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Volumn 7, Issue MAY, 2014, Pages

Premature lethality, hyperactivity, and aberrant phosphorylation in transgenic mice expressing a constitutively active form of Fyn

Author keywords

Alzheimer; Dendrite; Fyn kinase; Palmitoylation; Phosphorylation; Spine; Tau

Indexed keywords

N METHYL DEXTRO ASPARTIC ACID RECEPTOR; PROTEIN KINASE FYN; PROTEIN TYROSINE KINASE; TAU PROTEIN;

EID: 84901367930     PISSN: 16625099     EISSN: None     Source Type: Journal    
DOI: 10.3389/fnmol.2014.00040     Document Type: Article
Times cited : (26)

References (42)
  • 1
    • 77956504025 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of tau accompanies disease progression in transgenic mouse models of tauopathy
    • doi: 10.1111/j.1365-2990.2010.01103.x
    • Bhaskar, K., Hobbs, G. A., Yen, S. H., and Lee, G. (2010). Tyrosine phosphorylation of tau accompanies disease progression in transgenic mouse models of tauopathy. Neuropathol. Appl. Neurobiol. 36, 462-477. doi: 10.1111/j.1365-2990.2010.01103.x
    • (2010) Neuropathol. Appl. Neurobiol. , vol.36 , pp. 462-477
    • Bhaskar, K.1    Hobbs, G.A.2    Yen, S.H.3    Lee, G.4
  • 2
    • 84899019792 scopus 로고    scopus 로고
    • Amyloid-β and Tau: The trigger and bullet in Alzheimer disease pathogenesis
    • doi: 10.1001/jamaneurol.2013.5847
    • Bloom, G. S. (2014). Amyloid-β and Tau: the trigger and bullet in Alzheimer disease pathogenesis. JAMA Neurol. 71, 505-508. doi: 10.1001/jamaneurol.2013.5847
    • (2014) JAMA Neurol. , vol.71 , pp. 505-508
    • Bloom, G.S.1
  • 3
    • 84879217258 scopus 로고    scopus 로고
    • A 'danse macabre': Tau and Fyn in STEP with amyloid beta to facilitate induction of synaptic depression and excitotoxicity
    • doi: 10.1111/ejn.12251
    • Boehm, J. (2013). A 'danse macabre': tau and Fyn in STEP with amyloid beta to facilitate induction of synaptic depression and excitotoxicity. Eur. J. Neurosci. 37, 1925-1930. doi: 10.1111/ejn.12251
    • (2013) Eur. J. Neurosci. , vol.37 , pp. 1925-1930
    • Boehm, J.1
  • 4
    • 0028362458 scopus 로고
    • A sequence of cytoskeleton changes related to the formation of neurofibrillary tangles and neuropil threads
    • doi: 10.1007/BF00293315
    • Braak, E., Braak, H., and Mandelkow, E. M. (1994). A sequence of cytoskeleton changes related to the formation of neurofibrillary tangles and neuropil threads. Acta Neuropathol. 87, 554-567. doi: 10.1007/BF00293315
    • (1994) Acta Neuropathol. , vol.87 , pp. 554-567
    • Braak, E.1    Braak, H.2    Mandelkow, E.M.3
  • 5
    • 3442876436 scopus 로고    scopus 로고
    • Posttranslational modifications of tau-Role in human tauopathies and modeling in transgenic animals
    • doi: 10.2174/1389450043345236
    • Chen, F., David, D., Ferrari, A., and Götz, J. (2004). Posttranslational modifications of tau-Role in human tauopathies and modeling in transgenic animals. Curr. Drug Targets 5, 503-515. doi: 10.2174/1389450043345236
    • (2004) Curr. Drug Targets , vol.5 , pp. 503-515
    • Chen, F.1    David, D.2    Ferrari, A.3    Götz, J.4
  • 6
    • 27144489060 scopus 로고    scopus 로고
    • Fyn kinase induces synaptic and cognitive impairments in a transgenic mouse model of Alzheimer's disease
