메뉴 건너뛰기




Volumn 43, Issue 3, 2011, Pages 391-405

Aggregation of α-synuclein in S. cerevisiae is associated with defects in endosomal trafficking and phospholipid biosynthesis

Author keywords

Alpha synuclein; Neurodegenerative disease; Parkinson's disease; Rab GTPase; Vesicle trafficking; Yeast

Indexed keywords

ALPHA SYNUCLEIN; GUANOSINE TRIPHOSPHATASE; PHOSPHATIDIC ACID; PHOSPHOLIPID; RAB PROTEIN;

EID: 79953846844     PISSN: 08958696     EISSN: None     Source Type: Journal    
DOI: 10.1007/s12031-010-9455-5     Document Type: Article
Times cited : (67)

References (92)
  • 1
    • 0033231275 scopus 로고    scopus 로고
    • Cytoplasm to vacuole trafficking of aminopeptidase I requires a t-SNARE-Sec1p complex composed of Tlg2p and Vps45p
    • DOI 10.1093/emboj/18.21.6005
    • Abeliovich H, Darsow T, Emr SD (1999) Cytoplasm to vacuole trafficking of aminopeptidase I requires a t-SNARE-Sec1p complex composed of Tlg2p and Vps45p. EMBO J 18:6005-6016 (Pubitemid 29515677)
    • (1999) EMBO Journal , vol.18 , Issue.21 , pp. 6005-6016
    • Abeliovich, H.1    Darsow, T.2    Emr, S.D.3
  • 3
    • 0033584946 scopus 로고    scopus 로고
    • Two new members of a family of Ypt/Rab GTPase activating proteins: Promiscuity of substrate recognition
    • Albert S, Gallwitz D (1999) Two new members of a family of Ypt/Rab GTPase activating proteins - promiscuity of substrate recognition. J Biol Chem 274:33186-33189 (Pubitemid 129511611)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.47 , pp. 33186-33189
    • Albert, S.1    Gallwitz, D.2
  • 4
    • 0025094319 scopus 로고
    • An essential role for a phospholipid transfer protein in yeast Golgi function
    • Bankaitis VA, Aitken JR, Cleves AE, Dowhan W (1990) An essential role for a phospholipid transfer protein in yeast Golgi function. Nature 347:561-562
    • (1990) Nature , vol.347 , pp. 561-562
    • Bankaitis, V.A.1    Aitken, J.R.2    Cleves, A.E.3    Dowhan, W.4
  • 5
    • 0029804680 scopus 로고    scopus 로고
    • Two GTPase isoforms, Ypt31p and Ypt32p, are essential for Golgi function in yeast
    • Benli M, Doring F, Robinson DG, Yang XP, Gallwitz D (1996) Two GTPase isoforms, ypt31p and ypt32p, are essential for Golgi function in yeast. EMBO J 15:6460-6475 (Pubitemid 26413779)
    • (1996) EMBO Journal , vol.15 , Issue.23 , pp. 6460-6475
    • Benli, M.1    Doring, F.2    Robinson, D.G.3    Yang, X.4    Gallwitz, D.5
  • 6
    • 0033638350 scopus 로고    scopus 로고
    • The sodium/proton exchanger Nhx1p is required for endosomal protein trafficking in the yeast Saccharomyces cerevisiae
    • Bowers K, Levi BP, Patel FI, Stevens TH (2000) The sodium/proton exchanger Nhx1p is required for endosomal protein trafficking in the yeast Saccharomyces cerevisiae. Mol Biol Cell 11:4277-4294
    • (2000) Mol Biol Cell , vol.11 , pp. 4277-4294
    • Bowers, K.1    Levi, B.P.2    Patel, F.I.3    Stevens, T.H.4
  • 7
    • 0032579440 scopus 로고    scopus 로고
    • Designer deletion strains derived from Saccharomyces cerevisiae S288C: A useful set of strains and plasmids for PCR-mediated gene disruption and other applications
    • DOI 10.1002/(SICI)1097-0061(19980130)14:2<115::AID-YEA204>3.0.CO;2- 2
    • Brachmann CB, Davies A, Cost GJ, Caputo E, Li JC, Hieter P, Boeke JD (1998) Designer deletion strains derived from Saccharomyces cerevisiae S288C: a useful set of strains and plasmids for PCR-mediated gene disruption and other applications. Yeast 14:115-132 (Pubitemid 28062863)
    • (1998) Yeast , vol.14 , Issue.2 , pp. 115-132
    • Brachmann, C.B.1    Davies, A.2    Cost, G.J.3    Caputo, E.4    Li, J.5    Hieter, P.6    Boeke, J.D.7
  • 10
    • 27544507306 scopus 로고    scopus 로고
    • α-Synuclein cooperates with CSPalpha in preventing neurodegeneration
    • DOI 10.1016/j.cell.2005.09.028, PII S0092867405010226
    • Chandra S, Gallardo G, Fernandez-Chacon R, Schluter OM, Sudhof TC (2005) α-synuclein cooperates with CSP alpha in preventing neurodegeneration. Cell 123:383-396 (Pubitemid 41546670)
    • (2005) Cell , vol.123 , Issue.3 , pp. 383-396
    • Chandra, S.1    Gallardo, G.2    Fernandez-Chacon, R.3    Schluter, O.M.4    Sudhof, T.C.5
  • 12
    • 0026073075 scopus 로고
    • Mutations in the CDP-choline pathway for phospholipid biosynthesis bypass the requirement for an essential phospholipid transfer protein
