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Journal of Cell Biology
Volumn 209, Issue 3, 2015, Pages 419-433
Tau reduction prevents Aβ-induced axonal transport deficits by blocking activation of GSK3β
Author keywords

[No Author keywords available]
Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-42]; AMYLOID PRECURSOR PROTEIN; GLYCOGEN SYNTHASE KINASE 3BETA; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; OLIGOMER; PROTEIN KINASE FYN; TAU PROTEIN; AMYLOID BETA-PROTEIN (1-42); FYN PROTEIN, HUMAN; FYN PROTEIN, MOUSE; GLYCOGEN SYNTHASE KINASE 3; GSK3B PROTEIN, HUMAN; GSK3B PROTEIN, MOUSE; MAPT PROTEIN, HUMAN; MAPT PROTEIN, MOUSE; PEPTIDE FRAGMENT;
EID: 84936998627     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201407065     Document Type: Article
Times cited : (127)
References (94)
  • 1
    • 0037631324 scopus 로고    scopus 로고
    • 14-3-3 connects glycogen synthase kinase-3β to tau within a brain microtubule-associated tau phosphorylation complex
    • Agarwal-Mawal, A., H.Y. Qureshi, P.W. Cafferty, Z. Yuan, D. Han, R. Lin, and H.K. Paudel. 2003. 14-3-3 connects glycogen synthase kinase-3β to tau within a brain microtubule-associated tau phosphorylation complex. J. Biol. Chem. 278:12722-12728. http://dx.doi.org/10.1074/jbc.M211491200.
    • (2003) J. Biol. Chem , vol.278 , pp. 12722-12728
    • Agarwal-Mawal, A.1    Qureshi, H.Y.2    Cafferty, P.W.3    Yuan, Z.4    Han, D.5    Lin, R.6    Paudel, H.K.7
  • 3
    • 0036937699 scopus 로고    scopus 로고
    • Specific tau phosphorylation sites correlate with severity of neuronal cytopathology in Alzheimer's disease
    • Augustinack, J.C., A. Schneider, E.M. Mandelkow, and B.T. Hyman. 2002. Specific tau phosphorylation sites correlate with severity of neuronal cytopathology in Alzheimer's disease. Acta Neuropathol. 103:26-35. http://dx.doi.org/10.1007/s004010100423.
    • (2002) Acta Neuropathol , vol.103 , pp. 26-35
    • Augustinack, J.C.1    Schneider, A.2    Mandelkow, E.M.3    Hyman, B.T.4
  • 5
    • 77957335789 scopus 로고    scopus 로고
    • Stable mossy fiber long-term potentiation requires calcium influx at the granule cell soma, protein synthesis, and microtubuledependent axonal transport
    • Barnes, S.J., T. Opitz, M. Merkens, T. Kelly, C. von der Brelie, R. Krueppel, and H. Beck. 2010. Stable mossy fiber long-term potentiation requires calcium influx at the granule cell soma, protein synthesis, and microtubuledependent axonal transport. J. Neurosci. 30:12996-13004. http://dx.doi.org/10.1523/JNEUROSCI.1847-10.2010.
    • (2010) J. Neurosci , vol.30 , pp. 12996-13004
    • Barnes, S.J.1    Opitz, T.2    Merkens, M.3    Kelly, T.4    von der Brelie, C.5    Krueppel, R.6    Beck, H.7
  • 6
    • 80355123415 scopus 로고    scopus 로고
    • Calcium imaging of cortical neurons using Fura-2 AM
    • Barreto-Chang, O.L., and R.E. Dolmetsch. 2009. Calcium imaging of cortical neurons using Fura-2 AM. J. Vis. Exp. 19:1067. http://dx.doi.org/10.3791/1067.
    • (2009) J. Vis. Exp , vol.19 , pp. 1067
    • Barreto-Chang, O.L.1    Dolmetsch, R.E.2
  • 9
    • 0021718241 scopus 로고
    • Axonal tubulin and axonal microtubules: biochemical evidence for cold stability
    • Brady, S.T., M. Tytell, and R.J. Lasek. 1984. Axonal tubulin and axonal microtubules: biochemical evidence for cold stability. J. Cell Biol. 99:1716-1724. http://dx.doi.org/10.1083/jcb.99.5.1716.
    • (1984) J. Cell Biol , vol.99 , pp. 1716-1724
    • Brady, S.T.1    Tytell, M.2    Lasek, R.J.3
  • 11
    • 79751537405 scopus 로고    scopus 로고
    • Amyloid beta impairs mitochondrial anterograde transport and degenerates synapses in Alzheimer's disease neurons
    • Calkins, M.J., and P.H. Reddy. 2011. Amyloid beta impairs mitochondrial anterograde transport and degenerates synapses in Alzheimer's disease neurons. Biochim. Biophys. Acta. 1812:507-513. http://dx.doi.org/10.1016/j.bbadis.2011.01.007.
    • (2011) Biochim. Biophys. Acta , vol.1812 , pp. 507-513
    • Calkins, M.J.1    Reddy, P.H.2
  • 14
    • 64249133725 scopus 로고    scopus 로고
    • S-nitrosylation of Drp1 mediates β-amyloid-related mitochondrial fission and neuronal injury
    • Cho, D.H., T. Nakamura, J. Fang, P. Cieplak, A. Godzik, Z. Gu, and S.A. Lipton. 2009. S-nitrosylation of Drp1 mediates β-amyloid-related mitochondrial fission and neuronal injury. Science. 324:102-105. http://dx.doi.org/10.1126/science.1171091.
