메뉴 건너뛰기




Volumn 8, Issue 1, 2013, Pages

Overcoming barriers and thresholds - Signaling of oligomeric Aβ through the prion protein to Fyn

Author keywords

Alzheimer disease; Amyloid peptide; Excitotoxicity; Fyn; Prion protein; Tau

Indexed keywords

AMYLOID BETA PROTEIN; CAVEOLIN 1; FIBRONECTIN; GLYCOSYLPHOSPHATIDYLINOSITOL; INTEGRIN; LAMININ RECEPTOR; MEMBRANE PROTEIN; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; NERVE CELL ADHESION MOLECULE; OLIGOMERIC AMYLOID BETA PEPTIDE; PRION PROTEIN; PROTEIN KINASE FYN; TAU PROTEIN; UNCLASSIFIED DRUG;

EID: 84880087894     PISSN: None     EISSN: 17501326     Source Type: Journal    
DOI: 10.1186/1750-1326-8-24     Document Type: Review
Times cited : (19)

References (91)
  • 1
    • 78751644048 scopus 로고    scopus 로고
    • Amyloid-beta and tau-A toxic pas de deux in Alzheimer's disease
    • 21309096
    • Amyloid-beta and tau-a toxic pas de deux in Alzheimer's disease. Ittner LM, Gotz J, Nat Rev Neurosci 2011 12 65 72 21309096
    • (2011) Nat Rev Neurosci , vol.12 , pp. 65-72
    • Ittner, L.M.1    Gotz, J.2
  • 3
    • 0344505849 scopus 로고    scopus 로고
    • Tau interacts with src-family non-receptor tyrosine kinases
    • 9763511
    • Tau interacts with src-family non-receptor tyrosine kinases. Lee G, Newman ST, Gard DL, Band H, Panchamoorthy G, J Cell Sci 1998 111 Pt 21 3167 3177 9763511
    • (1998) J Cell Sci , vol.111 , Issue.PT 21 , pp. 3167-3177
    • Lee, G.1    Newman, S.T.2    Gard, D.L.3    Band, H.4    Panchamoorthy, G.5
  • 4
    • 0037197836 scopus 로고    scopus 로고
    • Tau is essential to beta -amyloid-induced neurotoxicity
    • 10.1073/pnas.092136199 11959919
    • Tau is essential to beta -amyloid-induced neurotoxicity. Rapoport M, Dawson HN, Binder LI, Vitek MP, Ferreira A, Proc Natl Acad Sci 2002 99 6364 6369 10.1073/pnas.092136199 11959919
    • (2002) Proc Natl Acad Sci , vol.99 , pp. 6364-6369
    • Rapoport, M.1    Dawson, H.N.2    Binder, L.I.3    Vitek, M.P.4    Ferreira, A.5
  • 5
    • 78651506630 scopus 로고    scopus 로고
    • Amyloid-beta/Fyn-induced synaptic, network, and cognitive impairments depend on tau levels in multiple mouse models of Alzheimer's disease
    • 10.1523/JNEUROSCI.4152-10.2011 21228179
    • Amyloid-beta/Fyn-induced synaptic, network, and cognitive impairments depend on tau levels in multiple mouse models of Alzheimer's disease. Roberson ED, Halabisky B, Yoo JW, Yao J, Chin J, Yan F, Wu T, Hamto P, Devidze N, Yu GQ, et al. J Neurosci 2011 31 700 711 10.1523/JNEUROSCI.4152-10.2011 21228179
    • (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
  • 7
    • 77955328980 scopus 로고    scopus 로고
    • Fyn-tau-amyloid: A toxic triad
    • 10.1016/j.cell.2010.07.032 20691893
    • Fyn-tau-amyloid: a toxic triad. Haass C, Mandelkow E, Cell 2010 142 356 358 10.1016/j.cell.2010.07.032 20691893
    • (2010) Cell , vol.142 , pp. 356-358
    • Haass, C.1    Mandelkow, E.2
  • 8
    • 84859070489 scopus 로고    scopus 로고
    • Neuronal receptors as targets for the action of amyloid-beta protein (Abeta) in the brain
    • 22261393
    • Neuronal receptors as targets for the action of amyloid-beta protein (Abeta) in the brain. Patel AN, Jhamandas JH, Expert Rev Mol Med 2012 14 2 22261393
    • (2012) Expert Rev Mol Med , vol.14 , pp. 52
    • Patel, A.N.1    Jhamandas, J.H.2
  • 9
    • 84882670192 scopus 로고    scopus 로고
    • Postsynaptic receptors for amyloid-beta oligomers as mediators of neuronal damage in Alzheimer's disease
    • 23267328
    • Postsynaptic receptors for amyloid-beta oligomers as mediators of neuronal damage in Alzheimer's disease. Dinamarca MC, Rios JA, Inestrosa NC, Front Physiol 2012 3 464 23267328
    • (2012) Front Physiol , vol.3 , pp. 464
    • Dinamarca, M.C.1    Rios, J.A.2    Inestrosa, N.C.3
  • 11
    • 79956302348 scopus 로고    scopus 로고
    • Alzheimer's disease brain-derived amyloid-beta-mediated inhibition of LTP in vivo is prevented by immunotargeting cellular prion protein
    • 10.1523/JNEUROSCI.6500-10.2011 21593310
    • Alzheimer's disease brain-derived amyloid-beta-mediated inhibition of LTP in vivo is prevented by immunotargeting cellular prion protein. Barry AE, Klyubin I, Mc Donald JM, Mably AJ, Farrell MA, Scott M, Walsh DM, Rowan MJ, J Neurosci 2011 31 7259 7263 10.1523/JNEUROSCI.6500-10.2011 21593310
    • (2011) J Neurosci , vol.31 , pp. 7259-7263
    • Barry, A.E.1    Klyubin, I.2    Mc Donald, J.M.3    Mably, A.J.4    Farrell, M.A.5    Scott, M.6    Walsh, D.M.7    Rowan, M.J.8
  • 13
    • 77956197815 scopus 로고    scopus 로고