    • Cleves AE, Mcgee TP, Whitters EA, Champion KM, Aitken JR, Dowhan W, Goebl M, Bankaitis VA (1991) Mutations in the Cdp choline pathway for phospholipid biosynthesis bypass the requirement for an essential phospholipid transfer protein. Cell 64:789-800 (Pubitemid 121001166)
    • (1991) Cell , vol.64 , Issue.4 , pp. 789-800
    • Cleves, A.E.1    McGee, T.P.2    Whitters, E.A.3    Champion, K.M.4    Aitken, J.R.5    Dowhan, W.6    Goebl, M.7    Bankaitis, V.A.8
  • 13
    • 0032837425 scopus 로고    scopus 로고
    • A role for Tlg1p in the transport of proteins within the Golgi apparatus of Saccharomyces cerevisiae
    • Coe JGS, Lim ACB, Xu J, Hong WJ (1999) A role for Tlg1p in the transport of proteins within the Golgi apparatus of Saccharomyces cerevisiae. Mol Biol Cell 10:2407-2423 (Pubitemid 29343143)
    • (1999) Molecular Biology of the Cell , vol.10 , Issue.7 , pp. 2407-2423
    • Coe, J.G.S.1    Lim, A.C.B.2    Xu, J.3    Hong, W.4
  • 14
    • 0031787871 scopus 로고    scopus 로고
    • Accelerated in vitro fibril formation by a mutant α-synuclein linked to early-onset Parkinson disease
    • DOI 10.1038/3311
    • Conway KA, Harper JD, Lansbury PT (1998) Accelerated in vitro fibril formation by a mutant α-synuclein linked to early-onset Parkinson disease. Nat Med 4:1318-1320 (Pubitemid 28512115)
    • (1998) Nature Medicine , vol.4 , Issue.11 , pp. 1318-1320
    • Conway, K.A.1    Harper, J.D.2    Lansbury, P.T.3
  • 17
    • 0032540327 scopus 로고    scopus 로고
    • Stabilization of α-Synuclein secondary structure upon binding to synthetic membranes
    • DOI 10.1074/jbc.273.16.9443
    • Davidson WS, Jonas A, Clayton DF, George JM (1998) Stabilization of α-synuclein secondary structure upon binding to synthetic membranes. J Biol Chem 273:9443-9449 (Pubitemid 28183026)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.16 , pp. 9443-9449
    • Davidson, W.S.1    Jonas, A.2    Clayton, D.F.3    George, J.M.4
  • 18
    • 0037175026 scopus 로고    scopus 로고
    • Significance of GTP hydrolysis in Ypt1p-regulated endoplasmic reticulum to Golgi transport revealed by the analysis of two novel Ypt1-GAPs
    • DOI 10.1074/jbc.M205783200
    • De Antoni A, Schmitzova J, Trepte HH, Gallwitz D, Albert S (2002) Significance of GTP hydrolysis in Ypt1p-regulated endoplasmic reticulum to Golgi transport revealed by the analysis of two novel Ypt1-GAPs. J Biol Chem 277:41023-41031 (Pubitemid 35215692)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.43 , pp. 41023-41031
    • De Antoni, A.1    Schmitzova, J.2    Trepte, H.-H.3    Gallwitz, D.4    Albert, S.5
  • 19
    • 84937088414 scopus 로고
    • Phase and electron microscopic observations of Lewy bodies and Melanin granules in substantia Nigra and Locus Caeruleus in Parkinsons Disease
    • Duffy PE, Tennyson VM (1965) Phase and electron microscopic observations of Lewy bodies and Melanin granules in substantia Nigra and Locus Caeruleus in Parkinsons Disease. J Neuropathol Exp Neurol 24:398
    • (1965) J Neuropathol Exp Neurol , vol.24 , pp. 398
    • Duffy, P.E.1    Tennyson, V.M.2
  • 20
    • 0029803610 scopus 로고    scopus 로고
    • Kes1p shares homology with human oxysterol binding protein and participates in a novel regulatory pathway for yeast Golgi-derived transport vesicle biogenesis
    • Fang M, Kearns BG, Gedvilaite A, Kagiwada S, Kearns M, Fung MKY, Bankaitis VA (1996) Kes1p shares homology with human oxysterol binding protein and participates in a novel regulatory pathway for yeast Golgi-derived transport vesicle biogenesis. EMBO J 15:6447-6459 (Pubitemid 26413778)
    • (1996) EMBO Journal , vol.15 , Issue.23 , pp. 6447-6459
    • Fang, M.1    Kearns, B.G.2    Gedvilaite, A.3    Kagiwada, S.4    Kearns, M.5    Fung, M.K.Y.6    Bankaitis, V.A.7
  • 21
    • 0017288256 scopus 로고
    • Ultrastructure of Lewy bodies in stellate ganglion
    • Forno LS, Norville RL (1976) Ultrastructure of Lewy bodies in stellate ganglion. Acta Neuropathol 34:183-197
    • (1976) Acta Neuropathol , vol.34 , pp. 183-197
    • Forno, L.S.1    Norville, R.L.2
  • 22
    • 0025133327 scopus 로고
    • The 31-Kda polypeptide is an essential subunit of the vacuolar atpase in Saccharomyces cerevisiae
    • Foury F (1990) The 31-Kda polypeptide is an essential subunit of the vacuolar atpase in Saccharomyces cerevisiae. J Biol Chem 265:18554-18560
    • (1990) J Biol Chem , vol.265 , pp. 18554-18560
    • Foury, F.1
  • 24
    • 0035109738 scopus 로고    scopus 로고
