EID: 12144288564     PISSN: 02706474     EISSN: None     Source Type: Journal    
DOI: 10.1523/JNEUROSCI.4162-03.2004     Document Type: Article
Times cited : (343)

References (54)
  • 1
    • 0033635506 scopus 로고    scopus 로고
    • Alzheimer's disease as a loss of differentiation control in a subset of neurons that retain immature features in the adult brain
    • Arendt T (2000) Alzheimer's disease as a loss of differentiation control in a subset of neurons that retain immature features in the adult brain. Neurobiol Aging 21:783-796.
    • (2000) Neurobiol Aging , vol.21 , pp. 783-796
    • Arendt, T.1
  • 2
    • 0037387147 scopus 로고    scopus 로고
    • A cell surface receptor complex for fibrillar beta-amyloid mediates microglial activation
    • Bamberger ME, Harris ME, McDonald DR, Husemann J, Landreth GE (2003) A cell surface receptor complex for fibrillar beta-amyloid mediates microglial activation. J Neurosci 23:2665-2674.
    • (2003) J Neurosci , vol.23 , pp. 2665-2674
    • Bamberger, M.E.1    Harris, M.E.2    McDonald, D.R.3    Husemann, J.4    Landreth, G.E.5
  • 6
    • 0027406644 scopus 로고
    • Functional organization of microtubule-associated protein tau. Identification of regions which affect microtubule growth, nucleation, and bundle formation in vitro
    • Brandt R, Lee G (1993) Functional organization of microtubule-associated protein tau. Identification of regions which affect microtubule growth, nucleation, and bundle formation in vitro. J Biol Chem 268:3414-3419.
    • (1993) J Biol Chem , vol.268 , pp. 3414-3419
    • Brandt, R.1    Lee, G.2
  • 7
    • 12644260802 scopus 로고    scopus 로고
    • Structural basis of monoclonal antibody Alz50's selectivity for Alzheimer's disease pathology
    • Carmel G, Mager EM, Binder LI, Kuret J (1996) Structural basis of monoclonal antibody Alz50's selectivity for Alzheimer's disease pathology. J Biol Chem 271:32789-32795.
    • (1996) J Biol Chem , vol.271 , pp. 32789-32795
    • Carmel, G.1    Mager, E.M.2    Binder, L.I.3    Kuret, J.4
  • 8
    • 0031964257 scopus 로고    scopus 로고
    • CpG DNA is a potent enhancer of specific immunity in mice immunized with recombinant hepatitis B surface antigen
    • Davis HL, Weeratna R, Waldschmidt TJ, Tygrett L, Schorr J, Krieg AM (1998) CpG DNA is a potent enhancer of specific immunity in mice immunized with recombinant hepatitis B surface antigen. J Immunol 160:870-876.
    • (1998) J Immunol , vol.160 , pp. 870-876
    • Davis, H.L.1    Weeratna, R.2    Waldschmidt, T.J.3    Tygrett, L.4    Schorr, J.5    Krieg, A.M.6
  • 9
    • 0031588018 scopus 로고    scopus 로고
    • Modified phage peptide libraries as a tool to study specificity of phosphorylation and recognition of tyrosine containing peptides
    • Dente L, Vetriani C, Zucconi A, Pelicci G, Lanfrancone L, Pelicci PG, Cesareni G (1997) Modified phage peptide libraries as a tool to study specificity of phosphorylation and recognition of tyrosine containing peptides. J Mol Biol 269:694-703.
    • (1997) J Mol Biol , vol.269 , pp. 694-703
    • Dente, L.1    Vetriani, C.2    Zucconi, A.3    Pelicci, G.4    Lanfrancone, L.5    Pelicci, P.G.6    Cesareni, G.7
  • 10
    • 0026451030 scopus 로고
    • Immunocytochemistry of neurofibrillary tangles with antibodies to subregions of tau protein: Identification of hidden and cleaved tau epitopes and a new phosphorylation site
    • Dickson DW, Ksiezak-Reding H, Liu WK, Davies P, Crowe A, Yen SH (1992) Immunocytochemistry of neurofibrillary tangles with antibodies to subregions of tau protein: identification of hidden and cleaved tau epitopes and a new phosphorylation site. Acta Neuropathol 84:596-605.
