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Volumn 6, Issue 3, 2015, Pages 403-416

Molecular determinants of α-synuclein mutants' oligomerization and membrane interactions

Author keywords

membrane interactions; molecular dynamics; neurodegeneration; oligomers; Synuclein; synuclein mutants

Indexed keywords

ALPHA SYNUCLEIN; MUTANT PROTEIN; PROTEIN A30P; PROTEIN A53T; PROTEIN E35K; PROTEIN E46K; UNCLASSIFIED DRUG;

EID: 84925599754     PISSN: None     EISSN: 19487193     Source Type: Journal    
DOI: 10.1021/cn500332w     Document Type: Article
Times cited : (36)

References (65)
  • 1
    • 0035409575 scopus 로고    scopus 로고
    • Alpha-synuclein and neurodegenerative diseases
    • Goedert, M. (2001) Alpha-synuclein and neurodegenerative diseases Nat. Rev. Neurosci. 2, 492-501
    • (2001) Nat. Rev. Neurosci. , vol.2 , pp. 492-501
    • Goedert, M.1
  • 9
    • 0031787871 scopus 로고    scopus 로고
    • Accelerated in vitro fibril formation by a mutant alpha-synuclein linked to early-onset Parkinson disease
    • Conway, K. A., Harper, J. D., and Lansbury, P. T. (1998) Accelerated in vitro fibril formation by a mutant alpha-synuclein linked to early-onset Parkinson disease Nat. Med. 4, 1318-1320
    • (1998) Nat. Med. , vol.4 , pp. 1318-1320
    • Conway, K.A.1    Harper, J.D.2    Lansbury, P.T.3
  • 10
    • 0034646391 scopus 로고    scopus 로고
    • Fibrils formed in vitro from alpha synuclein and two mutant forms linked to Parkinson's disease are typical amyloid
    • Conway, K. A., Harper, J. D., and Lansbury, P. T., Jr. (2000) Fibrils formed in vitro from alpha synuclein and two mutant forms linked to Parkinson's disease are typical amyloid Biochemistry 39, 2552-2563
    • (2000) Biochemistry , vol.39 , pp. 2552-2563
    • Conway, K.A.1    Harper, J.D.2    Lansbury, P.T.3
  • 13
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • Caughey, B. and Lansbury, P. T. (2003) Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders Annu. Rev. Neurosci. 26, 267-298
    • (2003) Annu. Rev. Neurosci. , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury, P.T.2
  • 14
    • 0037016741 scopus 로고    scopus 로고
    • Membrane-bound syn has a high aggregation propensity and the ability to seed the aggregation of the cytosolic form
    • Lee, H. J., Choi, C., and Lee, S. J. (2002) Membrane-bound syn has a high aggregation propensity and the ability to seed the aggregation of the cytosolic form J. Biol. Chem. 277, 671-678
    • (2002) J. Biol. Chem. , vol.277 , pp. 671-678
    • Lee, H.J.1    Choi, C.2    Lee, S.J.3
  • 15
    • 65249185574 scopus 로고    scopus 로고
    • Interplay of α-synuclein binding and conformational switching probe by single-molecule fluorescence
    • Ferreon, A. C., Gambin, Y., Lemke, E. A., and Deniz, A. A. (2009) Interplay of α-synuclein binding and conformational switching probe by single-molecule fluorescence Proc. Natl. Acad. Sci. U. S. A. 106, 5645-5650
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 5645-5650
    • Ferreon, A.C.1    Gambin, Y.2    Lemke, E.A.3    Deniz, A.A.4
  • 16
    • 0029127954 scopus 로고
    • Characterization of a novel protein regulated during the critical period for song learning in the zebra finch
