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Volumn 408, Issue 4, 2011, Pages 654-669

Molecular basis for the glycosphingolipid-binding specificity of α-synuclein: Key role of tyrosine 39 in membrane insertion

Author keywords

Alzheimer's amyloid peptide; glycosphingolipid; Langmuir monolayer; Parkinson's disease; synuclein

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[5-16]; CELL SURFACE GLYCOSPHINGOLIPID; GANGLIOSIDE; GLYCINE; GLYCOSPHINGOLIPID; SPHINGOMYELIN; TYROSINE; UNCLASSIFIED DRUG; WATER;

EID: 79954534373     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.03.009     Document Type: Article
Times cited : (96)

References (47)
  • 2
    • 77956994435 scopus 로고    scopus 로고
    • Molecular insights into amyloid regulation by membrane cholesterol and sphingolipids: Common mechanisms in neurodegenerative diseases
    • Fantini J., and Yahi N. Molecular insights into amyloid regulation by membrane cholesterol and sphingolipids: common mechanisms in neurodegenerative diseases Expert Rev. Mol. Med. 12 2010 e27
    • (2010) Expert Rev. Mol. Med. , vol.12 , pp. 27
    • Fantini, J.1    Yahi, N.2
  • 5
    • 77953235479 scopus 로고    scopus 로고
    • Aβ polymerization through interaction with membrane gangliosides
    • Matsuzaki K., Kato K., and Yanagisawa K. Aβ polymerization through interaction with membrane gangliosides Biochim. Biophys. Acta 1801 2010 868 877
    • (2010) Biochim. Biophys. Acta , vol.1801 , pp. 868-877
    • Matsuzaki, K.1    Kato, K.2    Yanagisawa, K.3
  • 6
    • 77955312210 scopus 로고    scopus 로고
    • Amyloidogenic protein-membrane interactions: Mechanistic insight from model systems
    • Butterfield S.M., and Lashuel H.A. Amyloidogenic protein-membrane interactions: mechanistic insight from model systems Angew. Chem. Int. Ed. Engl. 49 2010 5628 5654
    • (2010) Angew. Chem. Int. Ed. Engl. , vol.49 , pp. 5628-5654
    • Butterfield, S.M.1    Lashuel, H.A.2
  • 7
    • 0030823756 scopus 로고    scopus 로고
    • Acceleration of amyloid fibril formation by specific binding of Aβ-(1- 40) peptide to ganglioside-containing membrane vesicles
    • DOI 10.1074/jbc.272.37.22987
    • Choo-Smith L.P., Garzon-Rodriguez W., Glabe C.G., and Surewicz W.K. Acceleration of amyloid fibril formation by specific binding of Aβ-(1-40) peptide to ganglioside-containing membrane vesicles J. Biol. Chem. 272 1997 22987 22990 (Pubitemid 27392420)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.37 , pp. 22987-22990
    • Choo-Smith, L.-P.1    Garzon-Rodriguez, W.2    Glabe, C.G.3    Surewicz, W.K.4
  • 8
    • 33847738814 scopus 로고    scopus 로고
    • Lipid rafts: Structure, function and role in HIV, Alzheimer's and prion diseases
    • Fantini J., Garmy N., Mahfoud R., and Yahi N. Lipid rafts: structure, function and role in HIV, Alzheimer's and prion diseases Expert Rev. Mol. Med. 4 2002 1 22
    • (2002) Expert Rev. Mol. Med. , vol.4 , pp. 1-22
    • Fantini, J.1    Garmy, N.2    Mahfoud, R.3    Yahi, N.4
  • 9
    • 0034968340 scopus 로고    scopus 로고
    • Neuropeptides interact with glycolipid receptors A surface plasmon resonance study
    • DOI 10.1016/S0196-9781(01)00432-6, PII S0196978101004326
    • Valdes-Gonzalez T., Inagawa J., and Ido T. Neuropeptides interact with glycolipid receptors: a surface plasmon resonance study Peptides 22 2001 1099 1106 (Pubitemid 32614134)
    • (2001) Peptides , vol.22 , Issue.7 , pp. 1099-1106
    • Valdes-Gonzalez, T.1    Inagawa, J.2    Ido, T.3
  • 10
    • 0037192816 scopus 로고    scopus 로고
    • Identification of a common sphingolipid-binding domain in Alzheimer, prion, and HIV-1 proteins
    • DOI 10.1074/jbc.M111679200