    • Interaction between human prion protein and amyloid-beta (Abeta) oligomers: Role of N-terminal residues
    • 10.1074/jbc.M110.145516 20576610
    • Interaction between human prion protein and amyloid-beta (Abeta) oligomers: role OF N-terminal residues. Chen S, Yadav SP, Surewicz WK, J Biol Chem 2010 285 26377 26383 10.1074/jbc.M110.145516 20576610
    • (2010) J Biol Chem , vol.285 , pp. 26377-26383
    • Chen, S.1    Yadav, S.P.2    Surewicz, W.K.3
  • 15
    • 79955393816 scopus 로고    scopus 로고
    • Amyloid-beta42 interacts mainly with insoluble prion protein in the Alzheimer brain
    • 10.1074/jbc.M110.199356 21393248
    • Amyloid-beta42 interacts mainly with insoluble prion protein in the Alzheimer brain. Zou WQ, Xiao X, Yuan J, Puoti G, Fujioka H, Wang X, Richardson S, Zhou X, Zou R, Li S, et al. J Biol Chem 2011 286 15095 15105 10.1074/jbc.M110.199356 21393248
    • (2011) J Biol Chem , vol.286 , pp. 15095-15105
    • Zou, W.Q.1    Xiao, X.2    Yuan, J.3    Puoti, G.4    Fujioka, H.5    Wang, X.6    Richardson, S.7    Zhou, X.8    Zou, R.9    Li, S.10
  • 17
    • 79960660843 scopus 로고    scopus 로고
    • Ablation of cellular prion protein does not ameliorate abnormal neural network activity or cognitive dysfunction in the J20 line of human amyloid precursor protein transgenic mice
    • 10.1523/JNEUROSCI.1459-11.2011 21775587
    • Ablation of cellular prion protein does not ameliorate abnormal neural network activity or cognitive dysfunction in the J20 line of human amyloid precursor protein transgenic mice. Cisse M, Sanchez PE, Kim DH, Ho K, Yu GQ, Mucke L, J Neurosci 2011 31 10427 10431 10.1523/JNEUROSCI.1459-11.2011 21775587
    • (2011) J Neurosci , vol.31 , pp. 10427-10431
    • Cisse, M.1    Sanchez, P.E.2    Kim, D.H.3    Ho, K.4    Yu, G.Q.5    Mucke, L.6
  • 18
    • 77956965281 scopus 로고    scopus 로고
    • Prion protein in Alzheimer's pathogenesis: A hot and controversial issue
    • 10.1002/emmm.201000088 20698011
    • Prion protein in Alzheimer's pathogenesis: a hot and controversial issue. Benilova I, De Strooper B, EMBO Mol Med 2010 2 289 290 10.1002/emmm.201000088 20698011
    • (2010) EMBO Mol Med , vol.2 , pp. 289-290
    • Benilova, I.1    De Strooper, B.2
  • 19
    • 84856411525 scopus 로고    scopus 로고
    • Prion protein at the crossroads of physiology and disease
    • 10.1016/j.tins.2011.10.002 22137337
    • Prion protein at the crossroads of physiology and disease. Biasini E, Turnbaugh JA, Unterberger U, Harris DA, Trends Neurosci 2012 35 92 103 10.1016/j.tins.2011.10.002 22137337
    • (2012) Trends Neurosci , vol.35 , pp. 92-103
    • Biasini, E.1    Turnbaugh, J.A.2    Unterberger, U.3    Harris, D.A.4
  • 20
    • 84859937536 scopus 로고    scopus 로고
    • Prion protein is a key determinant of alcohol sensitivity through the modulation of N-methyl-D-aspartate receptor (NMDAR) activity
    • 10.1371/journal.pone.0034691 22536327
    • Prion protein is a key determinant of alcohol sensitivity through the modulation of N-methyl-D-aspartate receptor (NMDAR) activity. Petit-Paitel A, Menard B, Guyon A, Beringue V, Nahon JL, Zsurger N, Chabry J, PLoS One 2012 7 34691 10.1371/journal.pone.0034691 22536327
    • (2012) PLoS One , vol.7 , pp. 534691
    • Petit-Paitel, A.1    Menard, B.2    Guyon, A.3    Beringue, V.4    Nahon, J.L.5    Zsurger, N.6    Chabry, J.7
  • 21
    • 79955670132 scopus 로고    scopus 로고
    • The many faces of tau
    • 10.1016/j.neuron.2011.04.009 21555069
    • The many faces of tau. Morris M, Maeda S, Vossel K, Mucke L, Neuron 2011 70 410 426 10.1016/j.neuron.2011.04.009 21555069
    • (2011) Neuron , vol.70 , pp. 410-426
    • Morris, M.1    Maeda, S.2    Vossel, K.3    Mucke, L.4
  • 22
    • 61349138103 scopus 로고    scopus 로고
    • Alzheimer's Disease: A prion protein connection
    • 10.1038/4571090a 19242462
    • Alzheimer's Disease: a prion protein connection. Cisse M, Mucke L, Nature 2009 457 1090 1091 10.1038/4571090a 19242462
    • (2009) Nature , vol.457 , pp. 1090-1091
    • Cisse, M.1    Mucke, L.2
  • 23
    • 48249126806 scopus 로고    scopus 로고
    • The Prion's elusive reason for being
    • 10.1146/annurev.neuro.31.060407.125620 18558863
    • The Prion's elusive reason for being. Aguzzi A, Baumann F, Bremer J, Annu Rev Neurosci 2008 31 439 477 10.1146/annurev.neuro.31.060407.125620 18558863
    • (2008) Annu Rev Neurosci , vol.31 , pp. 439-477
    • Aguzzi, A.1    Baumann, F.2    Bremer, J.3
  • 24
    • 74249118091 scopus 로고    scopus 로고
    • Is, indeed, the prion protein a Harlequin servant of many masters?