    • doi: 10.1523/JNEUROSCI.2980-05.2005
    • Chin, J., Palop, J. J., Puolivali, J., Massaro, C., Bien-Ly, N., Gerstein, H., et al. (2005). Fyn kinase induces synaptic and cognitive impairments in a transgenic mouse model of Alzheimer's disease. J. Neurosci. 25, 9694-9703. doi: 10.1523/JNEUROSCI.2980-05.2005
    • (2005) J. Neurosci. , vol.25 , pp. 9694-9703
    • Chin, J.1    Palop, J.J.2    Puolivali, J.3    Massaro, C.4    Bien-Ly, N.5    Gerstein, H.6
  • 7
    • 2442711560 scopus 로고    scopus 로고
    • Fyn kinase modulates synaptotoxicity, but not aberrant sprouting, in human amyloid precursor protein transgenic mice
    • doi: 10.1523/JNEUROSCI.0277-04.2004
    • Chin, J., Palop, J. J., Yu, G. Q., Kojima, N., Masliah, E., and Mucke, L. (2004). Fyn kinase modulates synaptotoxicity, but not aberrant sprouting, in human amyloid precursor protein transgenic mice. J. Neurosci. 24, 4692-4697. doi: 10.1523/JNEUROSCI.0277-04.2004
    • (2004) J. Neurosci. , vol.24 , pp. 4692-4697
    • Chin, J.1    Palop, J.J.2    Yu, G.Q.3    Kojima, N.4    Masliah, E.5    Mucke, L.6
  • 8
    • 54049104444 scopus 로고    scopus 로고
    • Divergent phosphorylation pattern of tau in P301L tau transgenic mice
    • doi: 10.1111/j.1460-9568.2008.06318.x
    • Deters, N., Ittner, L. M., and Götz, J. (2008). Divergent phosphorylation pattern of tau in P301L tau transgenic mice. Eur. J. Neurosci. 28, 137-147. doi: 10.1111/j.1460-9568.2008.06318.x
    • (2008) Eur. J. Neurosci. , vol.28 , pp. 137-147
    • Deters, N.1    Ittner, L.M.2    Götz, J.3
  • 10
    • 77955328980 scopus 로고    scopus 로고
    • Fyn-tau-amyloid: A toxic triad
    • doi: 10.1016/j.cell.2010.07.032
    • Haass, C., and Mandelkow, E. (2010). Fyn-tau-amyloid: a toxic triad. Cell 142, 356-358. doi: 10.1016/j.cell.2010.07.032
    • (2010) Cell , vol.142 , pp. 356-358
    • Haass, C.1    Mandelkow, E.2
  • 11
    • 13644251548 scopus 로고    scopus 로고
    • Altered p59Fyn kinase expression accompanies disease progression in Alzheimer's disease: Implications for its functional role
    • doi: 10.1016/j.neurobiolaging.2004.06.016
    • Ho, G. J., Hashimoto, M., Adame, A., Izu, M., Alford, M. F., Thal, L. J., et al. (2005). Altered p59Fyn kinase expression accompanies disease progression in Alzheimer's disease: implications for its functional role. Neurobiol. Aging 26, 625-635. doi: 10.1016/j.neurobiolaging.2004.06.016
    • (2005) Neurobiol. Aging , vol.26 , pp. 625-635
    • Ho, G.J.1    Hashimoto, M.2    Adame, A.3    Izu, M.4    Alford, M.F.5    Thal, L.J.6
  • 12
    • 78650251838 scopus 로고    scopus 로고
    • Tau mislocalization to dendritic spines mediates synaptic dysfunction independently of neurodegeneration
    • doi: 10.1016/j.neuron.2010.11.030
    • Hoover, B. R., Reed, M. N., Su, J., Penrod, R. D., Kotilinek, L. A., Grant, M. K., et al. (2010). Tau mislocalization to dendritic spines mediates synaptic dysfunction independently of neurodegeneration. Neuron 68, 1067-1081. doi: 10.1016/j.neuron.2010.11.030
    • (2010) Neuron , vol.68 , pp. 1067-1081
    • Hoover, B.R.1    Reed, M.N.2    Su, J.3    Penrod, R.D.4    Kotilinek, L.A.5    Grant, M.K.6
  • 13
    • 34250219566 scopus 로고    scopus 로고
