메뉴 건너뛰기




Volumn 23, Issue 25, 2014, Pages 6732-6745

The small GTPase Rab11 co-localizes with α-synuclein in intracellular inclusions and modulates its aggregation, secretion and toxicity

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SYNUCLEIN; HYBRID PROTEIN; PROTEIN AGGREGATE; PROTEIN BINDING; RAB PROTEIN; RAB11 PROTEIN; SMALL INTERFERING RNA;

EID: 85005916286     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddu391     Document Type: Article
Times cited : (71)

References (55)
  • 1
    • 0023722437 scopus 로고
    • Synuclein: a neuron-specific protein localized to the nucleus and presynaptic nerve terminal
    • Maroteaux, L., Campanelli, J.T. and Scheller, R.H. (1988) Synuclein: a neuron-specific protein localized to the nucleus and presynaptic nerve terminal. J. Neurosci., 8, 2804–2815.
    • (1988) J. Neurosci , vol.8 , pp. 2804-2815
    • Maroteaux, L.1    Campanelli, J.T.2    Scheller, R.H.3
  • 2
    • 0032584686 scopus 로고    scopus 로고
    • Filamentous alpha-synuclein inclusions link multiple system atrophy with Parkinson’s disease and dementia with Lewy bodies
    • Spillantini, M.G., Crowther, R.A., Jakes, R., Cairns, N.J., Lantos, P.L. and Goedert, M. (1998) Filamentous alpha-synuclein inclusions link multiple system atrophy with Parkinson’s disease and dementia with Lewy bodies. Neurosci. Lett., 251, 205–208.
    • (1998) Neurosci. Lett , vol.251 , pp. 205-208
    • Spillantini, M.G.1    Crowther, R.A.2    Jakes, R.3    Cairns, N.J.4    Lantos, P.L.5    Goedert, M.6
  • 3
    • 0032568534 scopus 로고    scopus 로고
    • alpha-Synuclein in filamentous inclusions of Lewy bodies from Parkinson’s disease and dementia with lewy bodies
    • Spillantini, M.G., Crowther, R.A., Jakes, R., Hasegawa, M. and Goedert, M. (1998) alpha-Synuclein in filamentous inclusions of Lewy bodies from Parkinson’s disease and dementia with lewy bodies. Proc. Natl Acad. Sci. USA, 95, 6469 – 6473.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 6469-6473
    • Spillantini, M.G.1    Crowther, R.A.2    Jakes, R.3    Hasegawa, M.4    Goedert, M.5
  • 5
    • 84864870837 scopus 로고    scopus 로고
    • Alpha-synuclein: from secretion to dysfunction and death
    • Marques, O. and Outeiro, T.F. (2012) Alpha-synuclein: from secretion to dysfunction and death. Cell Death Dis., 3, e350.
    • (2012) Cell Death Dis , vol.3 , pp. e350
    • Marques, O.1    Outeiro, T.F.2
  • 6
    • 84875415994 scopus 로고    scopus 로고
    • alpha-Synuclein oligomers and clinical implications for Parkinson disease
    • Kalia, L.V., Kalia, S.K., McLean, P.J., Lozano, A.M. and Lang, A.E. (2013) alpha-Synuclein oligomers and clinical implications for Parkinson disease. Ann. Neurol., 73, 155 – 169.
    • (2013) Ann. Neurol , vol.73 , pp. 155-169
    • Kalia, L.V.1    Kalia, S.K.2    McLean, P.J.3    Lozano, A.M.4    Lang, A.E.5
  • 7
    • 0032540327 scopus 로고    scopus 로고
    • Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes
    • Davidson, W.S., Jonas, A., Clayton, D.F. and George, J.M. (1998) Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes. J. Biol. Chem., 273, 9443–9449.