    • 10.4161/pri.3.4.10012 19887913
    • Is, indeed, the prion protein a Harlequin servant of "many" masters? Sorgato MC, Peggion C, Bertoli A, Prion 2009 3 202 205 10.4161/pri.3.4.10012 19887913
    • (2009) Prion , vol.3 , pp. 202-205
    • Sorgato, M.C.1    Peggion, C.2    Bertoli, A.3
  • 25
    • 18544376071 scopus 로고    scopus 로고
    • Prion protein recruits its neuronal receptor NCAM to lipid rafts to activate p59fyn and to enhance neurite outgrowth
    • 10.1083/jcb.200409127 15851519
    • Prion protein recruits its neuronal receptor NCAM to lipid rafts to activate p59fyn and to enhance neurite outgrowth. Santuccione A, Sytnyk V, Leshchyns'ka I, Schachner M, J Cell Biol 2005 169 341 354 10.1083/jcb.200409127 15851519
    • (2005) J Cell Biol , vol.169 , pp. 341-354
    • Santuccione, A.1    Sytnyk, V.2    Leshchyns'Ka, I.3    Schachner, M.4
  • 27
    • 73349140865 scopus 로고    scopus 로고
    • Interactome analyses identify ties of PrP and its mammalian paralogs to oligomannosidic N-glycans and endoplasmic reticulum-derived chaperones
    • 10.1371/journal.ppat.1000608 19798432
    • Interactome analyses identify ties of PrP and its mammalian paralogs to oligomannosidic N-glycans and endoplasmic reticulum-derived chaperones. Watts JC, Huo H, Bai Y, Ehsani S, Jeon AH, Shi T, Daude N, Lau A, Young R, Xu L, et al. PLoS Pathog 2009 5 1000608 10.1371/journal.ppat.1000608 19798432
    • (2009) PLoS Pathog , vol.5 , pp. 51000608
    • Watts, J.C.1    Huo, H.2    Bai, Y.3    Ehsani, S.4    Jeon, A.H.5    Shi, T.6    Daude, N.7    Lau, A.8    Young, R.9    Xu, L.10
  • 29
    • 84869992747 scopus 로고    scopus 로고
    • The Complex PrPc-Fyn couples human oligomeric abeta with pathological Tau changes in Alzheimer's disease
    • 10.1523/JNEUROSCI.1858-12.2012 23175838
    • The Complex PrPc-Fyn couples human oligomeric abeta with pathological Tau changes in Alzheimer's disease. Larson M, Sherman MA, Amar F, Nuvolone M, Schneider JA, Bennett DA, Aguzzi A, Lesne SE, J Neurosci 2012 32 16857 16871 10.1523/JNEUROSCI.1858-12.2012 23175838
    • (2012) J Neurosci , vol.32 , pp. 16857-16871
    • Larson, M.1    Sherman, M.A.2    Amar, F.3    Nuvolone, M.4    Schneider, J.A.5    Bennett, D.A.6    Aguzzi, A.7    Lesne, S.E.8
  • 30
    • 33845882730 scopus 로고    scopus 로고
    • Neural recognition molecules of the immunoglobulin superfamily: Signaling transducers of axon guidance and neuronal migration
    • 10.1038/nn1827 17189949
    • Neural recognition molecules of the immunoglobulin superfamily: signaling transducers of axon guidance and neuronal migration. Maness PF, Schachner M, Nat Neurosci 2007 10 19 26 10.1038/nn1827 17189949
    • (2007) Nat Neurosci , vol.10 , pp. 19-26
    • Maness, P.F.1    Schachner, M.2
  • 31
    • 0037193470 scopus 로고    scopus 로고
    • Cosignaling of NCAM via lipid rafts and the FGF receptor is required for neuritogenesis
    • 10.1083/jcb.200109059 11980923
    • Cosignaling of NCAM via lipid rafts and the FGF receptor is required for neuritogenesis. Niethammer P, Delling M, Sytnyk V, Dityatev A, Fukami K, Schachner M, J Cell Biol 2002 157 521 532 10.1083/jcb.200109059 11980923
    • (2002) J Cell Biol , vol.157 , pp. 521-532
    • Niethammer, P.1    Delling, M.2    Sytnyk, V.3    Dityatev, A.4    Fukami, K.5    Schachner, M.6
  • 33
    • 0027971705 scopus 로고
    • NCAM-dependent neurite outgrowth is inhibited in neurons from Fyn-minus mice
    • 10.1083/jcb.127.3.825 7962063
    • NCAM-dependent neurite outgrowth is inhibited in neurons from Fyn-minus mice. Beggs HE, Soriano P, Maness PF, J Cell Biol 1994 127 825 833 10.1083/jcb.127.3.825 7962063
    • (1994) J Cell Biol , vol.127 , pp. 825-833
    • Beggs, H.E.1    Soriano, P.2    Maness, P.F.3
  • 35
    • 0033571032 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase alpha (PTPalpha) and contactin form a novel neuronal receptor complex linked to the intracellular tyrosine kinase fyn
    • 10.1083/jcb.147.4.707 10562275
    • Protein tyrosine phosphatase alpha (PTPalpha) and contactin form a novel neuronal receptor complex linked to the intracellular tyrosine kinase fyn. Zeng L, D'Alessandri L, Kalousek MB, Vaughan L, Pallen CJ, J Cell Biol 1999 147 707 714 10.1083/jcb.147.4.707 10562275
    • (1999) J Cell Biol , vol.147 , pp. 707-714
    • Zeng, L.1    D'Alessandri, L.2    Kalousek, M.B.3    Vaughan, L.4    Pallen, C.J.5
  • 36
    • 0033587069 scopus 로고    scopus 로고
    • Receptor protein tyrosine phosphatase alpha activates Src-family kinases and controls integrin-mediated responses in fibroblasts
    • 10.1016/S0960-9822(99)80234-6 10339427
    • Receptor protein tyrosine phosphatase alpha activates Src-family kinases and controls integrin-mediated responses in fibroblasts. Su J, Muranjan M, Sap J, Current biology: CB 1999 9 505 511 10.1016/S0960-9822(99)80234-6 10339427
    • (1999) Current Biology: CB , vol.9 , pp. 505-511
    • Su, J.1    Muranjan, M.2    Sap, J.3
  • 37
    • 0037437150 scopus 로고    scopus 로고