    • Pronuclear injection for the generation of transgenic mice
    • doi: 10.1038/nprot.2007.145
    • Ittner, L. M., and Götz, J. (2007). Pronuclear injection for the generation of transgenic mice. Nat. Protoc. 2, 1206-1215. doi: 10.1038/nprot.2007.145
    • (2007) Nat. Protoc. , vol.2 , pp. 1206-1215
    • Ittner, L.M.1    Götz, J.2
  • 14
    • 78751644048 scopus 로고    scopus 로고
    • Amyloid-beta and tau-a toxic pas de deux in Alzheimer's disease
    • doi: 10.1038/nrn2967
    • Ittner, L. M., and Götz, J. (2011). Amyloid-beta and tau-a toxic pas de deux in Alzheimer's disease. Nat. Rev. Neurosci. 12, 65-72. doi: 10.1038/nrn2967
    • (2011) Nat. Rev. Neurosci. , vol.12 , pp. 65-72
    • Ittner, L.M.1    Götz, J.2
  • 15
    • 77955322042 scopus 로고    scopus 로고
    • Dendritic function of tau mediates amyloid-beta toxicity in Alzheimer's disease mouse models
    • doi: 10.1016/j.cell.2010.06.036
    • Ittner, L. M., Ke, Y. D., Delerue, F., Bi, M., Gladbach, A., van Eersel, J., et al. (2010). Dendritic function of tau mediates amyloid-beta toxicity in Alzheimer's disease mouse models. Cell 142, 387-397. doi: 10.1016/j.cell.2010.06.036
    • (2010) Cell , vol.142 , pp. 387-397
    • Ittner, L.M.1    Ke, Y.D.2    Delerue, F.3    Bi, M.4    Gladbach, A.5    van Eersel, J.6
  • 16
    • 0035851175 scopus 로고    scopus 로고
    • Reduced PP2A activity induces hyperphosphorylation and altered compartmentalization of tau in transgenic mice
    • doi: 10.1074/jbc.M102621200
    • Kins, S., Crameri, A., Evans, D. R., Hemmings, B. A., Nitsch, R. M., and Götz, J. (2001). Reduced PP2A activity induces hyperphosphorylation and altered compartmentalization of tau in transgenic mice. J. Biol. Chem. 276, 38193-38200. doi: 10.1074/jbc.M102621200
    • (2001) J. Biol. Chem. , vol.276 , pp. 38193-38200
    • Kins, S.1    Crameri, A.2    Evans, D.R.3    Hemmings, B.A.4    Nitsch, R.M.5    Götz, J.6
  • 17
    • 0036469248 scopus 로고    scopus 로고
    • Process outgrowth of oligodendrocytes is promoted by interaction of fyn kinase with the cytoskeletal protein tau
    • Klein, C., Kramer, E. M., Cardine, A. M., Schraven, B., Brandt, R., and 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
  • 18
    • 84873461276 scopus 로고    scopus 로고
    • Active glycogen synthase kinase-3 and tau pathology-related tyrosine phosphorylation in pR5 human tau transgenic mice
    • doi: 10.1016/j.neurobiolaging.2012.11.010
    • Köhler, C., Dinekov, M., and Götz, J. (2013). Active glycogen synthase kinase-3 and tau pathology-related tyrosine phosphorylation in pR5 human tau transgenic mice. Neurobiol. Aging 34, 1369-1379. doi: 10.1016/j.neurobiolaging.2012.11.010
    • (2013) Neurobiol. Aging , vol.34 , pp. 1369-1379
    • Köhler, C.1    Dinekov, M.2    Götz, J.3
  • 19
    • 0032459183 scopus 로고    scopus 로고
    • Higher seizure susceptibility and enhanced tyrosine phosphorylation of N-methyl-D-aspartate receptor subunit 2B in fyn transgenic mice
    • Kojima, N., Ishibashi, H., Obata, K., and Kandel, E. R. (1998). Higher seizure susceptibility and enhanced tyrosine phosphorylation of N-methyl-D-aspartate receptor subunit 2B in fyn transgenic mice. Learn. Mem. 5, 429-445.