    • (1998) J. Biol. Chem , vol.273 , pp. 9443-9449
    • Davidson, W.S.1    Jonas, A.2    Clayton, D.F.3    George, J.M.4
  • 8
  • 13
    • 21344456506 scopus 로고    scopus 로고
    • Intravesicular localization and exocytosis of alpha-synuclein and its aggregates
    • Lee, H.J., Patel, S. and Lee, S.J. (2005) Intravesicular localization and exocytosis of alpha-synuclein and its aggregates. J. Neurosci., 25, 6016–6024.
    • (2005) J. Neurosci , vol.25 , pp. 6016-6024
    • Lee, H.J.1    Patel, S.2    Lee, S.J.3
  • 14
    • 79251565507 scopus 로고    scopus 로고
    • Heat-shock protein 70 modulates toxic extracellular alpha-synuclein oligomers and rescues trans-synaptic toxicity
    • Danzer, K.M., Ruf, W.P., Putcha, P., Joyner, D., Hashimoto, T., Glabe, C., Hyman, B.T. and McLean, P.J. (2011) Heat-shock protein 70 modulates toxic extracellular alpha-synuclein oligomers and rescues trans-synaptic toxicity. FASEB J., 25, 326–336.
    • (2011) FASEB J , vol.25 , pp. 326-336
    • Danzer, K.M.1    Ruf, W.P.2    Putcha, P.3    Joyner, D.4    Hashimoto, T.5    Glabe, C.6    Hyman, B.T.7    McLean, P.J.8
  • 18
    • 33748932543 scopus 로고    scopus 로고
    • The plasma alpha-synuclein levels in patients with Parkinson’s disease and multiple system atrophy
    • Lee, P.H., Lee, G., Park, H.J., Bang, O.Y., Joo, I.S. and Huh, K. (2006) The plasma alpha-synuclein levels in patients with Parkinson’s disease and multiple system atrophy. J. Neural Transm., 113, 1435–1439.
    • (2006) J. Neural Transm , vol.113 , pp. 1435-1439
    • Lee, P.H.1    Lee, G.2    Park, H.J.3    Bang, O.Y.4    Joo, I.S.5    Huh, K.6
  • 20
    • 77951885732 scopus 로고    scopus 로고
    • Non-classical exocytosis of alpha-synuclein is sensitive to folding states and promoted under stress conditions
    • Jang, A., Lee, H.J., Suk, J.E., Jung, J.W., Kim, K.P. and Lee, S.J. (2010) Non-classical exocytosis of alpha-synuclein is sensitive to folding states and promoted under stress conditions. J. Neurochem., 113, 1263 – 1274.
    • (2010) J. Neurochem , vol.113 , pp. 1263-1274
    • Jang, A.1    Lee, H.J.2    Suk, J.E.3    Jung, J.W.4    Kim, K.P.5    Lee, S.J.6
  • 25
    • 70349223775 scopus 로고    scopus 로고
    • Seeding induced by alpha-synuclein oligomers provides evidence for spreading of alpha-synuclein pathology
    • Danzer, K.M., Krebs, S.K., Wolff, M., Birk, G. and Hengerer, B. (2009) Seeding induced by alpha-synuclein oligomers provides evidence for spreading of alpha-synuclein pathology. J. Neurochem., 111, 192–203.
    • (2009) J. Neurochem , vol.111 , pp. 192-203
    • Danzer, K.M.1    Krebs, S.K.2    Wolff, M.3    Birk, G.4    Hengerer, B.5
  • 26
    • 0023789193 scopus 로고
    • Reactive microglia are positive for HLA-DR in the substantia nigra of Parkinson’s and Alzheimer’s disease brains
    • McGeer, P.L., Itagaki, S., Boyes, B.E. and McGeer, E.G. (1988) Reactive microglia are positive for HLA-DR in the substantia nigra of Parkinson’s and Alzheimer’s disease brains. Neurology, 38, 1285 – 1291.