    • RPTP-alpha acts as a transducer of mechanical force on alphav/beta3-integrin-cytoskeleton linkages
    • 10.1083/jcb.200211061 12682088
    • RPTP-alpha acts as a transducer of mechanical force on alphav/beta3-integrin-cytoskeleton linkages. von Wichert G, Jiang G, Kostic A, De Vos K, Sap J, Sheetz MP, J Cell Biol 2003 161 143 153 10.1083/jcb.200211061 12682088
    • (2003) J Cell Biol , vol.161 , pp. 143-153
    • Von Wichert, G.1    Jiang, G.2    Kostic, A.3    De Vos, K.4    Sap, J.5    Sheetz, M.P.6
  • 38
    • 0028933161 scopus 로고
    • The receptor-like protein-tyrosine phosphatase, RPTP alpha, is phosphorylated by protein kinase C on two serines close to the inner face of the plasma membrane
    • 10.1074/jbc.270.18.10587 7537734
    • The receptor-like protein-tyrosine phosphatase, RPTP alpha, is phosphorylated by protein kinase C on two serines close to the inner face of the plasma membrane. Tracy S, van der Geer P, Hunter T, J Biol Chem 1995 270 10587 10594 10.1074/jbc.270.18.10587 7537734
    • (1995) J Biol Chem , vol.270 , pp. 10587-10594
    • Tracy, S.1    Van Der Geer, P.2    Hunter, T.3
  • 39
    • 0037077275 scopus 로고    scopus 로고
    • Mitotic activation of protein-tyrosine phosphatase alpha and regulation of its Src-mediated transforming activity by its sites of protein kinase C phosphorylation
    • 10.1074/jbc.M201394200 11923305
    • Mitotic activation of protein-tyrosine phosphatase alpha and regulation of its Src-mediated transforming activity by its sites of protein kinase C phosphorylation. Zheng XM, Resnick RJ, Shalloway D, J Biol Chem 2002 277 21922 21929 10.1074/jbc.M201394200 11923305
    • (2002) J Biol Chem , vol.277 , pp. 21922-21929
    • Zheng, X.M.1    Resnick, R.J.2    Shalloway, D.3
  • 40
    • 52249122222 scopus 로고    scopus 로고
    • NCAM induces CaMKIIalpha-mediated RPTPalpha phosphorylation to enhance its catalytic activity and neurite outgrowth
    • 10.1083/jcb.200803045 18809727
    • NCAM induces CaMKIIalpha-mediated RPTPalpha phosphorylation to enhance its catalytic activity and neurite outgrowth. Bodrikov V, Sytnyk V, Leshchyns'ka I, den Hertog J, Schachner M, J Cell Biol 2008 182 1185 1200 10.1083/jcb.200803045 18809727
    • (2008) J Cell Biol , vol.182 , pp. 1185-1200
    • Bodrikov, V.1    Sytnyk, V.2    Leshchyns'Ka, I.3    Den Hertog, J.4    Schachner, M.5
  • 43
    • 0029963724 scopus 로고    scopus 로고
    • Peptide G, containing the binding site of the 67-kDa laminin receptor, increases and stabilizes laminin binding to cancer cells
    • 10.1074/jbc.271.49.31179 8940117
    • Peptide G, containing the binding site of the 67-kDa laminin receptor, increases and stabilizes laminin binding to cancer cells. Magnifico A, Tagliabue E, Buto S, Ardini E, Castronovo V, Colnaghi MI, Menard S, J Biol Chem 1996 271 31179 31184 10.1074/jbc.271.49.31179 8940117
    • (1996) J Biol Chem , vol.271 , pp. 31179-31184
    • Magnifico, A.1    Tagliabue, E.2    Buto, S.3    Ardini, E.4    Castronovo, V.5    Colnaghi, M.I.6    Menard, S.7
  • 44
    • 33947733680 scopus 로고
    • Laminin receptor expression and function in small-cell lung carcinoma
    • 8194888
    • Laminin receptor expression and function in small-cell lung carcinoma. Pellegrini R, Martignone S, Menard S, Colnaghi MI, Int J Cancer Suppl 1994 8 116 120 8194888
    • (1994) Int J Cancer Suppl , vol.8 , pp. 116-120
    • Pellegrini, R.1    Martignone, S.2    Menard, S.3    Colnaghi, M.I.4
  • 45
    • 0031030316 scopus 로고    scopus 로고
    • Co-regulation and physical association of the 67-kDa monomeric laminin receptor and the alpha6beta4 integrin
    • 10.1074/jbc.272.4.2342 8999943
    • Co-regulation and physical association of the 67-kDa monomeric laminin receptor and the alpha6beta4 integrin. Ardini E, Tagliabue E, Magnifico A, Buto S, Castronovo V, Colnaghi MI, Menard S, J Biol Chem 1997 272 2342 2345 10.1074/jbc.272.4.2342 8999943
    • (1997) J Biol Chem , vol.272 , pp. 2342-2345
    • Ardini, E.1    Tagliabue, E.2    Magnifico, A.3    Buto, S.4    Castronovo, V.5    Colnaghi, M.I.6    Menard, S.7
  • 46
    • 0029565212 scopus 로고
    • The L1 adhesion molecule is a cellular ligand for VLA-5
    • 10.1083/jcb.131.6.1881 8557754
    • The L1 adhesion molecule is a cellular ligand for VLA-5. Ruppert M, Aigner S, Hubbe M, Yagita H, Altevogt P, J Cell Biol 1995 131 1881 1891 10.1083/jcb.131.6.1881 8557754
    • (1995) J Cell Biol , vol.131 , pp. 1881-1891
    • Ruppert, M.1    Aigner, S.2    Hubbe, M.3    Yagita, H.4    Altevogt, P.5
  • 47
    • 15644366702 scopus 로고    scopus 로고
    • A single immunoglobulin-like domain of the human neural cell adhesion molecule L1 supports adhesion by multiple vascular and platelet integrins
    • 10.1083/jcb.139.6.1567 9396761
    • A single immunoglobulin-like domain of the human neural cell adhesion molecule L1 supports adhesion by multiple vascular and platelet integrins. Felding-Habermann B, Silletti S, Mei F, Siu CH, Yip PM, Brooks PC, Cheresh DA, O'Toole TE, Ginsberg MH, Montgomery AM, J Cell Biol 1997 139 1567 1581 10.1083/jcb.139.6.1567 9396761