    • (1998) Learn. Mem. , vol.5 , pp. 429-445
    • Kojima, N.1    Ishibashi, H.2    Obata, K.3    Kandel, E.R.4
  • 20
    • 0030970839 scopus 로고    scopus 로고
    • Rescuing impairment of long-term potentiation in fyn-deficient mice by introducing Fyn transgene
    • doi: 10.1073/pnas.94.9.4761
    • Kojima, N., Wang, J., Mansuy, I. M., Grant, S. G., Mayford, M., and Kandel, E. R. (1997). Rescuing impairment of long-term potentiation in fyn-deficient mice by introducing Fyn transgene. Proc. Natl. Acad. Sci. U.S.A. 94, 4761-4765. doi: 10.1073/pnas.94.9.4761
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 4761-4765
    • Kojima, N.1    Wang, J.2    Mansuy, I.M.3    Grant, S.G.4    Mayford, M.5    Kandel, E.R.6
  • 21
    • 79958252836 scopus 로고    scopus 로고
    • From axon-glial signalling to myelination: The integrating role of oligodendroglial Fyn kinase
    • doi: 10.1007/s00018-010-0616-z
    • Kramer-Albers, E. M., and White, R. (2011). From axon-glial signalling to myelination: the integrating role of oligodendroglial Fyn kinase. Cell. Mol. Life Sci. 68, 2003-2012. doi: 10.1007/s00018-010-0616-z
    • (2011) Cell. Mol. Life Sci. , vol.68 , pp. 2003-2012
    • Kramer-Albers, E.M.1    White, R.2
  • 22
    • 84869992747 scopus 로고    scopus 로고
    • The complex PrP(c)-Fyn couples human oligomeric Abeta with pathological tau changes in Alzheimer's disease
    • doi: 10.1523/JNEUROSCI.1858-12.2012
    • Larson, M., Sherman, M. A., Amar, F., Nuvolone, M., Schneider, J. A., Bennett, D. A., et al. (2012). The complex PrP(c)-Fyn couples human oligomeric Abeta with pathological tau changes in Alzheimer's disease. J. Neurosci. 32, 16857-16871a. doi: 10.1523/JNEUROSCI.1858-12.2012
    • (2012) J. Neurosci. , vol.32
    • Larson, M.1    Sherman, M.A.2    Amar, F.3    Nuvolone, M.4    Schneider, J.A.5    Bennett, D.A.6
  • 23
    • 84871414210 scopus 로고    scopus 로고
    • The many faces of alpha-synuclein: From structure and toxicity to therapeutic target
    • doi: 10.1038/nrn3406
    • Lashuel, H. A., Overk, C. R., Oueslati, A., and Masliah, E. (2013). The many faces of alpha-synuclein: from structure and toxicity to therapeutic target. Nat. Rev. Neurosci. 14, 38-48. doi: 10.1038/nrn3406
    • (2013) Nat. Rev. Neurosci. , vol.14 , pp. 38-48
    • Lashuel, H.A.1    Overk, C.R.2    Oueslati, A.3    Masliah, E.4
  • 24
    • 0344505849 scopus 로고    scopus 로고
    • Tau interacts with src-family non-receptor tyrosine kinases
    • Lee, G., Newman, S. T., Gard, D. L., Band, H., and Panchamoorthy, G. (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
  • 25
    • 33847752706 scopus 로고    scopus 로고
    • Srcasm corrects Fyn-induced epidermal hyperplasia by kinase down-regulation
    • doi: 10.1074/jbc.M606583200
    • Li, W., Marshall, C., Mei, L., Gelfand, J., and Seykora, J. T. (2007). Srcasm corrects Fyn-induced epidermal hyperplasia by kinase down-regulation. J. Biol. Chem. 282, 1161-1169. doi: 10.1074/jbc.M606583200
    • (2007) J. Biol. Chem. , vol.282 , pp. 1161-1169
    • Li, W.1    Marshall, C.2    Mei, L.3    Gelfand, J.4    Seykora, J.T.5
  • 26