    • Synucleinopathies- Clinical and pathological implications
    • Galvin JE, Lee VMY, Trojanowski JQ (2001) Synucleinopathies- Clinical and pathological implications. Arch Neurol 58:186-190
    • (2001) Arch Neurol , vol.58 , pp. 186-190
    • Galvin, J.E.1    Lee, V.M.Y.2    Trojanowski, J.Q.3
  • 25
    • 0033583215 scopus 로고    scopus 로고
    • Mutant and wild type human α-synucleins assemble into elongated filaments with distinct morphologies in vitro
    • Giasson BI, Uryu K, Trojanowski JQ, Lee VMY (1999) Mutant and wild type human α-synucleins assemble into elongated filaments with distinct morphologies in vitro. J Biol Chem 274:7619-7622
    • (1999) J Biol Chem , vol.274 , pp. 7619-7622
    • Giasson, B.I.1    Uryu, K.2    Trojanowski, J.Q.3    Lee, V.M.Y.4
  • 26
    • 0034651575 scopus 로고    scopus 로고
    • A panel of epitope-specific antibodies detects protein domains distributed throughout human α-synuclein in Lewy bodies of Parkinson's disease
    • DOI 10.1002/(SICI)1097-4547(20000215)59:4<528::AID-JNR8>3.0.CO;2-0
    • Giasson BI, Jakes R, Goedert M, Duda JE, Leight S, Trojanowski JQ, Lee VMY (2000) A panel of epitope-specific antibodies detects protein domains distributed throughout human α-synuclein in Lewy bodies of Parkinson's disease. J Neurosci Res 59:528-533 (Pubitemid 30090580)
    • (2000) Journal of Neuroscience Research , vol.59 , Issue.4 , pp. 528-533
    • Giasson, B.I.1    Jakes, R.2    Goedert, M.3    Duda, J.E.4    Leight, S.5    Trojanowski, J.Q.6    Lee, V.M.Y.7
  • 27
    • 0037118259 scopus 로고    scopus 로고
    • Neuronal α-synucleinopathy with severe movement disorder in mice expressing A53T human α-synuclein
    • DOI 10.1016/S0896-6273(02)00682-7
    • Giasson BI, Duda JE, Quinn SM, Zhang B, Trojanowski JQ, Lee VMY (2002) Neuronal α-synucleinopathy with severe movement disorder in mice expressing A53T human α-synuclein. Neuron 34:521-533 (Pubitemid 34628750)
    • (2002) Neuron , vol.34 , Issue.4 , pp. 521-533
    • Giasson, B.I.1    Duda, J.E.2    Quinn, S.M.3    Zhang, B.4    Trojanowski, J.Q.5    Lee, V.M.-Y.6
  • 28
    • 0030773139 scopus 로고    scopus 로고
    • Identification of proteins that interact with a protein of interest: Applications of the yeast two-hybrid system
    • DOI 10.1023/A:1006859319926
    • Gietz RD, TriggsRaine B, Robbins A, Graham KC, Woods RA (1997) Identification of proteins that interact with a protein of interest: applications of the yeast two-hybrid system. Mol Cell Biochem 172:67-79 (Pubitemid 27374575)
    • (1997) Molecular and Cellular Biochemistry , vol.172 , Issue.1-2 , pp. 67-79
    • Gietz, R.D.1    Triggs-Raine, B.2    Robbins, A.3    Graham, K.C.4    Woods, R.A.5
  • 31
    • 0033638861 scopus 로고    scopus 로고
    • A snc1 endocytosis mutant: Phenotypic analysis and suppression by overproduction of dihydrosphingosine phosphate lyase
    • Grote E, Vlacich G, Pypaert M, Novick PJ (2000) A snc1 endocytosis mutant: phenotypic analysis and suppression by overproduction of dihydrosphingosine phosphate lyase. Mol Biol Cell 11:4051-4065
    • (2000) Mol Biol Cell , vol.11 , pp. 4051-4065
    • Grote, E.1    Vlacich, G.2    Pypaert, M.3    Novick, P.J.4
  • 32
    • 0033558093 scopus 로고    scopus 로고
    • The exocyst is an effector for Sec4P, targeting secretory vesicles to sites of exocytosis
    • DOI 10.1093/emboj/18.4.1071
    • Guo W, Roth D, Walch-Solimena C, Novick P (1999) The exocyst is an effector for Sec4p, targeting secretory vesicles to sites of exocytosis. EMBO J 18:1071-1080 (Pubitemid 29082285)
    • (1999) EMBO Journal , vol.18 , Issue.4 , pp. 1071-1080
    • Guo, G.1    Roth, D.2    Walch-Solimena, C.3    Novick, P.4
  • 33
    • 0027538111 scopus 로고
    • An early cytoplasmic change before Lewy body maturation: An ultrastructural study of the substantia nigra from an autopsy case of juvenile parkinsonism
    • Hayashida K, Oyanagi S, Mizutani Y, Yokochi M (1993) An early cytoplasmic change before Lewy body maturation-an ultrastructural-study of the Substantia-Nigra from an autopsy case of Juvenile Parkinsonism. Acta Neuropathol 85:445-448 (Pubitemid 23100936)
    • (1993) Acta Neuropathologica , vol.85 , Issue.4 , pp. 445-448
    • Hayashida, K.1    Oyanagi, S.2    Mizutani, Y.3    Yokochi, M.4
  • 35
    • 0028985267 scopus 로고
    • The precursor protein of non-a-beta component of Alzheimers-disease amyloid is a presynaptic protein of the central-nervous-system