    • (1997) J Cell Biol , vol.139 , pp. 1567-1581
    • Felding-Habermann, B.1    Silletti, S.2    Mei, F.3    Siu, C.H.4    Yip, P.M.5    Brooks, P.C.6    Cheresh, D.A.7    O'Toole, T.E.8    Ginsberg, M.H.9    Montgomery, A.M.10
  • 48
    • 0037421205 scopus 로고    scopus 로고
    • PTP alpha regulates integrin-stimulated FAK autophosphorylation and cytoskeletal rearrangement in cell spreading and migration
    • 10.1083/jcb.200206049 12515828
    • PTP alpha regulates integrin-stimulated FAK autophosphorylation and cytoskeletal rearrangement in cell spreading and migration. Zeng L, Si X, Yu WP, Le HT, Ng KP, Teng RM, Ryan K, Wang DZ, Ponniah S, Pallen CJ, J Cell Biol 2003 160 137 146 10.1083/jcb.200206049 12515828
    • (2003) J Cell Biol , vol.160 , pp. 137-146
    • Zeng, L.1    Si, X.2    Yu, W.P.3    Le, H.T.4    Ng, K.P.5    Teng, R.M.6    Ryan, K.7    Wang, D.Z.8    Ponniah, S.9    Pallen, C.J.10
  • 49
    • 33744956948 scopus 로고    scopus 로고
    • Integrin-induced tyrosine phosphorylation of protein-tyrosine phosphatase-alpha is required for cytoskeletal reorganization and cell migration
    • 10.1074/jbc.M600561200 16507567
    • Integrin-induced tyrosine phosphorylation of protein-tyrosine phosphatase-alpha is required for cytoskeletal reorganization and cell migration. Chen M, Chen SC, Pallen CJ, J Biol Chem 2006 281 11972 11980 10.1074/jbc.M600561200 16507567
    • (2006) J Biol Chem , vol.281 , pp. 11972-11980
    • Chen, M.1    Chen, S.C.2    Pallen, C.J.3
  • 50
    • 11144354850 scopus 로고    scopus 로고
    • The caveolin proteins
    • 10.1186/gb-2004-5-3-214 15003112
    • The caveolin proteins. Williams TM, Lisanti MP, Genome Biol 2004 5 214 10.1186/gb-2004-5-3-214 15003112
    • (2004) Genome Biol , vol.5 , pp. 214
    • Williams, T.M.1    Lisanti, M.P.2
  • 51
    • 0029803093 scopus 로고    scopus 로고
    • Src tyrosine kinases, galpha subunits, and H-Ras share a common membrane-anchored scaffolding protein, caveolin. Caveolin binding negatively regulates the auto-activation of Src tyrosine kinases
    • 10.1074/jbc.271.46.29182 8910575
    • Src tyrosine kinases, galpha subunits, and H-Ras share a common membrane-anchored scaffolding protein, caveolin. Caveolin binding negatively regulates the auto-activation of Src tyrosine kinases. Li S, Couet J, Lisanti MP, J Biol Chem 1996 271 29182 29190 10.1074/jbc.271.46.29182 8910575
    • (1996) J Biol Chem , vol.271 , pp. 29182-29190
    • Li, S.1    Couet, J.2    Lisanti, M.P.3
  • 52
    • 33746787634 scopus 로고    scopus 로고
    • Cellular prion protein and caveolin-1 interaction in a neuronal cell line precedes Fyn/Erk 1/2 signal transduction
    • 17489019
    • Cellular prion protein and caveolin-1 interaction in a neuronal cell line precedes Fyn/Erk 1/2 signal transduction. Toni M, Spisni E, Griffoni C, Santi S, Riccio M, Lenaz P, Tomasi V, J Biomed Biotechnol 2006 2006 69469 17489019
    • (2006) J Biomed Biotechnol , vol.2006 , pp. 69469
    • Toni, M.1    Spisni, E.2    Griffoni, C.3    Santi, S.4    Riccio, M.5    Lenaz, P.6    Tomasi, V.7
  • 53
    • 67449149931 scopus 로고    scopus 로고
    • PrPc activation induces neurite outgrowth and differentiation in PC12 cells: Role for caveolin-1 in the signal transduction pathway
    • 10.1111/j.1471-4159.2009.06123.x 19457127
    • PrPc activation induces neurite outgrowth and differentiation in PC12 cells: role for caveolin-1 in the signal transduction pathway. Pantera B, Bini C, Cirri P, Paoli P, Camici G, Manao G, Caselli A, J Neurochem 2009 110 194 207 10.1111/j.1471-4159.2009.06123.x 19457127
    • (2009) J Neurochem , vol.110 , pp. 194-207
    • Pantera, B.1    Bini, C.2    Cirri, P.3    Paoli, P.4    Camici, G.5    Manao, G.6    Caselli, A.7
  • 54
    • 84877707375 scopus 로고    scopus 로고
    • One-Step generation of mice carrying mutations in multiple genes by CRISPR/Cas-mediated genome engineering
    • 10.1016/j.cell.2013.04.025 23643243
    • One-Step generation of mice carrying mutations in multiple genes by CRISPR/Cas-mediated genome engineering. Wang H, Yang H, Shivalila CS, Dawlaty MM, Cheng AW, Zhang F, Jaenisch R, Cell 2013 153 910 918 10.1016/j.cell.2013.04. 025 23643243
    • (2013) Cell , vol.153 , pp. 910-918
    • Wang, H.1    Yang, H.2    Shivalila, C.S.3    Dawlaty, M.M.4    Cheng, A.W.5    Zhang, F.6    Jaenisch, R.7
  • 55
    • 84876907931 scopus 로고    scopus 로고
    • Integrated systems approach identifies genetic nodes and networks in late-onset Alzheimer's disease
    • 10.1016/j.cell.2013.03.030 23622250
    • Integrated systems approach identifies genetic nodes and networks in late-onset Alzheimer's disease. Zhang B, Cell 2013 153 707 720 10.1016/j.cell.2013.03.030 23622250
    • (2013) Cell , vol.153 , pp. 707-720
    • Zhang, B.1
  • 56
    • 84864616734 scopus 로고    scopus 로고
    • Beyond 'furballs' and 'dumpling soups' - Towards a molecular architecture of signaling complexes and networks
    • 10.1016/j.febslet.2012.04.029 22710161