    • 84876078566 scopus 로고    scopus 로고
    • The CAMKK2-AMPK kinase pathway mediates the synaptotoxic effects of Abeta oligomers through Tau phosphorylation
    • doi: 10.1016/j.neuron.2013.02.003
    • Mairet-Coello, G., Courchet, J., Pieraut, S., Courchet, V., Maximov, A., and Polleux, F. (2013). The CAMKK2-AMPK kinase pathway mediates the synaptotoxic effects of Abeta oligomers through Tau phosphorylation. Neuron 78, 94-108. doi: 10.1016/j.neuron.2013.02.003
    • (2013) Neuron , vol.78 , pp. 94-108
    • Mairet-Coello, G.1    Courchet, J.2    Pieraut, S.3    Courchet, V.4    Maximov, A.5    Polleux, F.6
  • 27
    • 0027176228 scopus 로고
    • Constitutive activation of Src family kinases in mouse embryos that lack Csk
    • doi: 10.1016/0092-8674(93)90642-4
    • Nada, S., Yagi, T., Takeda, H., Tokunaga, T., Nakagawa, H., Ikawa, Y., et al. (1993). Constitutive activation of Src family kinases in mouse embryos that lack Csk. Cell 73, 1125-1135. doi: 10.1016/0092-8674(93)90642-4
    • (1993) Cell , vol.73 , pp. 1125-1135
    • Nada, S.1    Yagi, T.2    Takeda, H.3    Tokunaga, T.4    Nakagawa, H.5    Ikawa, Y.6
  • 28
    • 0036276219 scopus 로고    scopus 로고
    • c-Src-mediated phosphorylation of hnRNP K drives translational activation of specifically silenced mRNAs
    • doi: 10.1128/MCB.22.13.4535-4543.2002
    • Ostareck-Lederer, A., Ostareck, D. H., Cans, C., Neubauer, G., Bomsztyk, K., Superti-Furga, G., et al. (2002). c-Src-mediated phosphorylation of hnRNP K drives translational activation of specifically silenced mRNAs. Mol. Cell. Biol. 22, 4535-4543. doi: 10.1128/MCB.22.13.4535-4543.2002
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 4535-4543
    • Ostareck-Lederer, A.1    Ostareck, D.H.2    Cans, C.3    Neubauer, G.4    Bomsztyk, K.5    Superti-Furga, G.6
  • 29
    • 77955653372 scopus 로고    scopus 로고
    • Determinants of membrane association in the SH4 domain of Fyn: Roles of N-terminus myristoylation and side-chain thioacylation
    • doi: 10.1016/j.bbamem.2010.06.009
    • Rawat, A., and Nagaraj, R. (2010). Determinants of membrane association in the SH4 domain of Fyn: roles of N-terminus myristoylation and side-chain thioacylation. Biochim. Biophys. Acta 1798, 1854-1863. doi: 10.1016/j.bbamem.2010.06.009
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 1854-1863
    • Rawat, A.1    Nagaraj, R.2
  • 30
    • 13544256790 scopus 로고    scopus 로고
    • Src protein-tyrosine kinase structure and regulation
    • doi: 10.1016/j.bbrc.2004.09.171
    • Roskoski, R. Jr. (2004). Src protein-tyrosine kinase structure and regulation. Biochem. Biophys. Res. Commun. 324, 1155-1164. doi: 10.1016/j.bbrc.2004.09.171
    • (2004) Biochem. Biophys. Res. Commun. , vol.324 , pp. 1155-1164
    • Roskoski Jr., R.1
  • 31
    • 34548282678 scopus 로고    scopus 로고
    • The membrane targeting and spatial activation of Src, Yes and Fyn is influenced by palmitoylation and distinct RhoB/RhoD endosome requirements
    • doi: 10.1242/jcs.003657
    • Sandilands, E., Brunton, V. G., and Frame, M. C. (2007). The membrane targeting and spatial activation of Src, Yes and Fyn is influenced by palmitoylation and distinct RhoB/RhoD endosome requirements. J. Cell Sci. 120, 2555-2564. doi: 10.1242/jcs.003657