    • George, J. M., Jin, H., Woods, W. S., and Clayton, D. F. (1995) Characterization of a novel protein regulated during the critical period for song learning in the zebra finch Neuron 15, 361-372
    • (1995) Neuron , vol.15 , pp. 361-372
    • George, J.M.1    Jin, H.2    Woods, W.S.3    Clayton, D.F.4
  • 17
    • 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
  • 18
    • 84860289084 scopus 로고    scopus 로고
    • Effect of the A30P mutation on the structural dynamics of micelle-bound αsynuclein released in water: A molecular dynamics study
    • Chatterjee, P. and Sengupta, N. (2012) Effect of the A30P mutation on the structural dynamics of micelle-bound αSynuclein released in water: a molecular dynamics study Eur. Biophys. J. 41, 483-489
    • (2012) Eur. Biophys. J. , vol.41 , pp. 483-489
    • Chatterjee, P.1    Sengupta, N.2
  • 20
    • 79960260042 scopus 로고    scopus 로고
    • Familial Parkinson disease mutations influence α-synuclein assembly
    • Ono, K., Ikeda, T., Takasaki, J., and Yamada, M. (2011) Familial Parkinson disease mutations influence α-synuclein assembly Neurobiol. Dis. 43, 715-724
    • (2011) Neurobiol. Dis. , vol.43 , pp. 715-724
    • Ono, K.1    Ikeda, T.2    Takasaki, J.3    Yamada, M.4
  • 22
    • 80051521167 scopus 로고    scopus 로고
    • Structural role of compensatory amino acid replacements in the α-synuclein protein
    • Losasso, V., Pietropaolo, A., Zannoni, C., Gustincich, S., and Carloni, P. (2011) Structural role of compensatory amino acid replacements in the α-synuclein protein Biochemistry 50, 6994-7001
    • (2011) Biochemistry , vol.50 , pp. 6994-7001
    • Losasso, V.1    Pietropaolo, A.2    Zannoni, C.3    Gustincich, S.4    Carloni, P.5
  • 23
    • 84875523636 scopus 로고    scopus 로고
    • Structures and free energy landscapes of the wild-type and A30P mutant-type α-synuclein proteins with dynamics
    • Wise-Scira, O., Aloglu, A. K., Dunn, A., Sakallioglu, I. T., and Coskuner, O. (2013) Structures and free energy landscapes of the wild-type and A30P mutant-type α-synuclein proteins with dynamics ACS Chem. Neurosci. 4, 486-497
    • (2013) ACS Chem. Neurosci. , vol.4 , pp. 486-497
    • Wise-Scira, O.1    Aloglu, A.K.2    Dunn, A.3    Sakallioglu, I.T.4    Coskuner, O.5
  • 24
    • 84875486735 scopus 로고    scopus 로고
    • Structures of the E46K mutant-type α-synuclein protein and impact of E46K mutation on the structures of the wild-type α-synuclein protein
    • Wise-Scira, O., Dunn, A., Aloglu, A. K., Sakallioglu, I. T., and Coskuner, O. (2013) Structures of the E46K mutant-type α-synuclein protein and impact of E46K mutation on the structures of the wild-type α-synuclein protein ACS Chem. Neurosci. 4, 498-508
    • (2013) ACS Chem. Neurosci. , vol.4 , pp. 498-508
    • Wise-Scira, O.1    Dunn, A.2    Aloglu, A.K.3    Sakallioglu, I.T.4    Coskuner, O.5
  • 26
    • 84880394668 scopus 로고    scopus 로고
    • Structures and free energy landscapes of the A53T mutant-type α-synuclein protein and impact of A53T mutation on the structures of the wild-type α-synuclein protein with dynamics
    • Coskuner, O. and Wise-Scira, O. (2013) Structures and free energy landscapes of the A53T mutant-type α-synuclein protein and impact of A53T mutation on the structures of the wild-type α-synuclein protein with dynamics ACS Chem. Neurosci. 4, 1101-1113