    • Beyond 'furballs' and 'dumpling soups'-towards a molecular architecture of signaling complexes and networks. Lewitzky M, Simister PC, Feller SM, FEBS Lett 2012 586 2740 2750 10.1016/j.febslet.2012.04.029 22710161
    • (2012) FEBS Lett , vol.586 , pp. 2740-2750
    • Lewitzky, M.1    Simister, P.C.2    Feller, S.M.3
  • 57
    • 84887212358 scopus 로고    scopus 로고
    • The comprehensive native interactome of a fully functional tagged prion protein
    • 10.1371/journal.pone.0004446 19209230
    • The comprehensive native interactome of a fully functional tagged prion protein. Rutishauser D, Mertz KD, Moos R, Brunner E, Rulicke T, Calella AM, Aguzzi A, PLoS One 2009 4 4446 10.1371/journal.pone.0004446 19209230
    • (2009) PLoS One , vol.4 , pp. 54446
    • Rutishauser, D.1    Mertz, K.D.2    Moos, R.3    Brunner, E.4    Rulicke, T.5    Calella, A.M.6    Aguzzi, A.7
  • 59
    • 0027291065 scopus 로고
    • Release of the cellular prion protein from cultured cells after loss of its glycoinositol phospholipid anchor
    • 10.1093/glycob/3.4.319 7691278
    • Release of the cellular prion protein from cultured cells after loss of its glycoinositol phospholipid anchor. Borchelt DR, Rogers M, Stahl N, Telling G, Prusiner SB, Glycobiology 1993 3 319 329 10.1093/glycob/3.4.319 7691278
    • (1993) Glycobiology , vol.3 , pp. 319-329
    • Borchelt, D.R.1    Rogers, M.2    Stahl, N.3    Telling, G.4    Prusiner, S.B.5
  • 60
    • 0030894380 scopus 로고    scopus 로고
    • Characterization of detergent-insoluble complexes containing the cellular prion protein and its scrapie isoform
    • 10.1074/jbc.272.10.6324 9045652
    • Characterization of detergent-insoluble complexes containing the cellular prion protein and its scrapie isoform. Naslavsky N, Stein R, Yanai A, Friedlander G, Taraboulos A, J Biol Chem 1997 272 6324 6331 10.1074/jbc.272.10. 6324 9045652
    • (1997) J Biol Chem , vol.272 , pp. 6324-6331
    • Naslavsky, N.1    Stein, R.2    Yanai, A.3    Friedlander, G.4    Taraboulos, A.5
  • 61
    • 84875981923 scopus 로고    scopus 로고
    • Prion protein-mediated toxicity of amyloid-beta oligomers requires lipid rafts and the transmembrane LRP1
    • 10.1074/jbc.M112.400358 23386614
    • Prion protein-mediated toxicity of amyloid-beta oligomers requires lipid rafts and the transmembrane LRP1. Rushworth JV, Griffiths HH, Watt NT, Hooper NM, J Biol Chem 2013 288 8935 8951 10.1074/jbc.M112.400358 23386614
    • (2013) J Biol Chem , vol.288 , pp. 8935-8951
    • Rushworth, J.V.1    Griffiths, H.H.2    Watt, N.T.3    Hooper, N.M.4
  • 62
    • 82255173996 scopus 로고    scopus 로고
    • Mysteries of the cell. Do lipid rafts exist?
    • 22116853
    • Mysteries of the cell. Do lipid rafts exist? Leslie M, Science 2011 334 1046 1047 22116853
    • (2011) Science , vol.334 , pp. 1046-1047
    • Leslie, M.1
  • 63
    • 74849118341 scopus 로고    scopus 로고
    • Lipid rafts as a membrane-organizing principle
    • 10.1126/science.1174621 20044567
    • Lipid rafts as a membrane-organizing principle. Lingwood D, Simons K, Science 2010 327 46 50 10.1126/science.1174621 20044567
    • (2010) Science , vol.327 , pp. 46-50
    • Lingwood, D.1    Simons, K.2
  • 64
    • 24644505858 scopus 로고    scopus 로고
    • A lipid raft-associated 67kDa laminin receptor mediates suppressive effect of epigallocatechin-3-O-gallate on FcepsilonRI expression
    • 10.1016/j.bbrc.2005.08.146 16140266
    • A lipid raft-associated 67kDa laminin receptor mediates suppressive effect of epigallocatechin-3-O-gallate on FcepsilonRI expression. Fujimura Y, Yamada K, Tachibana H, Biochem Biophys Res Commun 2005 336 674 681 10.1016/j.bbrc.2005.08.146 16140266
    • (2005) Biochem Biophys Res Commun , vol.336 , pp. 674-681
    • Fujimura, Y.1    Yamada, K.2    Tachibana, H.3
  • 65
    • 73249138376 scopus 로고    scopus 로고
    • Hotspots of GPI-anchored proteins and integrin nanoclusters function as nucleation sites for cell adhesion
    • 10.1073/pnas.0905217106 19850864
    • Hotspots of GPI-anchored proteins and integrin nanoclusters function as nucleation sites for cell adhesion. van Zanten TS, Cambi A, Koopman M, Joosten B, Figdor CG, Garcia-Parajo MF, Proc Natl Acad Sci USA 2009 106 18557 18562 10.1073/pnas.0905217106 19850864
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 18557-18562
    • Van Zanten, T.S.1    Cambi, A.2    Koopman, M.3    Joosten, B.4    Figdor, C.G.5    Garcia-Parajo, M.F.6
  • 66
    • 0030294361 scopus 로고    scopus 로고
    • Beta1 integrin-mediated activation of focal adhesion kinase and its association with Fyn and Zap-70 in human NK cells
    • 8892616
    • Beta1 integrin-mediated activation of focal adhesion kinase and its association with Fyn and Zap-70 in human NK cells. Rabinowich H, Manciulea M, Herberman RB, Whiteside TL, J Immunol 1996 157 3860 3868 8892616
    • (1996) J Immunol , vol.157 , pp. 3860-3868
    • Rabinowich, H.1    Manciulea, M.2    Herberman, R.B.3    Whiteside, T.L.4
  • 67
    • 65549164330 scopus 로고    scopus 로고