    • (2007) J. Cell Sci. , vol.120 , pp. 2555-2564
    • Sandilands, E.1    Brunton, V.G.2    Frame, M.C.3
  • 32
    • 0037107424 scopus 로고    scopus 로고
    • Tr-kit-induced resumption of the cell cycle in mouse eggs requires activation of a Src-like kinase
    • doi: 10.1093/emboj/cdf553
    • Sette, C., Paronetto, M. P., Barchi, M., Bevilacqua, A., Geremia, R., and 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. doi: 10.1093/emboj/cdf553
    • (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
  • 33
    • 84860354271 scopus 로고    scopus 로고
    • The protein phosphatase PP2A/Balpha binds to the microtubule-associated proteins Tau and MAP2 at a motif also recognized by the kinase Fyn: Implications for tauopathies
    • doi: 10.1074/jbc.M111.338681
    • Sontag, J. M., Nunbhakdi-Craig, V., White, C. L. 3rd., Halpain, S., and Sontag, E. (2012). The protein phosphatase PP2A/Balpha binds to the microtubule-associated proteins Tau and MAP2 at a motif also recognized by the kinase Fyn: implications for tauopathies. J. Biol. Chem. 287, 14984-14993. doi: 10.1074/jbc.M111.338681
    • (2012) J. Biol. Chem. , vol.287 , pp. 14984-14993
    • Sontag, J.M.1    Nunbhakdi-Craig, V.2    White III, C.L.3    Halpain, S.4    Sontag, E.5
  • 34
    • 0035152814 scopus 로고    scopus 로고
    • Neurotrophins are required for nerve growth during development
    • doi: 10.1038/82868
    • Tucker, K. L., Meyer, M., and Barde, Y. A. (2001). Neurotrophins are required for nerve growth during development. Nat. Neurosci. 4, 29-37. doi: 10.1038/82868
    • (2001) Nat. Neurosci. , vol.4 , pp. 29-37
    • Tucker, K.L.1    Meyer, M.2    Barde, Y.A.3
  • 35
    • 84884200967 scopus 로고    scopus 로고
    • Metabotropic glutamate receptor 5 is a coreceptor for Alzheimer abeta oligomer bound to cellular prion protein
    • doi: 10.1016/j.neuron.2013.06.036
    • Um, J. W., Kaufman, A. C., Kostylev, M., Heiss, J. K., Stagi, M., Takahashi, H., et al. (2013). Metabotropic glutamate receptor 5 is a coreceptor for Alzheimer abeta oligomer bound to cellular prion protein. Neuron 79, 887-902. doi: 10.1016/j.neuron.2013.06.036
    • (2013) Neuron , vol.79 , pp. 887-902
    • Um, J.W.1    Kaufman, A.C.2    Kostylev, M.3    Heiss, J.K.4    Stagi, M.5    Takahashi, H.6
  • 36
    • 84866065959 scopus 로고    scopus 로고
    • Alzheimer amyloid-beta oligomer bound to postsynaptic prion protein activates Fyn to impair neurons
    • doi: 10.1038/nn.3178
    • Um, J. W., Nygaard, H. B., Heiss, J. K., Kostylev, M. A., Stagi, M., Vortmeyer, A., et al. (2012). Alzheimer amyloid-beta oligomer bound to postsynaptic prion protein activates Fyn to impair neurons. Nat. Neurosci. 15, 1227-1235. doi: 10.1038/nn.3178
    • (2012) Nat. Neurosci. , vol.15 , pp. 1227-1235
    • Um, J.W.1    Nygaard, H.B.2    Heiss, J.K.3    Kostylev, M.A.4    Stagi, M.5    Vortmeyer, A.6
  • 37
    • 79961025441 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of tau regulates its interactions with Fyn SH2 domains, but not SH3 domains, altering the cellular localization of tau