    • (2013) ACS Chem. Neurosci. , vol.4 , pp. 1101-1113
    • Coskuner, O.1    Wise-Scira, O.2
  • 28
    • 65449137602 scopus 로고    scopus 로고
    • Curvature dynamics of alpha-synuclein familial Parkinson disease mutants: Molecular simulations of the micelle- and bilayer-bound forms
    • Perlmutter, J. D., Braun, A. R., and Sachs, J. N. (2009) Curvature dynamics of alpha-synuclein familial Parkinson disease mutants: Molecular simulations of the micelle- and bilayer-bound forms J. Biol. Chem. 284, 7177-7189
    • (2009) J. Biol. Chem. , vol.284 , pp. 7177-7189
    • Perlmutter, J.D.1    Braun, A.R.2    Sachs, J.N.3
  • 29
    • 79954534373 scopus 로고    scopus 로고
    • Molecular basis for the glycosphingolipid-binding specificity of α-synuclein: Key role of tyrosine 39 in membrane insertion
    • Fantini, J. and Yahi, N. (2011) Molecular basis for the glycosphingolipid-binding specificity of α-synuclein: Key role of tyrosine 39 in membrane insertion J. Mol. Biol. 408, 654-669
    • (2011) J. Mol. Biol. , vol.408 , pp. 654-669
    • Fantini, J.1    Yahi, N.2
  • 31
    • 84861060898 scopus 로고    scopus 로고
    • OPM database and PPM web server: Resources for positioning of proteins in membranes
    • Lomize, M. A., Pogozheva, I. D., Joo, H., Mosberg, H. I., and Lomize, A. L. (2012) OPM database and PPM web server: resources for positioning of proteins in membranes Nucleic Acids Res. 40, D370-D376
    • (2012) Nucleic Acids Res. , vol.40 , pp. 370-D376
    • Lomize, M.A.1    Pogozheva, I.D.2    Joo, H.3    Mosberg, H.I.4    Lomize, A.L.5
  • 32
    • 44349100972 scopus 로고    scopus 로고
    • Broken helix in vesicle and micelle-bound alpha-synuclein: Insights from site-directed spin labeling-EPR experiments and MD simulations
    • Bortolus, M., Tombolato, F., Tessari, I., Bisaglia, M., Mammi, S., Bubacco, L., Ferrarini, A., and Maniero, A. L. (2008) Broken helix in vesicle and micelle-bound alpha-synuclein: Insights from site-directed spin labeling-EPR experiments and MD simulations J. Am. Chem. Soc. 130, 6690-6691
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 6690-6691
    • Bortolus, M.1    Tombolato, F.2    Tessari, I.3    Bisaglia, M.4    Mammi, S.5    Bubacco, L.6    Ferrarini, A.7    Maniero, A.L.8
  • 33
    • 0034681163 scopus 로고    scopus 로고
    • Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: Implications for pathogenesis and therapy
    • Conway, K. A., Lee, S. J., Rochet, J. C., Ding, T. T., Williamson, R. E., and Lansbury, P. T. (2000) Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy Proc. Natl. Acad. Sci. U. S. A. 97, 571-576
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 571-576
    • Conway, K.A.1    Lee, S.J.2    Rochet, J.C.3    Ding, T.T.4    Williamson, R.E.5    Lansbury, P.T.6
  • 34
    • 77954275738 scopus 로고    scopus 로고
    • HexServer: An FFT-based protein docking server powered by graphics processors
    • Macindoe, G., Mavridis, L., Venkatraman, V., Devignes, M. D., and Ritchie, D. W. (2010) HexServer: An FFT-based protein docking server powered by graphics processors Nucleic Acids Res. 38 (Web Server issue) W445-W449
    • (2010) Nucleic Acids Res. , vol.38 , Issue.WEB SERVER ISSUE , pp. 445-W449
    • Macindoe, G.1    Mavridis, L.2    Venkatraman, V.3    Devignes, M.D.4    Ritchie, D.W.5