    • Iwai A, Masliah E, Yoshimoto M, Ge NF, Flanagan L, deSilva HAR, Kittel A, Saitoh T (1995) The precursor protein of non-a-beta component of Alzheimers-disease amyloid is a presynaptic protein of the central-nervous- system. Neuron 14:467-475
    • (1995) Neuron , vol.14 , pp. 467-475
    • Iwai, A.1    Masliah, E.2    Yoshimoto, M.3    Ge, N.F.4    Flanagan, L.5    DeSilva, H.A.R.6    Kittel, A.7    Saitoh, T.8
  • 36
    • 0028277520 scopus 로고
    • Identification of two distinct synucleins from human brain
    • DOI 10.1016/0014-5793(94)00395-5
    • Jakes R, Spillantini MG, Goedert M (1994) Identification of 2 Distinct Synucleins from Human Brain. FEBS Lett 345:27-32 (Pubitemid 24154659)
    • (1994) FEBS Letters , vol.345 , Issue.1 , pp. 27-32
    • Jakes, R.1    Spillantini, M.G.2    Goedert, M.3
  • 37
    • 0033516587 scopus 로고    scopus 로고
    • Epitope mapping of LB509, a monoclonal antibody directed against human α-synuclein
    • DOI 10.1016/S0304-3940(99)00411-5, PII S0304394099004115
    • Jakes R, Crowther RA, Lee VMY, Trojanowski JQ, Iwatsubo T, Goedert M (1999) Epitope mapping of LB509, a monoclonal antibody directed against human α-synuclein. Neurosci Lett 269:13-16 (Pubitemid 29305690)
    • (1999) Neuroscience Letters , vol.269 , Issue.1 , pp. 13-16
    • Jakes, R.1    Crowther, R.A.2    Lee, V.M.-Y.3    Trojanowski, J.Q.4    Iwatsubo, T.5    Goedert, M.6
  • 39
    • 0032500599 scopus 로고    scopus 로고
    • Binding of α-synuclein to brain vesicles is abolished by familial Parkinson's disease mutation
    • DOI 10.1074/jbc.273.41.26292
    • Jensen PH, Nielsen MS, Jakes R, Dotti G, Goedert M (1998) Binding of α-synuclein to brain vesicles is abolished by familial Parkinson's disease mutation. J Biol Chem 273:26292-26294 (Pubitemid 28471629)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.41 , pp. 26292-26294
    • Jensen, P.H.1    Nielsen, M.S.2    Jakes, R.3    Dotti, C.G.4    Goedert, M.5
  • 40
    • 33745279409 scopus 로고    scopus 로고
    • A Novel Mechanism of Interaction between α-Synuclein and Biological Membranes
    • DOI 10.1016/j.jmb.2006.05.004, PII S0022283606005705
    • Kim YS, Laurine E, Woods W, Lee SJ (2006) A novel mechanism of interaction between α-synuclein and biological membranes. J Mol Biol 360:386-397 (Pubitemid 43927829)
    • (2006) Journal of Molecular Biology , vol.360 , Issue.2 , pp. 386-397
    • Kim, Y.S.1    Laurine, E.2    Woods, W.3    Lee, S.-J.4
  • 41
    • 34548515059 scopus 로고    scopus 로고
    • An elaborate classification of SNARE proteins sheds light on the conservation of the eukaryotic endomembrane system
    • DOI 10.1091/mbc.E07-03-0193
    • Kloepper TH, Kienle CN, Fasshauer D (2007) An elaborate classification of SNARE proteins sheds light on the conservation of the eukaryotic endomembrane system. Mol Biol Cell 18:3463-3471 (Pubitemid 47378685)
    • (2007) Molecular Biology of the Cell , vol.18 , Issue.9 , pp. 3463-3471
    • Kloepper, T.H.1    Kienle, C.N.2    Fasshauer, D.3
  • 44
    • 0034733591 scopus 로고    scopus 로고
    • Rapid and reliable protein extraction from yeast
    • Kushnirov VV (2000) Rapid and reliable protein extraction from yeast. Yeast 16:857-860
    • (2000) Yeast , vol.16 , pp. 857-860
    • Kushnirov, V.V.1
  • 45
    • 52949083619 scopus 로고    scopus 로고
    • A systematic RNAi screen reveals involvement of endocytic pathway in neuronal dysfunction in α-synuclein transgenic C.elegans
    • Kuwahara T, Koyama A, Koyama S, Yoshina S, Ren CH, Kato T, Mitani S, Iwatsubo T (2008) A systematic RNAi screen reveals involvement of endocytic pathway in neuronal dysfunction in α-synuclein transgenic C.elegans. Hum Mol Genet 17:2997-3009
    • (2008) Hum Mol Genet , vol.17 , pp. 2997-3009
    • Kuwahara, T.1    Koyama, A.2    Koyama, S.3    Yoshina, S.4    Ren, C.H.5    Kato, T.6    Mitani, S.7    Iwatsubo, T.8
  • 47
    • 0037173006 scopus 로고    scopus 로고
    • Human α- synuclein-harboring familial Parkinson's disease-linked Ala-53 - >Thr mutation causes neurodegenerative disease with α- synuclein aggregation in transgenic mice
    • Lee MK, Stirling W, Xu YQ, Xu XY, Qui D, Mandir AS, Dawson TM, Copeland NG, Jenkins NA, Price DL (2002) Human α- synuclein-harboring familial Parkinson's disease-linked Ala-53 - >Thr mutation causes neurodegenerative disease with α- synuclein aggregation in transgenic mice. Proc Natl Acad Sci USA 99:8968-8973