    • (1988) Neurology , vol.38 , pp. 1285-1291
    • McGeer, P.L.1    Itagaki, S.2    Boyes, B.E.3    McGeer, E.G.4
  • 27
    • 27344438938 scopus 로고    scopus 로고
    • Microglial inflammation in the parkinsonian substantia nigra: relationship to alpha-synuclein deposition
    • Croisier, E., Moran, L.B., Dexter, D.T., Pearce, R.K. and Graeber, M.B. (2005) Microglial inflammation in the parkinsonian substantia nigra: relationship to alpha-synuclein deposition. J. Neuroinflamm., 2, 14.
    • (2005) J. Neuroinflamm , vol.2 , pp. 14
    • Croisier, E.1    Moran, L.B.2    Dexter, D.T.3    Pearce, R.K.4    Graeber, M.B.5
  • 28
    • 18844374851 scopus 로고    scopus 로고
    • Neuroinflammatory processes in Parkinson’s disease
    • (Suppl. 1)
    • Hirsch, E.C., Hunot, S. and Hartmann, A. (2005) Neuroinflammatory processes in Parkinson’s disease. Parkinsonism Relat. Disord., 11(Suppl. 1), S9 – S15.
    • (2005) Parkinsonism Relat. Disord , vol.11 , pp. S9-S15
    • Hirsch, E.C.1    Hunot, S.2    Hartmann, A.3
  • 29
    • 84876461130 scopus 로고    scopus 로고
    • Regulation of G protein-coupled receptor trafficking and signaling by Rab GTPases
    • Esseltine, J.L. and Ferguson, S.S. (2013) Regulation of G protein-coupled receptor trafficking and signaling by Rab GTPases. Small GTPases, 4, 132–135.
    • (2013) Small GTPases , vol.4 , pp. 132-135
    • Esseltine, J.L.1    Ferguson, S.S.2
  • 30
    • 68049105101 scopus 로고    scopus 로고
    • Rab GTPases as coordinators of vesicle traffic
    • Stenmark, H. (2009) Rab GTPases as coordinators of vesicle traffic. Nat. Rev. Mol. Cell Biol., 10, 513–525.
    • (2009) Nat. Rev. Mol. Cell Biol , vol.10 , pp. 513-525
    • Stenmark, H.1
  • 31
    • 0027370762 scopus 로고
    • Rab11, a small GTPase associated with both constitutive and regulated secretory pathways in PC12 cells
    • Urbe, S., Huber, L.A., Zerial, M., Tooze, S.A. and Parton, R.G. (1993) Rab11, a small GTPase associated with both constitutive and regulated secretory pathways in PC12 cells. FEBS Lett., 334, 175–182.
    • (1993) FEBS Lett , vol.334 , pp. 175-182
    • Urbe, S.1    Huber, L.A.2    Zerial, M.3    Tooze, S.A.4    Parton, R.G.5
  • 32
    • 0029850677 scopus 로고    scopus 로고
    • Rab11 regulates recycling through the pericentriolar recycling endosome
    • Ullrich, O., Reinsch, S., Urbe, S., Zerial, M. and Parton, R.G. (1996) Rab11 regulates recycling through the pericentriolar recycling endosome. J. Cell Biol., 135, 913 – 924.
    • (1996) J. Cell Biol , vol.135 , pp. 913-924
    • Ullrich, O.1    Reinsch, S.2    Urbe, S.3    Zerial, M.4    Parton, R.G.5
  • 33
    • 0034638828 scopus 로고    scopus 로고
    • Rab11 regulates the compartmentalization of early endosomes required for efficient transport from early endosomes to the trans-golgi network
    • Wilcke, M., Johannes, L., Galli, T., Mayau, V., Goud, B. and Salamero, J. (2000) Rab11 regulates the compartmentalization of early endosomes required for efficient transport from early endosomes to the trans-golgi network. J. Cell Biol., 151, 1207–1220.