    • (2009) Science , vol.324 , pp. 102-105
    • Cho, D.H.1    Nakamura, T.2    Fang, J.3    Cieplak, P.4    Godzik, A.5    Gu, Z.6    Lipton, S.A.7
  • 17
    • 0035087123 scopus 로고    scopus 로고
    • Selective small-molecule inhibitors of glycogen synthase kinase-3 activity protect primary neurones from death
    • Cross, D.A., A.A. Culbert, K.A. Chalmers, L. Facci, S.D. Skaper, and A.D. Reith. 2001. Selective small-molecule inhibitors of glycogen synthase kinase-3 activity protect primary neurones from death. J. Neurochem. 77:94-102. http://dx.doi.org/10.1046/j.1471-4159.2001.t01-1-00251.x.
    • (2001) J. Neurochem , vol.77 , pp. 94-102
    • Cross, D.A.1    Culbert, A.A.2    Chalmers, K.A.3    Facci, L.4    Skaper, S.D.5    Reith, A.D.6
  • 18
    • 0035067021 scopus 로고    scopus 로고
    • Inhibition of neuronal maturation in primary hippocampal neurons from tau deficient mice
    • Dawson, H.N., A. Ferreira, M.V. Eyster, N. Ghoshal, L.I. Binder, and M.P. Vitek. 2001. Inhibition of neuronal maturation in primary hippocampal neurons from tau deficient mice. J. Cell Sci. 114:1179-1187.
    • (2001) J. Cell Sci , vol.114 , pp. 1179-1187
    • Dawson, H.N.1    Ferreira, A.2    Eyster, M.V.3    Ghoshal, N.4    Binder, L.I.5    Vitek, M.P.6
  • 19
    • 77954466407 scopus 로고    scopus 로고
    • Amyloid-β peptide oligomers disrupt axonal transport through an NMDA receptor-dependent mechanism that is mediated by glycogen synthase kinase 3β in primary cultured hippocampal neurons
    • Decker, H., K.Y. Lo, S.M. Unger, S.T. Ferreira, and M.A. Silverman. 2010. Amyloid-β peptide oligomers disrupt axonal transport through an NMDA receptor-dependent mechanism that is mediated by glycogen synthase kinase 3β in primary cultured hippocampal neurons. J. Neurosci. 30:9166-9171. http://dx.doi.org/10.1523/JNEUROSCI.1074-10.2010.
    • (2010) J. Neurosci , vol.30 , pp. 9166-9171
    • Decker, H.1    Lo, K.Y.2    Unger, S.M.3    Ferreira, S.T.4    Silverman, M.A.5
  • 20
    • 34249672242 scopus 로고    scopus 로고
    • Aβ oligomers induce neuronal oxidative stress through an N-methyl-d-aspartate receptor-dependent mechanism that is blocked by the Alzheimer drug memantine
    • De Felice, F.G., P.T. Velasco, M.P. Lambert, K. Viola, S.J. Fernandez, S.T. Ferreira, and W.L. Klein. 2007. Aβ oligomers induce neuronal oxidative stress through an N-methyl-d-aspartate receptor-dependent mechanism that is blocked by the Alzheimer drug memantine. J. Biol. Chem. 282:11590-11601. http://dx.doi.org/10.1074/jbc.M607483200.
    • (2007) J. Biol. Chem , vol.282 , pp. 11590-11601
    • De Felice, F.G.1    Velasco, P.T.2    Lambert, M.P.3    Viola, K.4    Fernandez, S.J.5    Ferreira, S.T.6    Klein, W.L.7
  • 22
    • 84865352799 scopus 로고    scopus 로고
    • Tau promotes neurodegeneration via DRP1 mislocalization in vivo
    • DuBoff, B., J. Götz, and M.B. Feany. 2012. Tau promotes neurodegeneration via DRP1 mislocalization in vivo. Neuron. 75:618-632. http://dx.doi.org/10.1016/j.neuron.2012.06.026.
    • (2012) Neuron , vol.75 , pp. 618-632
    • DuBoff, B.1    Götz, J.2    Feany, M.B.3
  • 24
    • 71049158071 scopus 로고    scopus 로고
    • The proline-rich domain of tau plays a role in interactions with actin
    • He, H.J., X.S. Wang, R. Pan, D.L. Wang, M.N. Liu, and R.Q. He. 2009. The proline-rich domain of tau plays a role in interactions with actin. BMC Cell Biol. 10:81. http://dx.doi.org/10.1186/1471-2121-10-81.
    • (2009) BMC Cell Biol , vol.10 , pp. 81
    • He, H.J.1    Wang, X.S.2    Pan, R.3    Wang, D.L.4    Liu, M.N.5    He, R.Q.6
  • 25
    • 0141864562 scopus 로고    scopus 로고
    • Glutamate and amyloid β-protein rapidly inhibit fast axonal transport in cultured rat hippocampal neurons by different mechanisms
    • Hiruma, H., T. Katakura, S. Takahashi, T. Ichikawa, and T. Kawakami. 2003. Glutamate and amyloid β-protein rapidly inhibit fast axonal transport in cultured rat hippocampal neurons by different mechanisms. J. Neurosci. 23:8967-8977.