    • Transmembrane form agrin-induced process formation requires lipid rafts and the activation of Fyn and MAPK
    • 10.1074/jbc.M806719200 19139104
    • Transmembrane form agrin-induced process formation requires lipid rafts and the activation of Fyn and MAPK. Ramseger R, White R, Kroger S, J Biol Chem 2009 284 7697 7705 10.1074/jbc.M806719200 19139104
    • (2009) J Biol Chem , vol.284 , pp. 7697-7705
    • Ramseger, R.1    White, R.2    Kroger, S.3
  • 68
    • 61349201380 scopus 로고    scopus 로고
    • Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers
    • 10.1038/nature07761 19242475
    • Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers. Lauren J, Gimbel DA, Nygaard HB, Gilbert JW, Strittmatter SM, Nature 2009 457 1128 1132 10.1038/nature07761 19242475
    • (2009) Nature , vol.457 , pp. 1128-1132
    • Lauren, J.1    Gimbel, D.A.2    Nygaard, H.B.3    Gilbert, J.W.4    Strittmatter, S.M.5
  • 69
    • 33845382759 scopus 로고    scopus 로고
    • Alpha2beta1 and alphaVbeta1 integrin signaling pathways mediate amyloid-beta-induced neurotoxicity
    • 10.1016/j.neurobiolaging.2005.12.002 16448724
    • Alpha2beta1 and alphaVbeta1 integrin signaling pathways mediate amyloid-beta-induced neurotoxicity. Wright S, Malinin NL, Powell KA, Yednock T, Rydel RE, Griswold-Prenner I, Neurobiol Aging 2007 28 226 237 10.1016/j.neurobiolaging.2005.12.002 16448724
    • (2007) Neurobiol Aging , vol.28 , pp. 226-237
    • Wright, S.1    Malinin, N.L.2    Powell, K.A.3    Yednock, T.4    Rydel, R.E.5    Griswold-Prenner, I.6
  • 70
    • 80755143595 scopus 로고    scopus 로고
    • Abeta inhibition of ionic conductance in mouse basal forebrain neurons is dependent upon the cellular prion protein PrPC
    • 10.1523/JNEUROSCI.4367-11.2011 22072680
    • Abeta inhibition of ionic conductance in mouse basal forebrain neurons is dependent upon the cellular prion protein PrPC. Alier K, Ma L, Yang J, Westaway D, Jhamandas JH, J Neurosci 2011 31 16292 16297 10.1523/JNEUROSCI.4367-11.2011 22072680
    • (2011) J Neurosci , vol.31 , pp. 16292-16297
    • Alier, K.1    Ma, L.2    Yang, J.3    Westaway, D.4    Jhamandas, J.H.5
  • 71
    • 0038278925 scopus 로고    scopus 로고
    • Human amylin actions on rat cholinergic basal forebrain neurons: Antagonism of beta-amyloid effects
    • 10.1152/jn.01138.2002 12611974
    • Human amylin actions on rat cholinergic basal forebrain neurons: antagonism of beta-amyloid effects. Jhamandas JH, Harris KH, Cho C, Fu W, MacTavish D, J Neurophysiol 2003 89 2923 2930 10.1152/jn.01138.2002 12611974
    • (2003) J Neurophysiol , vol.89 , pp. 2923-2930
    • Jhamandas, J.H.1    Harris, K.H.2    Cho, C.3    Fu, W.4    Mactavish, D.5
  • 72
    • 0034703047 scopus 로고    scopus 로고
    • Visualization of the calcitonin receptor-like receptor and its receptor activity-modifying proteins during internalization and recycling
    • 10.1074/jbc.M004534200 10882736
    • Visualization of the calcitonin receptor-like receptor and its receptor activity-modifying proteins during internalization and recycling. Kuwasako K, Shimekake Y, Masuda M, Nakahara K, Yoshida T, Kitaura M, Kitamura K, Eto T, Sakata T, J Biol Chem 2000 275 29602 29609 10.1074/jbc.M004534200 10882736
    • (2000) J Biol Chem , vol.275 , pp. 29602-29609
    • Kuwasako, K.1    Shimekake, Y.2    Masuda, M.3    Nakahara, K.4    Yoshida, T.5    Kitaura, M.6    Kitamura, K.7    Eto, T.8    Sakata, T.9
  • 73
    • 84861547526 scopus 로고    scopus 로고
    • Amyloid beta (Abeta) peptide directly activates amylin-3 receptor subtype by triggering multiple intracellular signaling pathways
    • 10.1074/jbc.M111.331181 22500019
    • Amyloid beta (Abeta) peptide directly activates amylin-3 receptor subtype by triggering multiple intracellular signaling pathways. Fu W, Ruangkittisakul A, MacTavish D, Shi JY, Ballanyi K, Jhamandas JH, J Biol Chem 2012 287 18820 18830 10.1074/jbc.M111.331181 22500019
    • (2012) J Biol Chem , vol.287 , pp. 18820-18830
    • Fu, W.1    Ruangkittisakul, A.2    Mactavish, D.3    Shi, J.Y.4    Ballanyi, K.5    Jhamandas, J.H.6
  • 74
    • 17844365264 scopus 로고    scopus 로고
    • Pharmacological discrimination of calcitonin receptor: Receptor activity-modifying protein complexes
    • 10.1124/mol.104.008615 15692146
    • Pharmacological discrimination of calcitonin receptor: receptor activity-modifying protein complexes. Hay DL, Christopoulos G, Christopoulos A, Poyner DR, Sexton PM, Mol Pharmacol 2005 67 1655 1665 10.1124/mol.104.008615 15692146
    • (2005) Mol Pharmacol , vol.67 , pp. 1655-1665
    • Hay, D.L.1    Christopoulos, G.2    Christopoulos, A.3    Poyner, D.R.4    Sexton, P.M.5
  • 75
    • 83655192092 scopus 로고    scopus 로고
    • Regulation of NMDA receptors by the tyrosine kinase Fyn
    • 10.1111/j.1742-4658.2011.08391.x 21985328
    • Regulation of NMDA receptors by the tyrosine kinase Fyn. Trepanier CH, Jackson MF, MacDonald JF, FEBS J 2012 279 12 19 10.1111/j.1742-4658.2011.08391.x 21985328
    • (2012) FEBS J , vol.279 , pp. 12-19