  • 35
    • 80855144163 scopus 로고    scopus 로고
    • The mode of α-synuclein binding to membranes depends on lipid composition and lipid to protein ratio
    • Schvadchak, V. V., Yushchenko, D. A., Pievo, R., and Jovin, T. M. (2011) The mode of α-synuclein binding to membranes depends on lipid composition and lipid to protein ratio FEBS Lett. 585, 3513-3519
    • (2011) FEBS Lett. , vol.585 , pp. 3513-3519
    • Schvadchak, V.V.1    Yushchenko, D.A.2    Pievo, R.3    Jovin, T.M.4
  • 36
    • 77449085703 scopus 로고    scopus 로고
    • Altered ion channel formation by the Parkinson's-disease-linked E46K mutant of α-synuclein is corrected by GM3 but not by GM1 gangliosides
    • Di Pasquale, E., Fantini, J., Chahihian, H., Meresca, M., Taieb, N., and Yahi, N. (2010) Altered ion channel formation by the Parkinson's-disease-linked E46K mutant of α-synuclein is corrected by GM3 but not by GM1 gangliosides J. Mol. Biol. 397, 202-218
    • (2010) J. Mol. Biol. , vol.397 , pp. 202-218
    • Di Pasquale, E.1    Fantini, J.2    Chahihian, H.3    Meresca, M.4    Taieb, N.5    Yahi, N.6
  • 37
    • 0037192816 scopus 로고    scopus 로고
    • Identification of a common sphingolipid-binding domain in Alzheimer, prion, and HIV-1 proteins
    • Mahfoud, N., Garmy, M., Maresca, N., Yahi, A., Puigserver, A., and Fantini, J. (2002) Identification of a common sphingolipid-binding domain in Alzheimer, prion, and HIV-1 proteins J. Biol. Chem. 277, 11292-11296
    • (2002) J. Biol. Chem. , vol.277 , pp. 11292-11296
    • Mahfoud, N.1    Garmy, M.2    Maresca, N.3    Yahi, A.4    Puigserver, A.5    Fantini, J.6
  • 38
    • 15744362063 scopus 로고    scopus 로고
    • Structure and dynamics of micelle-bound human alpha-synuclein
    • Ulmer, T. S., Bax, A., Cole, N. B., and Nussbaum, R. L. (2005) Structure and dynamics of micelle-bound human alpha-synuclein J. Biol. Chem. 280, 9595-9603
    • (2005) J. Biol. Chem. , vol.280 , pp. 9595-9603
    • Ulmer, T.S.1    Bax, A.2    Cole, N.B.3    Nussbaum, R.L.4
  • 39
    • 59649110692 scopus 로고    scopus 로고
    • Structural insights on physiological functions and pathological effects of alpha-synuclein
    • Bisaglia, M., Mammi, S., and Bubacco, L. (2009) Structural insights on physiological functions and pathological effects of alpha-synuclein FASEB J. 23, 329-340
    • (2009) FASEB J. , vol.23 , pp. 329-340
    • Bisaglia, M.1    Mammi, S.2    Bubacco, L.3
  • 43
    • 84883079994 scopus 로고    scopus 로고
    • In-cell NMR characterization of the secondary structure populations of a disordered conformation of α-synuclein within E. Coli cells
    • Waudby, C. A., Camilloni, C., Fitzpatrick, A. W., Cabrita, L. D., Dobson, C. M., Vendruscolo, M., and Christodoulou, J. (2013) In-cell NMR characterization of the secondary structure populations of a disordered conformation of α-synuclein within E. coli cells PLoS One 8, e72286
    • (2013) PLoS One , vol.8 , pp. 72286
    • Waudby, C.A.1    Camilloni, C.2    Fitzpatrick, A.W.3    Cabrita, L.D.4    Dobson, C.M.5    Vendruscolo, M.6    Christodoulou, J.7
  • 46
    • 67649213482 scopus 로고    scopus 로고
    • Aggregation-defective alpha-synuclein mutants inhibit the fibrillation of Parkinson's disease-linked alpha-synuclein variants