    • (2003) J. Neurosci , vol.23 , pp. 8967-8977
    • Hiruma, H.1    Katakura, T.2    Takahashi, S.3    Ichikawa, T.4    Kawakami, T.5
  • 26
    • 84872729419 scopus 로고    scopus 로고
    • Tau loss attenuates neuronal network hyperexcitability in mouse and Drosophila genetic models of epilepsy
    • Holth, J.K., V.C. Bomben, J.G. Reed, T. Inoue, L. Younkin, S.G. Younkin, R.G. Pautler, J. Botas, and J.L. Noebels. 2013. Tau loss attenuates neuronal network hyperexcitability in mouse and Drosophila genetic models of epilepsy. J. Neurosci. 33:1651-1659. http://dx.doi.org/10.1523/JNEUROSCI.3191-12.2013.
    • (2013) J. Neurosci , vol.33 , pp. 1651-1659
    • Holth, J.K.1    Bomben, V.C.2    Reed, J.G.3    Inoue, T.4    Younkin, L.5    Younkin, S.G.6    Pautler, R.G.7    Botas, J.8    Noebels, J.L.9
  • 27
    • 57349172663 scopus 로고    scopus 로고
    • Parkinsonism and impaired axonal transport in a mouse model of frontotemporal dementia
    • Ittner, L.M., T. Fath, Y.D. Ke, M. Bi, J. van Eersel, K.M. Li, P. Gunning, and J. Götz. 2008. Parkinsonism and impaired axonal transport in a mouse model of frontotemporal dementia. Proc. Natl. Acad. Sci. USA. 105:15997-16002. http://dx.doi.org/10.1073/pnas.0808084105.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 15997-16002
    • Ittner, L.M.1    Fath, T.2    Ke, Y.D.3    Bi, M.4    van Eersel, J.5    Li, K.M.6    Gunning, P.7    Götz, J.8
  • 29
    • 79955044494 scopus 로고    scopus 로고
    • Soluble amyloid β-protein dimers isolated from Alzheimer cortex directly induce Tau hyperphosphorylation and neuritic degeneration
    • Jin, M., N. Shepardson, T. Yang, G. Chen, D. Walsh, and D.J. Selkoe. 2011. Soluble amyloid β-protein dimers isolated from Alzheimer cortex directly induce Tau hyperphosphorylation and neuritic degeneration. Proc. Natl. Acad. Sci. USA. 108:5819-5824. http://dx.doi.org/10.1073/pnas.1017033108.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 5819-5824
    • Jin, M.1    Shepardson, N.2    Yang, T.3    Chen, G.4    Walsh, D.5    Selkoe, D.J.6
  • 32
    • 79960032374 scopus 로고    scopus 로고
    • Pathogenic forms of tau inhibit kinesin-dependent axonal transport through a mechanism involving activation of axonal phosphotransferases
    • Kanaan, N.M., G.A. Morfini, N.E. LaPointe, G.F. Pigino, K.R. Patterson, Y. Song, A. Andreadis, Y. Fu, S.T. Brady, and L.I. Binder. 2011. Pathogenic forms of tau inhibit kinesin-dependent axonal transport through a mechanism involving activation of axonal phosphotransferases. J. Neurosci. 31:9858-9868. http://dx.doi.org/10.1523/JNEUROSCI.0560-11.2011.
    • (2011) J. Neurosci , vol.31 , pp. 9858-9868
    • Kanaan, N.M.1    Morfini, G.A.2    LaPointe, N.E.3    Pigino, G.F.4    Patterson, K.R.5    Song, Y.6    Andreadis, A.7    Fu, Y.8    Brady, S.T.9    Binder, L.I.10
  • 34
    • 33748792254 scopus 로고    scopus 로고
    • β-Amyloid-induced dynamin 1 degradation is mediated by N-methyl-d-aspartate receptors in hippocampal neurons
    • Kelly, B.L., and A. Ferreira. 2006. β-Amyloid-induced dynamin 1 degradation is mediated by N-methyl-d-aspartate receptors in hippocampal neurons. J. Biol. Chem. 281:28079-28089. http://dx.doi.org/10.1074/jbc.M605081200.
    • (2006) J. Biol. Chem , vol.281 , pp. 28079-28089
    • Kelly, B.L.1    Ferreira, A.2
  • 35
    • 84874629526 scopus 로고    scopus 로고
    • Metabotropic NMDA receptor function is required for β-amyloid-induced synaptic depression
    • Kessels, H.W., S. Nabavi, and R. Malinow. 2013. Metabotropic NMDA receptor function is required for β-amyloid-induced synaptic depression. Proc. Natl. Acad. Sci. USA. 110:4033-4038. http://dx.doi.org/10.1073/pnas.1219605110.
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 4033-4038
    • Kessels, H.W.1    Nabavi, S.2    Malinow, R.3
  • 37
    • 33751218015 scopus 로고    scopus 로고
    • Tau-dependent microtubule disassembly initiated by prefibrillar β-amyloid
    • King, M.E., H.M. Kan, P.W. Baas, A. Erisir, C.G. Glabe, and G.S. Bloom. 2006. Tau-dependent microtubule disassembly initiated by prefibrillar β-amyloid. J. Cell Biol. 175:541-546. http://dx.doi.org/10.1083/jcb.200605187.