    • Mahfoud R., Garmy N., Maresca M., Yahi N., Puigserver A., and Fantini J. Identification of a common sphingolipid-binding domain in Alzheimer, prion, and HIV-1 proteins J. Biol. Chem. 277 2002 11292 11296 (Pubitemid 34952893)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.13 , pp. 11292-11296
    • Mahfoud, R.1    Garmy, N.2    Maresca, M.3    Yahi, N.4    Puigserver, A.5    Fantini, J.6
  • 11
    • 50049127374 scopus 로고    scopus 로고
    • A fluorescent sphingolipid binding domain peptide probe interacts with sphingolipids and cholesterol-dependent raft domains
    • Hebbar S., Lee E., Manna M., Steinert S., Kumar G.S., and Wenk M. A fluorescent sphingolipid binding domain peptide probe interacts with sphingolipids and cholesterol-dependent raft domains J. Lipid Res. 49 2008 1077 1089
    • (2008) J. Lipid Res. , vol.49 , pp. 1077-1089
    • Hebbar, S.1    Lee, E.2    Manna, M.3    Steinert, S.4    Kumar, G.S.5    Wenk, M.6
  • 12
    • 0028885854 scopus 로고
    • GM1 ganglioside-bound amyloid β-protein (Aβ): A possible form of preamyloid in Alzheimer's disease
    • Yanagisawa K., Odaka A., Suzuki N., and Ihara Y. GM1 ganglioside-bound amyloid β-protein (Aβ): a possible form of preamyloid in Alzheimer's disease Nat. Med. 1 1995 1062 1066
    • (1995) Nat. Med. , vol.1 , pp. 1062-1066
    • Yanagisawa, K.1    Odaka, A.2    Suzuki, N.3    Ihara, Y.4
  • 13
    • 33847022701 scopus 로고    scopus 로고
    • GM1 specifically interacts with α-synuclein and inhibits fibrillation
    • Martinez Z., Zhu M., Han S., and Fink A.L. GM1 specifically interacts with α-synuclein and inhibits fibrillation Biochemistry 46 2007 1868 1877
    • (2007) Biochemistry , vol.46 , pp. 1868-1877
    • Martinez, Z.1    Zhu, M.2    Han, S.3    Fink, A.L.4
  • 14
    • 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., Chahinian H., Maresca M., Taïeb N., and Yahi N. 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 2010 202 218
    • (2010) J. Mol. Biol. , vol.397 , pp. 202-218
    • Di Pasquale, E.1    Fantini, J.2    Chahinian, H.3    Maresca, M.4    Taïeb, N.5    Yahi, N.6
  • 15
    • 1342329324 scopus 로고    scopus 로고
    • Prion protein is a component of the multimolecular signaling complex involved in T cell activation
    • DOI 10.1016/S0014-5793(04)00029-8
    • Mattei V., Garofalo T., Misasi R., Circella A., Manganelli V., and Lucania G. Prion protein is a component of the multimolecular signaling complex involved in T cell activation FEBS Lett. 560 2004 14 18 (Pubitemid 38264285)
    • (2004) FEBS Letters , vol.560 , Issue.1-3 , pp. 14-18
    • Mattei, V.1    Garofalo, T.2    Misasi, R.3    Circella, A.4    Manganelli, V.5    Lucania, G.6    Pavan, A.7    Sorice, M.8
  • 16
    • 0036306046 scopus 로고    scopus 로고
    • Binding of prion protein to lipid membranes and implications for prion conversion
    • DOI 10.1006/jmbi.2001.5322
    • Sanghera N., and Pinheiro T.J. Binding of prion protein to lipid membranes and implications for prion conversion J. Mol. Biol. 315 2002 1241 1256 (Pubitemid 34729301)
    • (2002) Journal of Molecular Biology , vol.315 , Issue.5 , pp. 1241-1256
    • Sanghera, N.1    Pinheiro, T.J.T.2
  • 18
    • 34447255463 scopus 로고    scopus 로고
    • Formation of Toxic Fibrils of Alzheimer's Amyloid β-Protein-(1-40) by Monosialoganglioside GM1, a Neuronal Membrane Component
    • DOI 10.1016/j.jmb.2007.05.069, PII S0022283607007176
    • Okada T., Wakabayashi M., Ikeda K., and Matsuzaki K. Formation of toxic fibrils of Alzheimer's amyloid β-protein-(1-40) by monosialoganglioside GM1, a neuronal membrane component J. Mol. Biol. 371 2007 481 489 (Pubitemid 47048280)
    • (2007) Journal of Molecular Biology , vol.371 , Issue.2 , pp. 481-489
    • Okada, T.1    Wakabayashi, M.2    Ikeda, K.3    Matsuzaki, K.4
  • 20