    • Trepanier, C.H.1    Jackson, M.F.2    Macdonald, J.F.3
  • 76
    • 82855161265 scopus 로고    scopus 로고
    • Src family kinases: Modulators of neurotransmitter receptor function and behavior
    • 10.1016/j.tins.2011.09.005 22051158
    • Src family kinases: modulators of neurotransmitter receptor function and behavior. Ohnishi H, Murata Y, Okazawa H, Matozaki T, Trends Neurosci 2011 34 629 637 10.1016/j.tins.2011.09.005 22051158
    • (2011) Trends Neurosci , vol.34 , pp. 629-637
    • Ohnishi, H.1    Murata, Y.2    Okazawa, H.3    Matozaki, T.4
  • 77
    • 0037025303 scopus 로고    scopus 로고
    • Striatal enriched phosphatase 61 dephosphorylates Fyn at phosphotyrosine 420
    • 10.1074/jbc.M111683200 11983687
    • Striatal enriched phosphatase 61 dephosphorylates Fyn at phosphotyrosine 420. Nguyen TH, Liu J, Lombroso PJ, J Biol Chem 2002 277 24274 24279 10.1074/jbc.M111683200 11983687
    • (2002) J Biol Chem , vol.277 , pp. 24274-24279
    • Nguyen, T.H.1    Liu, J.2    Lombroso, P.J.3
  • 79
    • 0028837693 scopus 로고
    • Regulation of the Src tyrosine kinase and Syp tyrosine phosphatase by their cellular association
    • 7478513
    • Regulation of the Src tyrosine kinase and Syp tyrosine phosphatase by their cellular association. Peng ZY, Cartwright CA, Oncogene 1995 11 1955 1962 7478513
    • (1995) Oncogene , vol.11 , pp. 1955-1962
    • Peng, Z.Y.1    Cartwright, C.A.2
  • 80
    • 83655167387 scopus 로고    scopus 로고
    • The regulation of N-methyl-D-aspartate receptors by Src kinase
    • 10.1111/j.1742-4658.2011.08413.x 22060915
    • The regulation of N-methyl-D-aspartate receptors by Src kinase. Groveman BR, Feng S, Fang XQ, Pflueger M, Lin SX, Bienkiewicz EA, Yu X, FEBS J 2012 279 20 28 10.1111/j.1742-4658.2011.08413.x 22060915
    • (2012) FEBS J , vol.279 , pp. 20-28
    • Groveman, B.R.1    Feng, S.2    Fang, X.Q.3    Pflueger, M.4    Lin, S.X.5    Bienkiewicz, E.A.6    Yu, X.7
  • 81
    • 0036469248 scopus 로고    scopus 로고
    • Process outgrowth of oligodendrocytes is promoted by interaction of fyn kinase with the cytoskeletal protein tau
    • 11826099
    • 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, J Neurosci 2002 22 698 707 11826099
    • (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
  • 83
    • 67651177571 scopus 로고    scopus 로고
    • An integrin-contactin complex regulates CNS myelination by differential Fyn phosphorylation
    • 10.1523/JNEUROSCI.5942-08.2009 19625508
    • An integrin-contactin complex regulates CNS myelination by differential Fyn phosphorylation. Laursen LS, Chan CW, ffrench-Constant C, J Neurosci 2009 29 9174 9185 10.1523/JNEUROSCI.5942-08.2009 19625508
    • (2009) J Neurosci , vol.29 , pp. 9174-9185
    • Laursen, L.S.1    Chan, C.W.2    Ffrench-Constant, C.3
  • 84
    • 79953161516 scopus 로고    scopus 로고
    • Fyn mediates transforming growth factor-beta1-induced down-regulation of E-cadherin in human A549 lung cancer cells
    • 10.1016/j.bbrc.2011.02.134 21371426
    • Fyn mediates transforming growth factor-beta1-induced down-regulation of E-cadherin in human A549 lung cancer cells. Kim AN, Jeon WK, Lim KH, Lee HY, Kim WJ, Kim BC, Biochem Biophys Res Commun 2011 407 181 184 10.1016/j.bbrc.2011.02. 134 21371426
    • (2011) Biochem Biophys Res Commun , vol.407 , pp. 181-184
    • Kim, A.N.1    Jeon, W.K.2    Lim, K.H.3    Lee, H.Y.4    Kim, W.J.5    Kim, B.C.6
  • 85
    • 84862001756 scopus 로고    scopus 로고
    • Reduced surface expression of epithelial E-cadherin evoked by interferon-gamma is Fyn kinase-dependent
    • 10.1371/journal.pone.0038441 22715382
    • Reduced surface expression of epithelial E-cadherin evoked by interferon-gamma is Fyn kinase-dependent. Smyth D, Leung G, Fernando M, McKay DM, PLoS One 2012 7 38441 10.1371/journal.pone.0038441 22715382
    • (2012) PLoS One , vol.7 , pp. 538441
    • Smyth, D.1    Leung, G.2    Fernando, M.3    McKay, D.M.4
  • 87
    • 77950251072 scopus 로고    scopus 로고
    • Fyn: A novel molecular target in cancer
    • 10.1002/cncr.24879 20151426
    • Fyn: a novel molecular target in cancer. Saito YD, Jensen AR, Salgia R, Posadas EM, Cancer 2010 116 1629 1637 10.1002/cncr.24879 20151426
    • (2010) Cancer , vol.116 , pp. 1629-1637
    • Saito, Y.D.1    Jensen, A.R.2    Salgia, R.3    Posadas, E.M.4
  • 89
    • 0038933866 scopus 로고    scopus 로고
    • Compartmentation of Fyn kinase with glycosylphosphatidylinositol-anchored molecules in oligodendrocytes facilitates kinase activation during myelination
    • 10.1074/jbc.274.41.29042 10506155
    • Compartmentation of Fyn kinase with glycosylphosphatidylinositol-anchored molecules in oligodendrocytes facilitates kinase activation during myelination. Kramer EM, Klein C, Koch T, Boytinck M, Trotter J, J Biol Chem 1999 274 29042 29049 10.1074/jbc.274.41.29042 10506155
    • (1999) J Biol Chem , vol.274 , pp. 29042-29049
    • Kramer, E.M.1    Klein, C.2    Koch, T.3    Boytinck, M.4    Trotter, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.