    • (2006) J. Cell Biol , vol.175 , pp. 541-546
    • King, M.E.1    Kan, H.M.2    Baas, P.W.3    Erisir, A.4    Glabe, C.G.5    Bloom, G.S.6
  • 39
    • 62849088641 scopus 로고    scopus 로고
    • The amino terminus of tau inhibits kinesin-dependent axonal transport: implications for filament toxicity
    • LaPointe, N.E., G. Morfini, G. Pigino, I.N. Gaisina, A.P. Kozikowski, L.I. Binder, and S.T. Brady. 2009. The amino terminus of tau inhibits kinesin-dependent axonal transport: implications for filament toxicity. J. Neurosci. Res. 87:440-451. http://dx.doi.org/10.1002/jnr.21850.
    • (2009) J. Neurosci. Res , vol.87 , pp. 440-451
    • LaPointe, N.E.1    Morfini, G.2    Pigino, G.3    Gaisina, I.N.4    Kozikowski, A.P.5    Binder, L.I.6    Brady, S.T.7
  • 40
    • 63649101642 scopus 로고    scopus 로고
    • Neuronal depolarization modifies motor protein mobility
    • Lardong, K., C. Maas, and M. Kneussel. 2009. Neuronal depolarization modifies motor protein mobility. Neuroscience. 160:1-5. http://dx.doi.org/10.1016/j.neuroscience.2009.02.034.
    • (2009) Neuroscience , vol.160 , pp. 1-5
    • Lardong, K.1    Maas, C.2    Kneussel, M.3
  • 41
    • 0344505849 scopus 로고    scopus 로고
    • Tau interacts with src-family non-receptor tyrosine kinases
    • Lee, G., S.T. Newman, D.L. Gard, H. Band, and G. Panchamoorthy. 1998. Tau interacts with src-family non-receptor tyrosine kinases. J. Cell Sci. 111:3167-3177.
    • (1998) J. Cell Sci , vol.111 , pp. 3167-3177
    • Lee, G.1    Newman, S.T.2    Gard, D.L.3    Band, H.4    Panchamoorthy, G.5
  • 44
    • 77953524779 scopus 로고    scopus 로고
    • Tau potentiates nerve growth factor-induced mitogen-activated protein kinase signaling and neurite initiation without a requirement for microtubule binding
    • Leugers, C.J., and G. Lee. 2010. Tau potentiates nerve growth factor-induced mitogen-activated protein kinase signaling and neurite initiation without a requirement for microtubule binding. J. Biol. Chem. 285:19125-19134. http://dx.doi.org/10.1074/jbc.M110.105387.
    • (2010) J. Biol. Chem , vol.285 , pp. 19125-19134
    • Leugers, C.J.1    Lee, G.2
  • 45
    • 67249087641 scopus 로고    scopus 로고
    • Soluble oligomers of amyloid β protein facilitate hippocampal long-term depression by disrupting neuronal glutamate uptake
    • Li, S., S. Hong, N.E. Shepardson, D.M. Walsh, G.M. Shankar, and D. Selkoe. 2009. Soluble oligomers of amyloid β protein facilitate hippocampal long-term depression by disrupting neuronal glutamate uptake. Neuron. 62:788-801. http://dx.doi.org/10.1016/j.neuron.2009.05.012.
    • (2009) Neuron , vol.62 , pp. 788-801
    • Li, S.1    Hong, S.2    Shepardson, N.E.3    Walsh, D.M.4    Shankar, G.M.5    Selkoe, D.6
  • 46
    • 0036468677 scopus 로고    scopus 로고
    • Germline transmission and tissue-specific expression of transgenes delivered by lentiviral vectors
    • Lois, C., E.J. Hong, S. Pease, E.J. Brown, and D. Baltimore. 2002. Germline transmission and tissue-specific expression of transgenes delivered by lentiviral vectors. Science. 295:868-872. http://dx.doi.org/10.1126/science.1067081.
    • (2002) Science , vol.295 , pp. 868-872
    • Lois, C.1    Hong, E.J.2    Pease, S.3    Brown, E.J.4    Baltimore, D.5
  • 48
    • 73949100672 scopus 로고    scopus 로고
    • Deletion of tau attenuates heat shock-induced injury in cultured cortical neurons
    • Miao, Y., J. Chen, Q. Zhang, and A. Sun. 2010. Deletion of tau attenuates heat shock-induced injury in cultured cortical neurons. J. Neurosci. Res. 88:102-110. http://dx.doi.org/10.1002/jnr.22188.
    • (2010) J. Neurosci. Res , vol.88 , pp. 102-110
    • Miao, Y.1    Chen, J.2    Zhang, Q.3    Sun, A.4
  • 49
    • 0036469290 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3 phosphorylates kinesin light chains and negatively regulates kinesin-based motility
    • Morfini, G., G. Szebenyi, R. Elluru, N. Ratner, and S.T. Brady. 2002. Glycogen synthase kinase 3 phosphorylates kinesin light chains and negatively regulates kinesin-based motility. EMBO J. 21:281-293. http://dx.doi.org/10.1093/emboj/21.3.281.
    • (2002) EMBO J , vol.21 , pp. 281-293
    • Morfini, G.1    Szebenyi, G.2    Elluru, R.3    Ratner, N.4    Brady, S.T.5
  • 50
    • 79955670132 scopus 로고    scopus 로고
    • The many faces of tau
    • Morris, M., S. Maeda, K. Vossel, and L. Mucke. 2011. The many faces of tau. Neuron. 70:410-426. http://dx.doi.org/10.1016/j.neuron.2011.04.009.