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 8968-8973
    • Lee, M.K.1    Stirling, W.2    Xu, Y.Q.3    Xu, X.Y.4    Qui, D.5    Mandir, A.S.6    Dawson, T.M.7    Copeland, N.G.8    Jenkins, N.A.9    Price, D.L.10
  • 48
    • 0036777533 scopus 로고    scopus 로고
    • Conformational behavior of human α-synuclein is modulated by familial Parkinson's disease point mutations A30P and A53T
    • DOI 10.1016/S0161-813X(02)00066-9, PII S0161813X02000669
    • Li J, Uversky VN, Fink AL (2002) Conformational behavior of human α-synuclein is modulated by familial Parkinson's disease point mutations A30P and A53T. Neurotoxicology 23:553-567 (Pubitemid 36527676)
    • (2002) NeuroToxicology , vol.23 , Issue.4-5 , pp. 553-567
    • Li, J.1    Uversky, V.N.2    Fink, A.L.3
  • 49
    • 0037428439 scopus 로고    scopus 로고
    • Biochemical and genetic evidence for the involvement of yeast Ypt6-GTPase in protein retrieval to different Golgi compartments
    • Luo ZL, Gallwitz D (2003) Biochemical and genetic evidence for the involvement of yeast Ypt6-GTPase in protein retrieval to different Golgi compartments. J Biol Chem 278:791-799
    • (2003) J Biol Chem , vol.278 , pp. 791-799
    • Luo, Z.L.1    Gallwitz, D.2
  • 50
    • 0037323503 scopus 로고    scopus 로고
    • Cdc50p, a conserved endosomal membrane protein, controls polarized growth in Saccharomyces cerevisiae
    • DOI 10.1091/mbc.E02-06-0314
    • Misu K, Fujimura-Kamada K, Ueda T, Nakano A, Katoh H, Tanaka K (2003) Cdc50p, a conserved endosomal membrane protein, controls polarized growth in Saccharomyces cerevisiae. Mol Biol Cell 14:730-747 (Pubitemid 36237028)
    • (2003) Molecular Biology of the Cell , vol.14 , Issue.2 , pp. 730-747
    • Misu, K.1    Fujimura-Kamada, K.2    Ueda, T.3    Nakano, A.4    Katoh, H.5    Tanaka, K.6
  • 51
    • 58149290227 scopus 로고    scopus 로고
    • Trans-golgi network and endosome dynamics connect ceramide homeostasis with regulation of the unfolded protein response and TOR signaling in yeast
    • Mousley CJ, Tyeryar K, Ile KE, Schaaf G, Brost RL, Boone C, Guan XL, Wenk MR, Bankaitis VA (2008) Trans-golgi network and endosome dynamics connect ceramide homeostasis with regulation of the unfolded protein response and TOR signaling in yeast. Mol Biol Cell 19:4785-4803
    • (2008) Mol Biol Cell , vol.19 , pp. 4785-4803
    • Mousley, C.J.1    Tyeryar, K.2    Ile, K.E.3    Schaaf, G.4    Brost, R.L.5    Boone, C.6    Guan, X.L.7    Wenk, M.R.8    Bankaitis, V.A.9
  • 52
    • 0033535585 scopus 로고    scopus 로고
    • The grip domain - A novel golgi-targeting domain found in several coiled-coil proteins
    • DOI 10.1016/S0960-9822(99)80166-3
    • Munro S, Nichols BJ (1999) The GRIP domain-a novel Golgitargeting domain found in several coiled-coil proteins. Curr Biol 9:377-380 (Pubitemid 29194880)
    • (1999) Current Biology , vol.9 , Issue.7 , pp. 377-380
    • Munro, S.1    Nichols, B.J.2
  • 53
    • 1642546271 scopus 로고    scopus 로고
    • Positive and negative regulation of a SNARE protein by control of intracellular localization
    • Nakanishi H, los Santos P, Neiman AM (2004) Positive and negative regulation of a SNARE protein by control of intracellular localization. Mol Biol Cell 15:1802-1815
    • (2004) Mol Biol Cell , vol.15 , pp. 1802-1815
    • Nakanishi, H.1    Los Santos, P.2    Neiman, A.M.3
  • 54
    • 73549085595 scopus 로고    scopus 로고
    • Increased expression of alpha-Synuclein reduces neurotransmitter release by inhibiting synaptic vesicle reclustering after endocytosis
    • Nemani VM, Lu W, Berge V, Nakamura K, Onoa B, Lee MK, Chaudhry FA, Nicoll RA, Edwards RH (2010) Increased expression of alpha-Synuclein reduces neurotransmitter release by inhibiting synaptic vesicle reclustering after endocytosis. Neuron 65:66-79
    • (2010) Neuron , vol.65 , pp. 66-79
    • Nemani, V.M.1    Lu, W.2    Berge, V.3    Nakamura, K.4    Onoa, B.5    Lee, M.K.6    Chaudhry, F.A.7    Nicoll, R.A.8    Edwards, R.H.9
  • 55
    • 0034675999 scopus 로고    scopus 로고
    • Sorting of yeast membrane proteins into an endosome-to-Golgi pathway involves direct interaction of their cytosolic domains with Vps35p
    • Nothwehr SF, Ha SA, Bruinsma P (2000) Sorting of yeast membrane proteins into an endosome-to-Golgi pathway involves direct interaction of their cytosolic domains with Vps35p. J Cell Biol 151:297-309
    • (2000) J Cell Biol , vol.151 , pp. 297-309