    • (1992) Acta Neuropathol , vol.84 , pp. 596-605
    • Dickson, D.W.1    Ksiezak-Reding, H.2    Liu, W.K.3    Davies, P.4    Crowe, A.5    Yen, S.H.6
  • 11
    • 0027534862 scopus 로고
    • Lack of the carboxyl terminal sequence of tau in ghost tangles of Alzheimer's disease
    • Endoh R, Ogawara M, Iwatsubo T, Nakano I, Mori H (1993) Lack of the carboxyl terminal sequence of tau in ghost tangles of Alzheimer's disease. Brain Res 601:164-172.
    • (1993) Brain Res , vol.601 , pp. 164-172
    • Endoh, R.1    Ogawara, M.2    Iwatsubo, T.3    Nakano, I.4    Mori, H.5
  • 12
    • 0038291981 scopus 로고    scopus 로고
    • Conformational changes and truncation of tau protein during tangle evolution in Alzheimer's disease
    • Garcia-Sierra F, Ghoshal N, Quinn B, Berry RW, Binder LI (2003) Conformational changes and truncation of tau protein during tangle evolution in Alzheimer's disease. J Alzheimers Dis 5:65-77.
    • (2003) J Alzheimers Dis , vol.5 , pp. 65-77
    • Garcia-Sierra, F.1    Ghoshal, N.2    Quinn, B.3    Berry, R.W.4    Binder, L.I.5
  • 13
    • 0036434880 scopus 로고    scopus 로고
    • Tau conformational changes correspond to impairments of episodic memory in mild cognitive impairment and Alzheimer's disease
    • Ghoshal N, Garcia-Sierra F, Wuu J, Leurgans S, Bennett DA, Berry RW, Binder LI (2002) Tau conformational changes correspond to impairments of episodic memory in mild cognitive impairment and Alzheimer's disease. Exp Neurol 177:475-493.
    • (2002) Exp Neurol , vol.177 , pp. 475-493
    • Ghoshal, N.1    Garcia-Sierra, F.2    Wuu, J.3    Leurgans, S.4    Bennett, D.A.5    Berry, R.W.6    Binder, L.I.7
  • 15
    • 0037439642 scopus 로고    scopus 로고
    • Aberrant activation of focal adhesion proteins mediates fibrillar amyloid beta-induced neuronal dystrophy
    • Grace EA, Busciglio J (2003) Aberrant activation of focal adhesion proteins mediates fibrillar amyloid beta-induced neuronal dystrophy. J Neurosci 23:493-502.
    • (2003) J Neurosci , vol.23 , pp. 493-502
    • Grace, E.A.1    Busciglio, J.2
  • 16
    • 0027092647 scopus 로고
    • Impaired long-term potentiation, spatial learning, and hippocampal development in fyn mutant mice
    • Grant SG, O'Dell TJ, Karl KA, Stein PL, Soriano P, Kandel ER (1992) Impaired long-term potentiation, spatial learning, and hippocampal development in fyn mutant mice. Science 258:1903-1910.
    • (1992) Science , vol.258 , pp. 1903-1910
    • Grant, S.G.1    O'Dell, T.J.2    Karl, K.A.3    Stein, P.L.4    Soriano, P.5    Kandel, E.R.6
  • 17
    • 0030894830 scopus 로고    scopus 로고
    • Human tau becomes phosphorylated and forms filamentous deposits when overexpressed in lamprey central neurons in situ
    • Hall GF, Yao J, Lee G (1997) Human tau becomes phosphorylated and forms filamentous deposits when overexpressed in lamprey central neurons in situ. Proc Natl Acad Sci USA 94:4733-4738.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 4733-4738
    • Hall, G.F.1    Yao, J.2    Lee, G.3
  • 18
    • 0034762645 scopus 로고    scopus 로고
    • Pictures in molecular medicine: Contemplating Alzheimer's disease as cancer: A loss of cell-cycle control
    • Herrup K, Yang Y (2001) Pictures in molecular medicine: contemplating Alzheimer's disease as cancer: a loss of cell-cycle control. Trends Mol Med 7:527.
    • (2001) Trends Mol Med , vol.7 , pp. 527
    • Herrup, K.1    Yang, Y.2
  • 19
    • 0030783142 scopus 로고    scopus 로고
    • A conformation- and phosphorylation-dependent antibody recognizing the paired helical filaments of Alzheimer's disease
    • Jicha GA, Lane E, Vincent I, Otvos Jr L, Hoffmann R, Davies P (1997) A conformation- and phosphorylation-dependent antibody recognizing the paired helical filaments of Alzheimer's disease. J Neurochem 69:2087-2095.