    • (2011) Neuron , vol.70 , pp. 410-426
    • Morris, M.1    Maeda, S.2    Vossel, K.3    Mucke, L.4
  • 51
    • 84875275094 scopus 로고    scopus 로고
    • Age-appropriate cognition and subtle dopamine-independent motor deficits in aged tau knockout mice
    • Morris, M., P. Hamto, A. Adame, N. Devidze, E. Masliah, and L. Mucke. 2013. Age-appropriate cognition and subtle dopamine-independent motor deficits in aged tau knockout mice. Neurobiol. Aging. 34:1523-1529. http://dx.doi.org/10.1016/j.neurobiolaging.2012.12.003.
    • (2013) Neurobiol. Aging , vol.34 , pp. 1523-1529
    • Morris, M.1    Hamto, P.2    Adame, A.3    Devidze, N.4    Masliah, E.5    Mucke, L.6
  • 53
    • 0037006018 scopus 로고    scopus 로고
    • Involvement of microtubule integrity in memory impairment caused by colchicine
    • Nakayama, T., and T. Sawada. 2002. Involvement of microtubule integrity in memory impairment caused by colchicine. Pharmacol. Biochem. Behav. 71:119-138. http://dx.doi.org/10.1016/S0091-3057(01)00634-7.
    • (2002) Pharmacol. Biochem. Behav , vol.71 , pp. 119-138
    • Nakayama, T.1    Sawada, T.2
  • 57
    • 69949172894 scopus 로고    scopus 로고
    • Physiological transgene regulation and functional complementation of a neurological disease gene deficiency in neurons
    • Peruzzi, P.P., S.E. Lawler, S.L. Senior, N. Dmitrieva, P.A. Edser, D. Gianni, E.A. Chiocca, and R. Wade-Martins. 2009. Physiological transgene regulation and functional complementation of a neurological disease gene deficiency in neurons. Mol. Ther. 17:1517-1526. http://dx.doi.org/10.1038/mt.2009.64.
    • (2009) Mol. Ther , vol.17 , pp. 1517-1526
    • Peruzzi, P.P.1    Lawler, S.E.2    Senior, S.L.3    Dmitrieva, N.4    Edser, P.A.5    Gianni, D.6    Chiocca, E.A.7    Wade-Martins, R.8
  • 58
    • 0030913980 scopus 로고    scopus 로고
    • The 'jaws' model of tau-microtubule interaction examined in CHO cells
    • Preuss, U., J. Biernat, E.M. Mandelkow, and E. Mandelkow. 1997. The 'jaws' model of tau-microtubule interaction examined in CHO cells. J. Cell Sci. 110:789-800.
    • (1997) J. Cell Sci , vol.110 , pp. 789-800
    • Preuss, U.1    Biernat, J.2    Mandelkow, E.M.3    Mandelkow, E.4
  • 59
    • 84882773635 scopus 로고    scopus 로고
    • Amyloid-β oligomers induce tau-independent disruption of BDNF axonal transport via calcineurin activation in cultured hippocampal neurons
    • Ramser, E.M., K.J. Gan, H. Decker, E.Y. Fan, M.M. Suzuki, S.T. Ferreira, and M.A. Silverman. 2013. Amyloid-β oligomers induce tau-independent disruption of BDNF axonal transport via calcineurin activation in cultured hippocampal neurons. Mol. Biol. Cell. 24:2494-2505. http://dx.doi.org/10.1091/mbc.E12-12-0858.
    • (2013) Mol. Biol. Cell , vol.24 , pp. 2494-2505
    • Ramser, E.M.1    Gan, K.J.2    Decker, H.3    Fan, E.Y.4    Suzuki, M.M.5    Ferreira, S.T.6    Silverman, M.A.7
  • 61
    • 77953658771 scopus 로고    scopus 로고
    • Deleterious effects of amyloid β oligomers acting as an extracellular scaffold for mGluR5
    • Renner, M., P.N. Lacor, P.T. Velasco, J. Xu, A. Contractor, W.L. Klein, and A. Triller. 2010. Deleterious effects of amyloid β oligomers acting as an extracellular scaffold for mGluR5. Neuron. 66:739-754. http://dx.doi.org/10.1016/j.neuron.2010.04.029.
    • (2010) Neuron , vol.66 , pp. 739-754
    • Renner, M.1    Lacor, P.N.2    Velasco, P.T.3    Xu, J.4    Contractor, A.5    Klein, W.L.6    Triller, A.7
  • 62
    • 49649119504 scopus 로고    scopus 로고
    • Phosphorylation regulates tau interactions with Src homology 3 domains of phosphatidylinositol 3-kinase, phospholipase Cγ1, Grb2, and Src family kinases
    • Reynolds, C.H., C.J. Garwood, S. Wray, C. Price, S. Kellie, T. Perera, M. Zvelebil, A. Yang, P.W. Sheppard, I.M. Varndell, et al. 2008. Phosphorylation regulates tau interactions with Src homology 3 domains of phosphatidylinositol 3-kinase, phospholipase Cγ1, Grb2, and Src family kinases. J. Biol. Chem. 283:18177-18186. http://dx.doi.org/10.1074/jbc.M709715200.