    • (2000) J. Cell Biol , vol.151 , pp. 1207-1220
    • Wilcke, M.1    Johannes, L.2    Galli, T.3    Mayau, V.4    Goud, B.5    Salamero, J.6
  • 34
    • 84866050788 scopus 로고    scopus 로고
    • Secretion of soluble vascular endothelial growth factor receptor 1 (sVEGFR1/sFlt1) requires Arf1, Arf6, and Rab11 GTPases
    • Jung, J.J., Tiwari, A., Inamdar, S.M., Thomas, C.P., Goel, A. and Choudhury, A. (2012) Secretion of soluble vascular endothelial growth factor receptor 1 (sVEGFR1/sFlt1) requires Arf1, Arf6, and Rab11 GTPases. PloS ONE, 7, e44572.
    • (2012) PloS ONE , vol.7 , pp. e44572
    • Jung, J.J.1    Tiwari, A.2    Inamdar, S.M.3    Thomas, C.P.4    Goel, A.5    Choudhury, A.6
  • 35
    • 0344011457 scopus 로고    scopus 로고
    • Divergent functions of neuronal Rab11b in Ca2+-regulated versus constitutive exocytosis
    • Khvotchev, M.V., Ren, M., Takamori, S., Jahn, R. and Sudhof, T.C. (2003) Divergent functions of neuronal Rab11b in Ca2+-regulated versus constitutive exocytosis. J. Neurosci., 23, 10531–10539.
    • (2003) J. Neurosci , vol.23 , pp. 10531-10539
    • Khvotchev, M.V.1    Ren, M.2    Takamori, S.3    Jahn, R.4    Sudhof, T.C.5
  • 36
    • 63349087876 scopus 로고    scopus 로고
    • Rab11 and its effector Rip11 participate in regulation of insulin granule exocytosis
    • Sugawara, K., Shibasaki, T., Mizoguchi, A., Saito, T. and Seino, S. (2009) Rab11 and its effector Rip11 participate in regulation of insulin granule exocytosis. Genes Cells, 14, 445–456.
    • (2009) Genes Cells , vol.14 , pp. 445-456
    • Sugawara, K.1    Shibasaki, T.2    Mizoguchi, A.3    Saito, T.4    Seino, S.5
  • 37
    • 0037096162 scopus 로고    scopus 로고
    • The exosome pathway in K562 cells is regulated by Rab11
    • Savina, A., Vidal, M. and Colombo, M.I. (2002) The exosome pathway in K562 cells is regulated by Rab11. J. Cell Sci., 115, 2505–2515.
    • (2002) J. Cell Sci , vol.115 , pp. 2505-2515
    • Savina, A.1    Vidal, M.2    Colombo, M.I.3
  • 42
    • 84863518971 scopus 로고    scopus 로고
    • Rab11 rescues synaptic dysfunction and behavioural deficits in a Drosophila model of Huntington’s disease
    • Steinert, J.R., Campesan, S., Richards, P., Kyriacou, C.P., Forsythe, I.D. and Giorgini, F. (2012) Rab11 rescues synaptic dysfunction and behavioural deficits in a Drosophila model of Huntington’s disease. Hum. Mol. Genet., 21, 2912 – 2922.
    • (2012) Hum. Mol. Genet , vol.21 , pp. 2912-2922
    • Steinert, J.R.1    Campesan, S.2    Richards, P.3    Kyriacou, C.P.4    Forsythe, I.D.5    Giorgini, F.6
  • 43
    • 77950682093 scopus 로고    scopus 로고
    • Aberrant Rab11-dependent trafficking of the neuronal glutamate transporter EAAC1 causes oxidative stress and cell death in Huntington’s disease
    • Li, X., Valencia, A., Sapp, E., Masso, N., Alexander, J., Reeves, P., Kegel, K.B., Aronin, N. and Difiglia, M. (2010) Aberrant Rab11-dependent trafficking of the neuronal glutamate transporter EAAC1 causes oxidative stress and cell death in Huntington’s disease. J. Neurosci., 30, 4552–4561.