    • (1997) J Neurochem , vol.69 , pp. 2087-2095
    • Jicha, G.A.1    Lane, E.2    Vincent, I.3    Otvos Jr., L.4    Hoffmann, R.5    Davies, P.6
  • 20
    • 0031025396 scopus 로고    scopus 로고
    • The t protein in human cerebrospinal fluid in Alzheimer's disease consists of proteolytically derived fragments
    • Johnson GVW, Seubert P, Cox TM, Motter R, Brown, JP, Galasko D (1997) The t protein in human cerebrospinal fluid in Alzheimer's disease consists of proteolytically derived fragments. J Neurochem 68:430-433.
    • (1997) J Neurochem , vol.68 , pp. 430-433
    • Johnson, G.V.W.1    Seubert, P.2    Cox, T.M.3    Motter, R.4    Brown, J.P.5    Galasko, D.6
  • 21
    • 0026711059 scopus 로고
    • Fetal-type phosphorylation of the τ in paired helical filaments
    • Kanemaru K, Takio K, Miura R, Titani K, Ihara Y (1992) Fetal-type phosphorylation of the τ in paired helical filaments. J Neurochem 58:1667-1675.
    • (1992) J Neurochem , vol.58 , pp. 1667-1675
    • Kanemaru, K.1    Takio, K.2    Miura, R.3    Titani, K.4    Ihara, Y.5
  • 22
    • 0025775930 scopus 로고
    • Evidence for tau expression in cells of monocyte lineage and its in vitro phosphorylation by v-fms kinase
    • Kim H, Strong TV, Anderson SJ (1991) Evidence for tau expression in cells of monocyte lineage and its in vitro phosphorylation by v-fms kinase. Oncogene 6:1085-1087.
    • (1991) Oncogene , vol.6 , pp. 1085-1087
    • Kim, H.1    Strong, T.V.2    Anderson, S.J.3
  • 23
    • 0036469248 scopus 로고    scopus 로고
    • Process outgrowth of oligodendrocytes is promoted by interaction of fyn kinase with the cytoskeletal protein tau
    • Klein C, Kramer EM, Cardine AM, Schraven B, Brandt R, Trotter J (2002) Process outgrowth of oligodendrocytes is promoted by interaction of fyn kinase with the cytoskeletal protein tau. J Neurosci 22:698-707.
    • (2002) J Neurosci , vol.22 , pp. 698-707
    • Klein, C.1    Kramer, E.M.2    Cardine, A.M.3    Schraven, B.4    Brandt, R.5    Trotter, J.6
  • 24
    • 0028297078 scopus 로고
    • Mass and physical dimensions of two distinct populations of paired helical filaments
    • Ksiezak-Reding H, Wall JS (1994) Mass and physical dimensions of two distinct populations of paired helical filaments. Neurobiol Aging 15:11-19.
    • (1994) Neurobiol Aging , vol.15 , pp. 11-19
    • Ksiezak-Reding, H.1    Wall, J.S.2
  • 26
    • 0026704256 scopus 로고
    • Expression of tau protein in non-neuronal cells: Microtubule binding and stabilization
    • Lee G, Rook SL (1992) Expression of tau protein in non-neuronal cells: microtubule binding and stabilization. J Cell Sci 102:227-237.
    • (1992) J Cell Sci , vol.102 , pp. 227-237
    • Lee, G.1    Rook, S.L.2
  • 27
    • 0024675418 scopus 로고
    • The microtubule binding domain of tau protein
    • Lee G, Neve RL, Kosik KS (1989) The microtubule binding domain of tau protein. Neuron 2:1615-1624.
    • (1989) Neuron , vol.2 , pp. 1615-1624
    • Lee, G.1    Neve, R.L.2    Kosik, K.S.3
  • 29
    • 0029786988 scopus 로고    scopus 로고
    • Knockouts of Src-family kinases: Stiff bones, wimpy T cells, and bad memories
    • Lowell CA, Soriano P (1996) Knockouts of Src-family kinases: stiff bones, wimpy T cells, and bad memories. Genes Dev 10:1845-1857.
    • (1996) Genes Dev , vol.10 , pp. 1845-1857
    • Lowell, C.A.1    Soriano, P.2
  • 30
    • 0037322816 scopus 로고    scopus 로고
    • Proline-directed phosphorylation and isomerization in mitotic regulation and in Alzheimer's disease
    • Lu KP, Liou YC, Vincent I (2003) Proline-directed phosphorylation and isomerization in mitotic regulation and in Alzheimer's disease. Bioessays 25:174-181.