    • (2008) J. Biol. Chem , vol.283 , pp. 18177-18186
    • Reynolds, C.H.1    Garwood, C.J.2    Wray, S.3    Price, C.4    Kellie, S.5    Perera, T.6    Zvelebil, M.7    Yang, A.8    Sheppard, P.W.9    Varndell, I.M.10
  • 63
    • 34248181511 scopus 로고    scopus 로고
    • Reducing endogenous tau ameliorates amyloid β-induced deficits in an Alzheimer's disease mouse model
    • Roberson, E.D., K. Scearce-Levie, J.J. Palop, F. Yan, I.H. Cheng, T. Wu, H. Gerstein, G.-Q. Yu, and L. Mucke. 2007. Reducing endogenous tau ameliorates amyloid β-induced deficits in an Alzheimer's disease mouse model. Science. 316:750-754. http://dx.doi.org/10.1126/science.1141736.
    • (2007) Science , vol.316 , pp. 750-754
    • Roberson, E.D.1    Scearce-Levie, K.2    Palop, J.J.3    Yan, F.4    Cheng, I.H.5    Wu, T.6    Gerstein, H.7    Yu, G.-Q.8    Mucke, L.9
  • 64
    • 78651506630 scopus 로고    scopus 로고
    • Amyloid-β/Fyn-induced synaptic, network, and cognitive impairments depend on tau levels in multiple mouse models of Alzheimer's disease
    • Roberson, E.D., B. Halabisky, J.W. Yoo, J. Yao, J. Chin, F. Yan, T. Wu, P. Hamto, N. Devidze, G.-Q. Yu, et al. 2011. Amyloid-β/Fyn-induced synaptic, network, and cognitive impairments depend on tau levels in multiple mouse models of Alzheimer's disease. J. Neurosci. 31:700-711. http://dx.doi.org/10.1523/JNEUROSCI.4152-10.2011.
    • (2011) J. Neurosci , vol.31 , pp. 700-711
    • Roberson, E.D.1    Halabisky, B.2    Yoo, J.W.3    Yao, J.4    Chin, J.5    Yan, F.6    Wu, T.7    Hamto, P.8    Devidze, N.9    Yu, G.-Q.10
  • 65
    • 33749854516 scopus 로고    scopus 로고
    • Acute impairment of mitochondrial trafficking by β-amyloid peptides in hippocampal neurons
    • Rui, Y., P. Tiwari, Z. Xie, and J.Q. Zheng. 2006. Acute impairment of mitochondrial trafficking by β-amyloid peptides in hippocampal neurons. J. Neurosci. 26:10480-10487. http://dx.doi.org/10.1523/JNEUROSCI.3231-06.2006.
    • (2006) J. Neurosci , vol.26 , pp. 10480-10487
    • Rui, Y.1    Tiwari, P.2    Xie, Z.3    Zheng, J.Q.4
  • 67
    • 84859230759 scopus 로고    scopus 로고
    • Tau's role in the developing brain: implications for intellectual disability
    • Sapir, T., M. Frotscher, T. Levy, E.M. Mandelkow, and O. Reiner. 2012. Tau's role in the developing brain: implications for intellectual disability. Hum. Mol. Genet. 21:1681-1692. http://dx.doi.org/10.1093/hmg/ddr603.
    • (2012) Hum. Mol. Genet , vol.21 , pp. 1681-1692
    • Sapir, T.1    Frotscher, M.2    Levy, T.3    Mandelkow, E.M.4    Reiner, O.5
  • 68
    • 84877879701 scopus 로고    scopus 로고
    • Amyloid-β signals through tau to drive ectopic neuronal cell cycle re-entry in Alzheimer's disease
    • Seward, M.E., E. Swanson, A. Norambuena, A. Reimann, J.N. Cochran, R. Li, E.D. Roberson, and G.S. Bloom. 2013. Amyloid-β signals through tau to drive ectopic neuronal cell cycle re-entry in Alzheimer's disease. J. Cell Sci. 126:1278-1286. http://dx.doi.org/10.1242/jcs.1125880.
    • (2013) J. Cell Sci , vol.126 , pp. 1278-1286
    • Seward, M.E.1    Swanson, E.2    Norambuena, A.3    Reimann, A.4    Cochran, J.N.5    Li, R.6    Roberson, E.D.7    Bloom, G.S.8
  • 69
    • 84857073309 scopus 로고    scopus 로고
    • Regulation of mitochondrial transport and inter-microtubule spacing by tau phosphorylation at the sites hyperphosphorylated in Alzheimer's disease
    • Shahpasand, K., I. Uemura, T. Saito, T. Asano, K. Hata, K. Shibata, Y. Toyoshima, M. Hasegawa, and S. Hisanaga. 2012. Regulation of mitochondrial transport and inter-microtubule spacing by tau phosphorylation at the sites hyperphosphorylated in Alzheimer's disease. J. Neurosci. 32:2430-2441. http://dx.doi.org/10.1523/JNEUROSCI.5927-11.2012.
    • (2012) J. Neurosci , vol.32 , pp. 2430-2441
    • Shahpasand, K.1    Uemura, I.2    Saito, T.3    Asano, T.4    Hata, K.5    Shibata, K.6    Toyoshima, Y.7    Hasegawa, M.8    Hisanaga, S.9
  • 71
    • 0027212769 scopus 로고
    • Identification and transport of full-length amyloid precursor proteins in rat peripheral nervous system
    • Sisodia, S.S., E.H. Koo, P.N. Hoffman, G. Perry, and D.L. Price. 1993. Identification and transport of full-length amyloid precursor proteins in rat peripheral nervous system. J. Neurosci. 13:3136-3142.