    • Nothwehr, S.F.1    Ha, S.A.2    Bruinsma, P.3
  • 56
    • 0345189364 scopus 로고    scopus 로고
    • Yeast Cells Provide Insight into Alpha-Synuclein Biology and Pathobiology
    • DOI 10.1126/science.1090439
    • Outeiro TF, Lindquist S (2003) Yeast cells provide insight into α- synuclein biology and pathobiology. Science 302:1772-1775 (Pubitemid 37505742)
    • (2003) Science , vol.302 , Issue.5651 , pp. 1772-1775
    • Outeiro, T.F.1    Lindquist, S.2
  • 57
    • 0034602271 scopus 로고    scopus 로고
    • Interaction of human α-synuclein and Parkinson's disease variants with phospholipids-Structural analysis using site-directed mutagenesis
    • Perrin RJ, Woods WS, Clayton DF, George JM (2000) Interaction of human α-synuclein and Parkinson's disease variants with phospholipids-Structural analysis using site-directed mutagenesis. J Biol Chem 275:34393-34398
    • (2000) J Biol Chem , vol.275 , pp. 34393-34398
    • Perrin, R.J.1    Woods, W.S.2    Clayton, D.F.3    George, J.M.4
  • 59
    • 0027249359 scopus 로고
    • Homologs of the synaptobrevin/VAMP family of synaptic vesicle proteins function on the late secretory pathway in S. cerevisiae
    • DOI 10.1016/0092-8674(93)90465-3
    • Protopopov V, Govindan B, Novick P, Gerst JE (1993) Homologs of the synaptobrevin Vamp family of synaptic vesicle proteins function on the late secretory pathway in Saccharomyces cerevisiae. Cell 74:855-861 (Pubitemid 23270605)
    • (1993) Cell , vol.74 , Issue.5 , pp. 855-861
    • Protopopov, V.1    Govindan, B.2    Novick, P.3    Gerst, J.E.4
  • 60
    • 33744788870 scopus 로고    scopus 로고
    • Quantification of α-synuclein binding to lipid vesicles using fluorescence correlation spectroscopy
    • DOI 10.1529/biophysj.105.079251
    • Rhoades E, Ramlall TF, Webb WW, Eliezer D (2006) Quantification of α-synuclein binding to lipid vesicles using fluorescence correlation spectroscopy. Biophys J 90:4692-4700 (Pubitemid 43830913)
    • (2006) Biophysical Journal , vol.90 , Issue.12 , pp. 4692-4700
    • Rhoades, E.1    Ramlall, T.F.2    Webb, W.W.3    Eliezer, D.4
  • 61
    • 0025327984 scopus 로고
    • Cloning and characterization of Kluyveromyces lactis SEC14, a gene whose product stimulates Golgi secretory function in Saccharomyces cerevisiae
    • Salama SR, Cleves AE, Malehorn DE, Whitters EA, Bankaitis VA (1990) Cloning and characterization of Kluyveromyces-Lactis Sec14, A gene whose product stimulates Golgi secretory function in Saccharomyces cerevisiae. J Bacteriol 172:4510-4521 (Pubitemid 20236746)
    • (1990) Journal of Bacteriology , vol.172 , Issue.8 , pp. 4510-4521
    • Salama, S.R.1    Clevels, A.E.2    Malehorn, D.E.3    Whitters, E.A.4    Bankaitis, V.A.5
  • 62
    • 0027449288 scopus 로고
    • Involvement of Ypt7p, a small GTPase, in traffic from late endosome to the vacuole in yeast
    • Schimmoller F, Riezman H (1993) Involvement of Ypt7P, a small Gtpase, in traffic from late endosome to the vacuole in yeast. J Cell Sci 106:823-830 (Pubitemid 23346795)
    • (1993) Journal of Cell Science , vol.106 , Issue.3 , pp. 823-830
    • Schimmoller, F.1    Riezman, H.2
  • 63
    • 77953796839 scopus 로고    scopus 로고
    • A pathologic cascade leading to synaptic dysfunction in α- Synuclein-induced neurodegeneration
    • Scott DA, Tabarean I, Tang Y, Cartier A, Masliah E, Roy S (2010) A pathologic cascade leading to synaptic dysfunction in α- synuclein-induced neurodegeneration. J Neurosci 30:8083-8095
    • (2010) J Neurosci , vol.30 , pp. 8083-8095
    • Scott, D.A.1    Tabarean, I.2    Tang, Y.3    Cartier, A.4    Masliah, E.5    Roy, S.6
  • 65
    • 11144267737 scopus 로고    scopus 로고
    • Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein
    • DOI 10.1038/nbt1037
    • Shaner NC, Campbell RE, Steinbach PA, Giepmans BNG, Palmer AE, Tsien RY (2004) Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein. Nat Biotechnol 22:1567-1572 (Pubitemid 40039460)
    • (2004) Nature Biotechnology , vol.22 , Issue.12 , pp. 1567-1572
    • Shaner, N.C.1    Campbell, R.E.2    Steinbach, P.A.3    Giepmans, B.N.G.4    Palmer, A.E.5    Tsien, R.Y.6
  • 66
    • 0028181704 scopus 로고
    • Role of 3 Rab5-Like Gtpases, Ypt51P, Ypt52P, and Ypt53P, in the endocytic and vacuolar protein sorting pathways of yeast
    • Singerkruger B, Stenmark H, Dusterhoft A, Philippsen P, Yoo JS, Gallwitz D, Zerial M (1994) Role of 3 Rab5-Like Gtpases, Ypt51P, Ypt52P, and Ypt53P, in the endocytic and vacuolar protein sorting pathways of yeast. J Cell Biol 125:283-298