    • (2003) Bioessays , vol.25 , pp. 174-181
    • Lu, K.P.1    Liou, Y.C.2    Vincent, I.3
  • 31
    • 0029837577 scopus 로고    scopus 로고
    • Physiologic levels of β-amyloid activate phosphatidylinositol 3-kinase with the involvement of tyrosine phosphorylation
    • Luo Y, Sunderland T, Wolozin B (1996) Physiologic levels of β-amyloid activate phosphatidylinositol 3-kinase with the involvement of tyrosine phosphorylation. J Neurochem 67:978-987.
    • (1996) J Neurochem , vol.67 , pp. 978-987
    • Luo, Y.1    Sunderland, T.2    Wolozin, B.3
  • 33
    • 0029835019 scopus 로고    scopus 로고
    • A spatial gradient of tau protein phosphorylation in nascent axons
    • Mandell JW, Banker GA (1996) A spatial gradient of tau protein phosphorylation in nascent axons. J Neurosci 16:5727-5740.
    • (1996) J Neurosci , vol.16 , pp. 5727-5740
    • Mandell, J.W.1    Banker, G.A.2
  • 34
    • 0027054568 scopus 로고
    • Nonreceptor protein tyrosine kinases associated with neuronal development
    • Maness PF (1992) Nonreceptor protein tyrosine kinases associated with neuronal development. Dev Neurosci 14:257-270.
    • (1992) Dev Neurosci , vol.14 , pp. 257-270
    • Maness, P.F.1
  • 37
    • 0023505501 scopus 로고
    • Phosphorylation determines two distinct species of Tau in the central nervous system
    • Papasozomenos SC, Binder LI (1987) Phosphorylation determines two distinct species of Tau in the central nervous system. Cell Motil Cytoskel 8:210-226.
    • (1987) Cell Motil Cytoskel , vol.8 , pp. 210-226
    • Papasozomenos, S.C.1    Binder, L.I.2
  • 40
    • 0031587787 scopus 로고    scopus 로고
    • Elevated amyloid β protein (1-40) level induces CREB phosphorylation at serine-133 via p44/42 MAP kinase (Erk1/2)-dependent pathway in rat pheochromocytoma PC12 cells
    • Sato N, Kamino K, Tateishi K, Satoh T, Nishiwaki Y, Yoshiiwa A, Miki T, Ogihara T (1997) Elevated amyloid β protein (1-40) level induces CREB phosphorylation at serine-133 via p44/42 MAP kinase (Erk1/2)-dependent pathway in rat pheochromocytoma PC12 cells. Biochem Biophys Res Commun 232:637-642.
    • (1997) Biochem Biophys Res Commun , vol.232 , pp. 637-642
    • Sato, N.1    Kamino, K.2    Tateishi, K.3    Satoh, T.4    Nishiwaki, Y.5    Yoshiiwa, A.6    Miki, T.7    Ogihara, T.8
  • 41
    • 0037107424 scopus 로고    scopus 로고
    • Tr-kit-induced resumption of the cell cycle in mouse eggs requires activation of a Src-like kinase
    • Sette C, Paronetto MP, Barchi M, Bevilacqua A, Geremia R, Rossi P (2002) Tr-kit-induced resumption of the cell cycle in mouse eggs requires activation of a Src-like kinase. EMBO J 21:5386-5395.
    • (2002) EMBO J , vol.21 , pp. 5386-5395
    • Sette, C.1    Paronetto, M.P.2    Barchi, M.3    Bevilacqua, A.4    Geremia, R.5    Rossi, P.6
  • 42
    • 0026071727 scopus 로고
    • Altered protein tyrosine phosphorylation in Alzheimer's disease
    • Shapiro IP, Masliah E, Saitoh T (1991) Altered protein tyrosine phosphorylation in Alzheimer's disease. J Neurochem 56:1154-1162.
    • (1991) J Neurochem , vol.56 , pp. 1154-1162
    • Shapiro, I.P.1    Masliah, E.2    Saitoh, T.3
  • 43
    • 0027447602 scopus 로고
    • The protein tyrosine kinase, fyn, in Alzheimer's disease pathology
    • Shirazi SK, Wood JG (1993) The protein tyrosine kinase, fyn, in Alzheimer's disease pathology. NeuroReport 4:435-437.