    • (1993) J. Neurosci , vol.13 , pp. 3136-3142
    • Sisodia, S.S.1    Koo, E.H.2    Hoffman, P.N.3    Perry, G.4    Price, D.L.5
  • 74
    • 84876089948 scopus 로고    scopus 로고
    • Transglutaminase and polyamination of tubulin: posttranslational modification for stabilizing axonal microtubules
    • Song, Y., L.L. Kirkpatrick, A.B. Schilling, D.L. Helseth, N. Chabot, J.W. Keillor, G.V. Johnson, and S.T. Brady. 2013. Transglutaminase and polyamination of tubulin: posttranslational modification for stabilizing axonal microtubules. Neuron. 78:109-123. http://dx.doi.org/10.1016/j.neuron.2013.01.036.
    • (2013) Neuron , vol.78 , pp. 109-123
    • Song, Y.1    Kirkpatrick, L.L.2    Schilling, A.B.3    Helseth, D.L.4    Chabot, N.5    Keillor, J.W.6    Johnson, G.V.7    Brady, S.T.8
  • 76
  • 77
    • 0027515127 scopus 로고
    • Inactivation of glycogen synthase kinase-3β by phosphorylation: new kinase connections in insulin and growth-factor signalling
    • Sutherland, C., I.A. Leighton, and P. Cohen. 1993. Inactivation of glycogen synthase kinase-3β by phosphorylation: new kinase connections in insulin and growth-factor signalling. Biochem. J. 296:15-19.
    • (1993) Biochem. J , vol.296 , pp. 15-19
    • Sutherland, C.1    Leighton, I.A.2    Cohen, P.3
  • 78
    • 0030044463 scopus 로고    scopus 로고
    • Exposure of rat hippocampal neurons to amyloid β peptide (25-35) induces the inactivation of phosphatidyl inositol-3 kinase and the activation of tau protein kinase I/glycogen synthase kinase-3β
    • Takashima, A., K. Noguchi, G. Michel, M. Mercken, M. Hoshi, K. Ishiguro, and K. Imahori. 1996. Exposure of rat hippocampal neurons to amyloid β peptide (25-35) induces the inactivation of phosphatidyl inositol-3 kinase and the activation of tau protein kinase I/glycogen synthase kinase-3β. Neurosci. Lett. 203:33-36. http://dx.doi.org/10.1016/0304-3940(95)12257-5.
    • (1996) Neurosci. Lett , vol.203 , pp. 33-36
    • Takashima, A.1    Noguchi, K.2    Michel, G.3    Mercken, M.4    Hoshi, M.5    Ishiguro, K.6    Imahori, K.7
  • 80
    • 84859577721 scopus 로고    scopus 로고
    • Early and selective impairments in axonal transport kinetics of synaptic cargoes induced by soluble amyloid β-protein oligomers
    • Tang, Y., D.A. Scott, U. Das, S.D. Edland, K. Radomski, E.H. Koo, and S. Roy. 2012. Early and selective impairments in axonal transport kinetics of synaptic cargoes induced by soluble amyloid β-protein oligomers. Traffic. 13:681-693. http://dx.doi.org/10.1111/j.1600-0854.2012.01340.x.
    • (2012) Traffic , vol.13 , pp. 681-693
    • Tang, Y.1    Scott, D.A.2    Das, U.3    Edland, S.D.4    Radomski, K.5    Koo, E.H.6    Roy, S.7
  • 82
    • 83655192092 scopus 로고    scopus 로고
    • Regulation of NMDA receptors by the tyrosine kinase Fyn
    • Trepanier, C.H., M.F. Jackson, and J.F. MacDonald. 2012. Regulation of NMDA receptors by the tyrosine kinase Fyn. FEBS J. 279:12-19. http://dx.doi.org/10.1111/j.1742-4658.2011.08391.x.
    • (2012) FEBS J , vol.279 , pp. 12-19
    • Trepanier, C.H.1    Jackson, M.F.2    MacDonald, J.F.3
  • 84
    • 84868587734 scopus 로고    scopus 로고
    • Decreased axonal transport rates in the Tg2576 APP transgenic mouse: improvement with the γ-secretase inhibitor MRK-560 as detected by manganeseenhanced MRI
    • Wang, F.H., P. Appelkvist, T. Klason, O. Gissberg, A. Bogstedt, K. Eliason, S. Martinsson, S. Briem, A. Andersson, S.A. Visser, et al. 2012. Decreased axonal transport rates in the Tg2576 APP transgenic mouse: improvement with the γ-secretase inhibitor MRK-560 as detected by manganeseenhanced MRI. Eur. J. Neurosci. 36:3165-3172. http://dx.doi.org/10.1111/j.1460-9568.2012.08258.x.
    • (2012) Eur. J. Neurosci , vol.36 , pp. 3165-3172
    • Wang, F.H.1    Appelkvist, P.2    Klason, T.3    Gissberg, O.4    Bogstedt, A.5    Eliason, K.6    Martinsson, S.7    Briem, S.8    Andersson, A.9    Visser, S.A.10
  • 85
    • 58149091896 scopus 로고    scopus 로고
    • 2+-dependent regulation of kinesin-mediated mitochondrial motility
    • 2+-dependent regulation of kinesin-mediated mitochondrial motility. Cell. 136:163-174. http://dx.doi.org/10.1016/j.cell.2008.11.046.