    • Koo, H. J., Choi, M. Y., and Im, H. (2009) Aggregation-defective alpha-synuclein mutants inhibit the fibrillation of Parkinson's disease-linked alpha-synuclein variants Biochem. Biophys. Res. Commun. 386, 165-169
    • (2009) Biochem. Biophys. Res. Commun. , vol.386 , pp. 165-169
    • Koo, H.J.1    Choi, M.Y.2    Im, H.3
  • 48
    • 0037130174 scopus 로고    scopus 로고
    • Neurodegenerative disease: Amyloid pores from pathogenic mutations
    • Lashuel, H. A., Hartley, D., Petre, B. M., Walz, T., and Lansbury, P. T., Jr. (2002) Neurodegenerative disease: amyloid pores from pathogenic mutations Nature 418, 4-5
    • (2002) Nature , vol.418 , pp. 4-5
    • Lashuel, H.A.1    Hartley, D.2    Petre, B.M.3    Walz, T.4    Lansbury, P.T.5
  • 50
    • 84918832224 scopus 로고    scopus 로고
    • Alpha-synuclein oligomers and fibrils originate in two distinct conformer pools: A small angle X-ray scattering and ensemble optimization modelling study
    • Curtain, C. C., Kirby, N. M., Mertens, H. D., Barnham, K. J., Knott, R. B., Masters, C. L., Cappai, R., Rekas, A., Kenche, V. B., and Ryan, T. (2015) Alpha-synuclein oligomers and fibrils originate in two distinct conformer pools: a small angle X-ray scattering and ensemble optimization modelling study Mol. BioSyst. 11, 190-196
    • (2015) Mol. BioSyst. , vol.11 , pp. 190-196
    • Curtain, C.C.1    Kirby, N.M.2    Mertens, H.D.3    Barnham, K.J.4    Knott, R.B.5    Masters, C.L.6    Cappai, R.7    Rekas, A.8    Kenche, V.B.9    Ryan, T.10
  • 53
    • 0034250744 scopus 로고    scopus 로고
    • An improved empirical potential energy function for molecular simulations of phospholipids
    • Feller, S. E. and MacKerell, A. D., Jr. (2000) An improved empirical potential energy function for molecular simulations of phospholipids J. Phys. Chem. B 104, 7510-7515
    • (2000) J. Phys. Chem. B , vol.104 , pp. 7510-7515
    • Feller, S.E.1    Mackerell, A.D.2
  • 54
    • 36449003554 scopus 로고
    • Constant pressure molecular dynamics algorithms
    • Martyna, G. J., Tobias, D. J., and Klein, M. L. (1994) Constant pressure molecular dynamics algorithms J. Chem. Phys. 101, 4177-4189
    • (1994) J. Chem. Phys. , vol.101 , pp. 4177-4189
    • Martyna, G.J.1    Tobias, D.J.2    Klein, M.L.3
  • 55
    • 0034250744 scopus 로고    scopus 로고
    • An improved empirical potential energy function for molecular simulations of phospholipids
    • Feller, S. E. and MacKerell, A. D., Jr. (2000) An improved empirical potential energy function for molecular simulations of phospholipids J. Phys. Chem. B 104, 7510-7515
    • (2000) J. Phys. Chem. B , vol.104 , pp. 7510-7515
    • Feller, S.E.1    Mackerell, A.D.2
  • 56
    • 0000408363 scopus 로고    scopus 로고
    • Approximate atomic surfaces from linear combinations of pairwise overlaps (LCPO)
    • Weiser, J., Shenkin, P. S., and Still, W. C. (1999) Approximate atomic surfaces from linear combinations of pairwise overlaps (LCPO) J. Comput. Chem. 20, 217-230
    • (1999) J. Comput. Chem. , vol.20 , pp. 217-230
    • Weiser, J.1    Shenkin, P.S.2    Still, W.C.3
  • 57
    • 0020997912 scopus 로고    scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W. and Sander, C. Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22, 2577-2637.
    • Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 58
    • 0031715982 scopus 로고    scopus 로고
    • Protein structure alignment by incremental combinatorial extension (CE) of the optimal path
    • Shindyalov, I. N. and Bourne, P. E. (1998) Protein structure alignment by incremental combinatorial extension (CE) of the optimal path Protein Eng. 11, 739-747
    • (1998) Protein Eng. , vol.11 , pp. 739-747
    • Shindyalov, I.N.1    Bourne, P.E.2
  • 60
    • 79958081714 scopus 로고    scopus 로고
    • Polymorphic structures of Alzheimer's beta-amyloid globulomers
    • Yu, X. and Zheng, J. (2011) Polymorphic structures of Alzheimer's beta-amyloid globulomers PloS One 6, e20575
    • (2011) PloS One , vol.6 , pp. 20575
    • Yu, X.1    Zheng, J.2
  • 61
    • 43549104227 scopus 로고    scopus 로고
    • Statins reduce neuronal alpha-synuclein aggregation in in vitro models of Parkinson's disease
    • Bar-On, P., Crews, L., Koob, A. O., Mizuno, H., Adame, A., Spencer, B., and Masliah, E. (2008) Statins reduce neuronal alpha-synuclein aggregation in in vitro models of Parkinson's disease J. Neurochem. 105, 1656-1667
    • (2008) J. Neurochem. , vol.105 , pp. 1656-1667
    • Bar-On, P.1    Crews, L.2    Koob, A.O.3    Mizuno, H.4    Adame, A.5    Spencer, B.6    Masliah, E.7
  • 62
    • 70350550208 scopus 로고    scopus 로고
    • Beclin 1 gene transfer activates autophagy and ameliorates the neurodegenerative pathology in alpha-synuclein models of Parkinson's and Lewy body diseases
    • Spencer, B., Potkar, R., Trejo, M., Rockenstein, E., Patrick, C., Gindi, R., Adame, A., Wyss-Coray, T., and Masliah, E. (2009) Beclin 1 gene transfer activates autophagy and ameliorates the neurodegenerative pathology in alpha-synuclein models of Parkinson's and Lewy body diseases J. Neurosci. 29, 13578-13588
    • (2009) J. Neurosci. , vol.29 , pp. 13578-13588
    • Spencer, B.1    Potkar, R.2    Trejo, M.3    Rockenstein, E.4    Patrick, C.5    Gindi, R.6    Adame, A.7    Wyss-Coray, T.8    Masliah, E.9
  • 63
    • 34250664283 scopus 로고    scopus 로고
    • Design and cloning of lentiviral vectors expressing small interfering RNAs
    • Tiscornia, G., Singer, O., and Verma, I. M. (2006) Design and cloning of lentiviral vectors expressing small interfering RNAs Nat. Protoc. 1, 234-240
    • (2006) Nat. Protoc. , vol.1 , pp. 234-240
    • Tiscornia, G.1    Singer, O.2    Verma, I.M.3
  • 65
    • 0034681471 scopus 로고    scopus 로고
    • Dopaminergic loss and inclusion body formation in alpha-synuclein mice: Implications for neurodegenerative disorders
    • Masliah, E., Rockenstein, E., Veinbergs, I., Mallory, M., Hashimoto, M., Takeda, A., Sagara, Y., Sisk, A., and Mucke, L. (2000) Dopaminergic loss and inclusion body formation in alpha-synuclein mice: Implications for neurodegenerative disorders Science 287, 1265-1269
    • (2000) Science , vol.287 , pp. 1265-1269
    • Masliah, E.1    Rockenstein, E.2    Veinbergs, I.3    Mallory, M.4    Hashimoto, M.5    Takeda, A.6    Sagara, Y.7    Sisk, A.8    Mucke, L.9


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