    • (1994) J Cell Biol , vol.125 , pp. 283-298
    • Singerkruger, B.1    Stenmark, H.2    Dusterhoft, A.3    Philippsen, P.4    Yoo, J.S.5    Gallwitz, D.6    Zerial, M.7
  • 68
    • 0035503740 scopus 로고    scopus 로고
    • An effector of Ypt6p binds the SNARE Tlg1p and mediates selective fusion of vesicles with late golgi membranes
    • DOI 10.1093/emboj/20.21.5991
    • Siniossoglou S, Pelham HRB (2001) An effector of Ypt6p binds the SNARE Tlg1p and mediates selective fusion of vesicles with late Golgi membranes. EMBO J 20:5991-5998 (Pubitemid 33049274)
    • (2001) EMBO Journal , vol.20 , Issue.21 , pp. 5991-5998
    • Siniossoglou, S.1    Pelham, H.R.B.2
  • 69
    • 0037073694 scopus 로고    scopus 로고
    • Vps51p links the VFT complex to the SNARE Tlg1p
    • DOI 10.1074/jbc.M209428200
    • Siniossoglou S, Pelham HRB (2002) Vps51p links the VFT complex to the SNARE Tlg1p. J Biol Chem 277:48318-48324 (Pubitemid 35470786)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.50 , pp. 48318-48324
    • Siniossoglou, S.1    Pelham, H.R.B.2
  • 70
    • 0034665261 scopus 로고    scopus 로고
    • Ric1p and Rgp1p form a complex that catalyses nucleotide exchange on Ypt6p
    • Siniossoglou S, Peak-Chew SY, Pelham HRB (2000) Ric1p and Rgp1p form a complex that catalyses nucleotide exchange on Ypt6p. EMBO J 19:4885-4894
    • (2000) EMBO J , vol.19 , pp. 4885-4894
    • Siniossoglou, S.1    Peak-Chew, S.Y.2    Pelham, H.R.B.3
  • 74
    • 37549068169 scopus 로고    scopus 로고
    • Alpha-Synuclein selectively binds to anionic phospholipids embedded in liquiddisordered domains
    • Stockl M, Fischer P, Wanker E, Herrmann A (2008) alpha-Synuclein selectively binds to anionic phospholipids embedded in liquiddisordered domains. J Mol Biol 375:1394-1404
    • (2008) J Mol Biol , vol.375 , pp. 1394-1404
    • Stockl, M.1    Fischer, P.2    Wanker, E.3    Herrmann, A.4
  • 75
    • 0027468660 scopus 로고
    • A yeast GTPase-activating protein that interacts specifically with a member of the Ypt/Rab family
    • DOI 10.1038/361736a0
    • Strom M, Vollmer P, Tan TJ, Gallwitz D (1993) A Yeast Gtpase-activating protein that interacts specifically with a member of the Ypt/Rab family. Nature 361:736-739 (Pubitemid 23070483)
    • (1993) Nature , vol.361 , Issue.6414 , pp. 736-739
    • Strom, M.1    Vollmer, P.2    Tan, T.J.3    Gallwitz, D.4
  • 76
    • 77952900626 scopus 로고    scopus 로고
    • {alpha}-Synuclein delays endoplasmic reticulum (ER)-to- Golgi transport in Mammalian cells by antagonizing ER/Golgi SNAREs
    • Thayanidhi N, Helm JR, Nycz DC, Bentley M, Liang Y, Hay JC (2010) {alpha}-Synuclein delays endoplasmic reticulum (ER)-to- Golgi transport in Mammalian cells by antagonizing ER/Golgi SNAREs. Mol Biol Cell 21:1850-1863
    • (2010) Mol Biol Cell , vol.21 , pp. 1850-1863
    • Thayanidhi, N.1    Helm, J.R.2    Nycz, D.C.3    Bentley, M.4    Liang, Y.5    Hay, J.C.6
  • 78
    • 0029985116 scopus 로고    scopus 로고
    • Isolation and characterization of SYS genes from yeast, multicopy suppressors of the functional loss of the transport GTPase Ypt6p
    • Tsukada M, Gallwitz D (1996) Isolation and characterization of SYS genes from yeast, multicopy suppressors of the functional loss of the transport GTPase Ypt6p. J Cell Sci 109:2471-2481 (Pubitemid 26377522)
    • (1996) Journal of Cell Science , vol.109 , Issue.10 , pp. 2471-2481
    • Tsukada, M.1    Gallwitz, D.2
  • 79
    • 33846817163 scopus 로고    scopus 로고
    • Relationships between the Sequence of α-Synuclein and its Membrane Affinity, Fibrillization Propensity, and Yeast Toxicity
    • DOI 10.1016/j.jmb.2006.12.044, PII S0022283606017219
    • Volles MJ, Lansbury PT (2007) Relationships between the sequence of α-synuclein and its membrane affinity, fibrillization propensity, and yeast toxicity. J Mol Biol 366:1510-1522 (Pubitemid 46215614)
    • (2007) Journal of Molecular Biology , vol.366 , Issue.5 , pp. 1510-1522
    • Volles, M.J.1    Lansbury Jr., P.T.2
  • 80
    • 0033557836 scopus 로고    scopus 로고
    • Primary structure and biochemical characterization of yeast GTPase- activating proteins with substrate preference for the transport GTPase Ypt7p
    • DOI 10.1046/j.1432-1327.1999.00192.x