    • (2009) Cell , vol.136 , pp. 163-174
    • Wang, X.1    Schwarz, T.L.2
  • 86
    • 58049218922 scopus 로고    scopus 로고
    • Amyloid-β overproduction causes abnormal mitochondrial dynamics via differential modulation of mitochondrial fission/fusion proteins
    • Wang, X., B. Su, S.L. Siedlak, P.I. Moreira, H. Fujioka, Y. Wang, G. Casadesus, and X. Zhu. 2008. Amyloid-β overproduction causes abnormal mitochondrial dynamics via differential modulation of mitochondrial fission/fusion proteins. Proc. Natl. Acad. Sci. USA. 105:19318-19323. http://dx.doi.org/10.1073/pnas.0804871105.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 19318-19323
    • Wang, X.1    Su, B.2    Siedlak, S.L.3    Moreira, P.I.4    Fujioka, H.5    Wang, Y.6    Casadesus, G.7    Zhu, X.8
  • 87
    • 67650732998 scopus 로고    scopus 로고
    • Impaired balance of mitochondrial fission and fusion in Alzheimer's disease
    • Wang, X., B. Su, H.G. Lee, X. Li, G. Perry, M.A. Smith, and X. Zhu. 2009. Impaired balance of mitochondrial fission and fusion in Alzheimer's disease. J. Neurosci. 29:9090-9103. http://dx.doi.org/10.1523/JNEUROSCI.1357-09.2009.
    • (2009) J. Neurosci , vol.29 , pp. 9090-9103
    • Wang, X.1    Su, B.2    Lee, H.G.3    Li, X.4    Perry, G.5    Smith, M.A.6    Zhu, X.7
  • 88
    • 76549123596 scopus 로고    scopus 로고
    • Amyloid-β-derived diffusible ligands cause impaired axonal transport of mitochondria in neurons
    • Wang, X., G. Perry, M.A. Smith, and X. Zhu. 2010. Amyloid-β-derived diffusible ligands cause impaired axonal transport of mitochondria in neurons. Neurodegener. Dis. 7:56-59. http://dx.doi.org/10.1159/000283484.
    • (2010) Neurodegener. Dis , vol.7 , pp. 56-59
    • Wang, X.1    Perry, G.2    Smith, M.A.3    Zhu, X.4
  • 89
    • 0043092647 scopus 로고    scopus 로고
    • The mitochondrial protein hFis1 regulates mitochondrial fission in mammalian cells through an interaction with the dynamin-like protein DLP1
    • Yoon, Y., E.W. Krueger, B.J. Oswald, and M.A. McNiven. 2003. The mitochondrial protein hFis1 regulates mitochondrial fission in mammalian cells through an interaction with the dynamin-like protein DLP1. Mol. Cell. Biol. 23:5409-5420. http://dx.doi.org/10.1128/MCB.23.15.5409-5420.2003.
    • (2003) Mol. Cell. Biol , vol.23 , pp. 5409-5420
    • Yoon, Y.1    Krueger, E.W.2    Oswald, B.J.3    McNiven, M.A.4
  • 90
    • 33746565567 scopus 로고    scopus 로고
    • Tau associates with actin in differentiating PC12 cells
    • Yu, J.Z., and M.M. Rasenick. 2006. Tau associates with actin in differentiating PC12 cells. FASEB J. 20:1452-1461. http://dx.doi.org/10.1096/fj.05-5206com.
    • (2006) FASEB J , vol.20 , pp. 1452-1461
    • Yu, J.Z.1    Rasenick, M.M.2
  • 91
    • 39549117998 scopus 로고    scopus 로고
    • Axonal transport rates in vivo are unaffected by tau deletion or overexpression in mice
    • Yuan, A., A. Kumar, C. Peterhoff, K. Duff, and R.-A. Nixon. 2008. Axonal transport rates in vivo are unaffected by tau deletion or overexpression in mice. J. Neurosci. 28:1682-1687. http://dx.doi.org/10.1523/JNEUROSCI.5242-07.2008.
    • (2008) J. Neurosci , vol.28 , pp. 1682-1687
    • Yuan, A.1    Kumar, A.2    Peterhoff, C.3    Duff, K.4    Nixon, R.-A.5
  • 92
    • 77956587739 scopus 로고    scopus 로고
    • 2+ elevation, missorting of endogenous Tau into dendrites, Tau phosphorylation, and destruction of microtubules and spines
    • 2+ elevation, missorting of endogenous Tau into dendrites, Tau phosphorylation, and destruction of microtubules and spines. J. Neurosci. 30:11938-11950. http://dx.doi.org/10.1523/JNEUROSCI.2357-10.2010.
    • (2010) J. Neurosci , vol.30 , pp. 11938-11950
    • Zempel, H.1    Thies, E.2    Mandelkow, E.3    Mandelkow, E.M.4
  • 93
    • 84887828122 scopus 로고    scopus 로고
    • Amyloid-β oligomers induce synaptic damage via Tau-dependent microtubule severing by TTLL6 and spastin
    • Zempel, H., J. Luedtke, Y. Kumar, J. Biernat, H. Dawson, E. Mandelkow, and E.M. Mandelkow. 2013. Amyloid-β oligomers induce synaptic damage via Tau-dependent microtubule severing by TTLL6 and spastin. EMBO J. 32:2920-2937. http://dx.doi.org/10.1038/emboj.2013.207.
    • (2013) EMBO J , vol.32 , pp. 2920-2937
    • Zempel, H.1    Luedtke, J.2    Kumar, Y.3    Biernat, J.4    Dawson, H.5    Mandelkow, E.6    Mandelkow, E.M.7

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