    • (2010) J. Neurosci , vol.30 , pp. 4552-4561
    • Li, X.1    Valencia, A.2    Sapp, E.3    Masso, N.4    Alexander, J.5    Reeves, P.6    Kegel, K.B.7    Aronin, N.8    Difiglia, M.9
  • 44
    • 65549102934 scopus 로고    scopus 로고
    • Inducible over-expression of wild type alpha-synuclein in human neuronal cells leads to caspase-dependent non-apoptotic death
    • Vekrellis, K., Xilouri, M., Emmanouilidou, E. and Stefanis, L. (2009) Inducible over-expression of wild type alpha-synuclein in human neuronal cells leads to caspase-dependent non-apoptotic death. J. Neurochem., 109, 1348–1362.
    • (2009) J. Neurochem , vol.109 , pp. 1348-1362
    • Vekrellis, K.1    Xilouri, M.2    Emmanouilidou, E.3    Stefanis, L.4
  • 45
    • 0021073678 scopus 로고
    • Sorting and recycling of cell surface receptors and endocytosed ligands: the asialoglycoprotein and transferrin receptors
    • Ciechanover, A., Schwartz, A.L. and Lodish, H.F. (1983) Sorting and recycling of cell surface receptors and endocytosed ligands: the asialoglycoprotein and transferrin receptors. J. Cell Biochem., 23, 107 – 130.
    • (1983) J. Cell Biochem , vol.23 , pp. 107-130
    • Ciechanover, A.1    Schwartz, A.L.2    Lodish, H.F.3
  • 48
    • 84874377202 scopus 로고    scopus 로고
    • Extracellular vesicles: exosomes, microvesicles, and friends
    • Raposo, G. and Stoorvogel, W. (2013) Extracellular vesicles: exosomes, microvesicles, and friends. J. Cell Biol., 200, 373–383.
    • (2013) J. Cell Biol , vol.200 , pp. 373-383
    • Raposo, G.1    Stoorvogel, W.2
  • 49
    • 0035859226 scopus 로고    scopus 로고
    • Alpha-synuclein-enhanced green fluorescent protein fusion proteins form proteasome sensitive inclusions in primary neurons
    • McLean, P.J., Kawamata, H. and Hyman, B.T. (2001) Alpha-synuclein-enhanced green fluorescent protein fusion proteins form proteasome sensitive inclusions in primary neurons. Neuroscience, 104, 901–912.
    • (2001) Neuroscience , vol.104 , pp. 901-912
    • McLean, P.J.1    Kawamata, H.2    Hyman, B.T.3
  • 53
    • 84875275175 scopus 로고    scopus 로고
    • Arrivals and departures at the plasma membrane: direct and indirect transport routes
    • Prydz, K., Tveit, H., Vedeler, A. and Saraste, J. (2013) Arrivals and departures at the plasma membrane: direct and indirect transport routes. Cell Tissue Res., 352, 5 – 20.
    • (2013) Cell Tissue Res , vol.352 , pp. 5-20
    • Prydz, K.1    Tveit, H.2    Vedeler, A.3    Saraste, J.4
  • 54
    • 84881147729 scopus 로고    scopus 로고
    • Autophagic failure promotes the exocytosis and intercellular transfer of alpha-synuclein
    • Lee, H.J., Cho, E.D., Lee, K.W., Kim, J.H., Cho, S.G. and Lee, S.J. (2013) Autophagic failure promotes the exocytosis and intercellular transfer of alpha-synuclein. Exp. Mol. Med., 45, e22.
    • (2013) Exp. Mol. Med , vol.45 , pp. e22
    • Lee, H.J.1    Cho, E.D.2    Lee, K.W.3    Kim, J.H.4    Cho, S.G.5    Lee, S.J.6
  • 55
    • 33846817163 scopus 로고    scopus 로고
    • Relationships between the sequence of alpha-synuclein and its membrane affinity, fibrillization propensity, and yeast toxicity
    • Volles, M.J. and Lansbury, P.T. Jr (2007) Relationships between the sequence of alpha-synuclein and its membrane affinity, fibrillization propensity, and yeast toxicity. J. Mol. Biol., 366, 1510–1522.
    • (2007) J. Mol. Biol , vol.366 , pp. 1510-1522
    • Volles, M.J.1    Lansbury, P.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.