    • (1993) NeuroReport , vol.4 , pp. 435-437
    • Shirazi, S.K.1    Wood, J.G.2
  • 44
    • 0032401602 scopus 로고    scopus 로고
    • Protein LA, a novel hybrid protein with unique single-chain Fv antibody- and Fab-binding properties
    • Svensson HG, Hoogenboom HR, Sjobring U (1998) Protein LA, a novel hybrid protein with unique single-chain Fv antibody- and Fab-binding properties. Eur J Biochem 258:890-896.
    • (1998) Eur J Biochem , vol.258 , pp. 890-896
    • Svensson, H.G.1    Hoogenboom, H.R.2    Sjobring, U.3
  • 45
    • 0036135106 scopus 로고    scopus 로고
    • Morphological and biochemical correlations of abnormal tau filaments in progressive supranuclear palsy
    • Takahashi M, Weidenheim KM, Dickson DW, Ksiezak-Reding H (2002) Morphological and biochemical correlations of abnormal tau filaments in progressive supranuclear palsy. J Neuropathol Exp Neurol 61:33-45.
    • (2002) J Neuropathol Exp Neurol , vol.61 , pp. 33-45
    • Takahashi, M.1    Weidenheim, K.M.2    Dickson, D.W.3    Ksiezak-Reding, H.4
  • 46
    • 0031439247 scopus 로고    scopus 로고
    • Cellular functions regulated by src family kinases
    • Thomas SM, Brugge JS (1997) Cellular functions regulated by src family kinases. Annu Rev Cell Dev Biol 13:513-609.
    • (1997) Annu Rev Cell Dev Biol , vol.13 , pp. 513-609
    • Thomas, S.M.1    Brugge, J.S.2
  • 47
    • 0027361624 scopus 로고
    • Some modular features of temporal cortex in humans as revealed by pathological changes in Alzheimer's disease
    • Van Hoesen GW, Solodkin A (1993) Some modular features of temporal cortex in humans as revealed by pathological changes in Alzheimer's disease. Cereb Cortex 3:465-475.
    • (1993) Cereb Cortex , vol.3 , pp. 465-475
    • Van Hoesen, G.W.1    Solodkin, A.2
  • 50
    • 0026018693 scopus 로고
    • Tyrosine phosphorylation systems in Alzheimer's disease pathology
    • Wood JG, Zinsmeister P (1991) Tyrosine phosphorylation systems in Alzheimer's disease pathology. Neurosci Lett 121:12-16.
    • (1991) Neurosci Lett , vol.121 , pp. 12-16
    • Wood, J.G.1    Zinsmeister, P.2
  • 51
    • 0035871660 scopus 로고    scopus 로고
    • DNA replication precedes neuronal cell death in Alzheimer's disease
    • Yang Y, Geldmacher DS, Herrup K (2001) DNA replication precedes neuronal cell death in Alzheimer's disease. J Neurosci 21:2661-2668.
    • (2001) J Neurosci , vol.21 , pp. 2661-2668
    • Yang, Y.1    Geldmacher, D.S.2    Herrup, K.3
  • 53
    • 0035955702 scopus 로고    scopus 로고
    • Binding of Fyn to MAP-2c through an SH3 binding domain. Regulation of the interaction by ERK2
    • Zamora-Leon SP, Lee G, Davies P, Shafit-Zagardo B (2001) Binding of Fyn to MAP-2c through an SH3 binding domain. Regulation of the interaction by ERK2. J Biol Chem 276:39950-39958.
    • (2001) J Biol Chem , vol.276 , pp. 39950-39958
    • Zamora-Leon, S.P.1    Lee, G.2    Davies, P.3    Shafit-Zagardo, B.4
  • 54
    • 0027988046 scopus 로고
    • Focal adhesion kinase expressed by nerve cell lines shows increased tyrosine phosphorylation in response to Alzheimer's Aβ peptide
    • Zhang C, Lambert MP, Bunch C, Barber K, Wade WS, Krafft GA, Klein WL (1994) Focal adhesion kinase expressed by nerve cell lines shows increased tyrosine phosphorylation in response to Alzheimer's Aβ peptide. J Biol Chem 269:25247-25250.
    • (1994) J Biol Chem , vol.269 , pp. 25247-25250
    • Zhang, C.1    Lambert, M.P.2    Bunch, C.3    Barber, K.4    Wade, W.S.5    Krafft, G.A.6    Klein, W.L.7


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