    • doi: 10.1111/j.1742-4658.2011.08218.x
    • Usardi, A., Pooler, A. M., Seereeram, A., Reynolds, C. H., Derkinderen, P., Anderton, B., et al. (2011). Tyrosine phosphorylation of tau regulates its interactions with Fyn SH2 domains, but not SH3 domains, altering the cellular localization of tau. FEBS J. 278, 2927-2937. doi: 10.1111/j.1742-4658.2011.08218.x
    • (2011) FEBS J. , vol.278 , pp. 2927-2937
    • Usardi, A.1    Pooler, A.M.2    Seereeram, A.3    Reynolds, C.H.4    Derkinderen, P.5    Anderton, B.6
  • 38
    • 84880087894 scopus 로고    scopus 로고
    • Overcoming barriers and thresholds-signaling of oligomeric Abeta through the prion protein to Fyn
    • doi: 10.1186/1750-1326-8-24
    • Wang, H., Ren, C. H., Gunawardana, C. G., and Schmitt-Ulms, G. (2013). Overcoming barriers and thresholds-signaling of oligomeric Abeta through the prion protein to Fyn. Mol. Neurodegener. 8, 24. doi: 10.1186/1750-1326-8-24
    • (2013) Mol. Neurodegener. , vol.8 , pp. 24
    • Wang, H.1    Ren, C.H.2    Gunawardana, C.G.3    Schmitt-Ulms, G.4
  • 39
    • 0030613520 scopus 로고    scopus 로고
    • Palmitoylation of p59fyn is reversible and sufficient for plasma membrane association
    • doi: 10.1091/mbc.8.6.1159
    • Wolven, A., Okamura, H., Rosenblatt, Y., and Resh, M. D. (1997). Palmitoylation of p59fyn is reversible and sufficient for plasma membrane association. Mol. Biol. Cell 8, 1159-1173. doi: 10.1091/mbc.8.6.1159
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1159-1173
    • Wolven, A.1    Okamura, H.2    Rosenblatt, Y.3    Resh, M.D.4
  • 40
    • 0035955702 scopus 로고    scopus 로고
    • Binding of Fyn to MAP-2c through an SH3 binding domain. Regulation of the interaction by ERK2
    • doi: 10.1074/jbc.M107807200
    • Zamora-Leon, S. P., Lee, G., Davies, P., and 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. doi: 10.1074/jbc.M107807200
    • (2001) J. Biol. Chem. , vol.276 , pp. 39950-39958
    • Zamora-Leon, S.P.1    Lee, G.2    Davies, P.3    Shafit-Zagardo, B.4
  • 41
    • 84887828122 scopus 로고    scopus 로고
    • Amyloid-beta oligomers induce synaptic damage via Tau-dependent microtubule severing by TTLL6 and spastin
    • doi: 10.1038/emboj.2013.207
    • Zempel, H., Luedtke, J., Kumar, Y., Biernat, J., Dawson, H., Mandelkow, E., et al. (2013). Amyloid-beta oligomers induce synaptic damage via Tau-dependent microtubule severing by TTLL6 and spastin. EMBO J. 32, 2920-2937. doi: 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
  • 42
    • 77956587739 scopus 로고    scopus 로고
    • Abeta oligomers cause localized Ca(2+) elevation, missorting of endogenous Tau into dendrites, Tau phosphorylation, and destruction of microtubules and spines
    • doi: 10.1523/JNEUROSCI.2357-10.2010
    • Zempel, H., Thies, E., Mandelkow, E., and Mandelkow, E. M. (2010). Abeta oligomers cause localized Ca(2+) elevation, missorting of endogenous Tau into dendrites, Tau phosphorylation, and destruction of microtubules and spines. J. Neurosci. 30, 11938-11950. doi: 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.