    • Vollmer P, Will E, Scheglmann D, Strom M, Gallwitz D (1999) Primary structure and biochemical characterization of yeast GTPase-activating proteins with substrate preference for the transport GTPase Ypt7p. Eur J Biochem 260:284-290 (Pubitemid 29095720)
    • (1999) European Journal of Biochemistry , vol.260 , Issue.1 , pp. 284-290
    • Vollmer, P.1    Will, E.2    Scheglmann, D.3    Strom, M.4    Gallwitz, D.5
  • 81
    • 0017641210 scopus 로고
    • Dense core vesicles around the lewy body in incidental Parkinson's disease: an electron microscopic study
    • DOI 10.1007/BF00703325
    • Watanabe I, Vachal E, Tomita T (1977) Dense core vesicles around Lewy body in incidental Parkinsons-disease - electron-microscopic study. Acta Neuropathol 39:173-175 (Pubitemid 8153210)
    • (1977) Acta Neuropathologica , vol.39 , Issue.2 , pp. 173-175
    • Watanabe, I.1    Vachal, E.2    Tomita, T.3
  • 82
    • 0027092937 scopus 로고
    • Endocytosis in yeast: Evidence for the involvement of a small GTP-binding protein (Ypt7p)
    • DOI 10.1016/S0092-8674(05)80062-5
    • Wichmann H, Hengst L, Gallwitz D (1992) Endocytosis in yeast - evidence for the involvement of a small Gtp-binding protein (Ypt7P). Cell 71:1131-1142 (Pubitemid 23016548)
    • (1992) Cell , vol.71 , Issue.7 , pp. 1131-1142
    • Wichmann, H.1    Hengst, L.2    Gallwitz, D.3
  • 83
    • 0034678365 scopus 로고    scopus 로고
    • The F-box protein Rcy1p is involved in endocytic membrane traffic and recycling out of an early endosome in Saccharomyces cerevisiae
    • DOI 10.1083/jcb.149.2.397
    • Wiederkehr A, Avaro S, Prescianotto-Baschong C, Haguenauer-Tsapis R, Riezman H (2000) The F-box protein Rcy1p is involved in endocytic membrane traffic and recycling out of an early endosome in Saccharomyces cerevisiae. J Cell Biol 149:397-410 (Pubitemid 30227156)
    • (2000) Journal of Cell Biology , vol.149 , Issue.2 , pp. 397-410
    • Wiederkehr, A.1    Avaro, S.2    Prescianotto-Baschong, C.3    Haguenauer-Tsapis, R.4    Riezman, H.5
  • 84
    • 0345189365 scopus 로고    scopus 로고
    • Yeast Genes that Enhance the Toxicity of a Mutant Huntingtin Fragment or α-Synuclein
    • DOI 10.1126/science.1090389
    • Willingham S, Outeiro TF, Devit MJ, Lindquist SL, Muchowski PJ (2003) Yeast genes that enhance the toxicity of a mutant huntingtin fragment or α-synuclein. Science 302:1769-1772 (Pubitemid 37505741)
    • (2003) Science , vol.302 , Issue.5651 , pp. 1769-1772
    • Willingham, S.1    Outeiro, T.F.2    DeVit, M.J.3    Lindquist, S.L.4    Muchowski, P.J.5
  • 85
    • 0033538541 scopus 로고    scopus 로고
    • α-synuclein fibrillogenesis is nucleation-dependent- Implications for the pathogenesis of Parkinson's disease
    • Wood SJ, Wypych J, Steavenson S, Louis JC, Citron M, Biere AL (1999) α-synuclein fibrillogenesis is nucleation-dependent- Implications for the pathogenesis of Parkinson's disease. J Biol Chem 274:19509-19512
    • (1999) J Biol Chem , vol.274 , pp. 19509-19512
    • Wood, S.J.1    Wypych, J.2    Steavenson, S.3    Louis, J.C.4    Citron, M.5    Biere, A.L.6
  • 87
    • 0036278335 scopus 로고    scopus 로고
    • Dopamine-dependent neurotoxicity of α-synuclein: A mechanism for selective neurodegeneration in Parkinson disease
    • DOI 10.1038/nm0602-600
    • Xu J, Kao SY, Lee FJS, Song WH, Jin LW, Yankner BA (2002) Dopamine-dependent neurotoxicity of α-synuclein: a mechanism for selective neurodegeneration in Parkinson disease. Nat Med 8:600-606 (Pubitemid 34633438)
    • (2002) Nature Medicine , vol.8 , Issue.6 , pp. 600-606
    • Xu, J.1    Kao, S.-Y.2    Lee, F.J.S.3    Song, W.4    Jin, L.-W.5    Yankner, B.A.6
  • 88
    • 10944243102 scopus 로고    scopus 로고
    • Role of α-synuclein in presynaptic dopamine recruitment
    • DOI 10.1523/JNEUROSCI.2559-04.2004
    • Yavich L, Tanila H, Vepsalainen S, Jakala P (2004) Role of α- synuclein in presynaptic dopamine recruitment. J Neurosci 24:11165-11170 (Pubitemid 40012976)
    • (2004) Journal of Neuroscience , vol.24 , Issue.49 , pp. 11165-11170
    • Yavich, L.1    Tanila, H.2    Vepsalainen, S.3    Jakala, P.4
  • 92
    • 0029009125 scopus 로고
    • Isolation and biochemical-characterization of organelles from the yeast, Saccharomyces cerevisiae
    • Zinser E, Daum G (1995) Isolation and biochemical-characterization of organelles from the yeast, Saccharomyces cerevisiae. Yeast 11:493-536
    • (1995) Yeast , vol.11 , pp. 493-536
    • Zinser, E.1    Daum, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.