    • 0033597931 scopus 로고    scopus 로고
    • Sphingolipid depletion increases formation of the scrapie prion protein in neuroblastoma cells infected with prions
    • Naslavsky N., Shmeeda H., Friedlander G., Yanai A., Futerman A.H., Barenholz Y., and Taraboulos A. Sphingolipid depletion increases formation of the scrapie prion protein in neuroblastoma cells infected with prions J. Biol. Chem. 274 1999 20763 20771
    • (1999) J. Biol. Chem. , vol.274 , pp. 20763-20771
    • Naslavsky, N.1    Shmeeda, H.2    Friedlander, G.3    Yanai, A.4    Futerman, A.H.5    Barenholz, Y.6    Taraboulos, A.7
  • 21
    • 0038386467 scopus 로고    scopus 로고
    • How sphingolipids bind and shape proteins: Molecular basis of lipid-protein interactions in lipid shells, rafts and related biomembrane domains
    • Fantini J. How sphingolipids bind and shape proteins: molecular basis of lipid-protein interactions in lipid shells, rafts and related biomembrane domains Cell. Mol. Life Sci. 60 2003 1027 1032 (Pubitemid 36791909)
    • (2003) Cellular and Molecular Life Sciences , vol.60 , Issue.6 , pp. 1027-1032
    • Fantini, J.1
  • 22
    • 0029731557 scopus 로고    scopus 로고
    • Spc3, a V3 loop-derived synthetic peptide inhibitor of HIV-1 infection, binds to cell surface glycosphingolipids
    • DOI 10.1021/bi961205g
    • Delézay O., Hammache D., Fantini J., and Yahi N. SPC3, a V3 loop-derived synthetic peptide inhibitor of HIV-1 infection, binds to cell surface glycosphingolipids Biochemistry 35 1996 15663 15671 (Pubitemid 26422303)
    • (1996) Biochemistry , vol.35 , Issue.49 , pp. 15663-15671
    • Delezay, O.1    Hammache, D.2    Fantini, J.3    Yahi, N.4
  • 24
    • 33748513877 scopus 로고    scopus 로고
    • Prediction of glycolipid-binding domains from the amino acid sequence of lipid raft-associated proteins: Application to HpaA, a protein involved in the adhesion of Helicobacter pylori to gastrointestinal cells
    • DOI 10.1021/bi060762s
    • Fantini J., Garmy N., and Yahi N. Prediction of glycolipid-binding domains from the amino acid sequence of lipid raft-associated proteins: application to HpaA, a protein involved in the adhesion of Helicobacter pylori to gastrointestinal cells Biochemistry 45 2006 10957 10962 (Pubitemid 44360165)
    • (2006) Biochemistry , vol.45 , Issue.36 , pp. 10957-10962
    • Fantini, J.1    Garmy, N.2    Yahi, N.3
  • 25
    • 64849096118 scopus 로고    scopus 로고
    • The first extracellular domain of the tumour stem cell marker CD133 contains an antigenic ganglioside-binding motif
    • Taïeb N., Maresca M., Guo X.J., Garmy N., Fantini J., and Yahi N. The first extracellular domain of the tumour stem cell marker CD133 contains an antigenic ganglioside-binding motif Cancer Lett. 278 2009 164 173
    • (2009) Cancer Lett. , vol.278 , pp. 164-173
    • Taïeb, N.1    Maresca, M.2    Guo, X.J.3    Garmy, N.4    Fantini, J.5    Yahi, N.6
  • 26
    • 77149159510 scopus 로고    scopus 로고
    • Notch ligand activity is modulated by glycosphingolipid membrane composition in Drosophila melanogaster
    • Hamel S., Fantini J., and Schweisguth F. Notch ligand activity is modulated by glycosphingolipid membrane composition in Drosophila melanogaster J. Cell Biol. 188 2010 581 594
    • (2010) J. Cell Biol. , vol.188 , pp. 581-594
    • Hamel, S.1    Fantini, J.2    Schweisguth, F.3
  • 27
    • 4143064622 scopus 로고    scopus 로고
    • The combinatorial extension method reveals a sphingolipid binding domain on pancreatic bile salt-dependent lipase: Role in secretion
    • DOI 10.1016/j.str.2004.05.016, PII S0969212604002345
    • Aubert-Jousset E., Garmy N., Sbarra V., Fantini J., Sadoulet M.O., and Lombardo D. The combinatorial extension method reveals a sphingolipid binding domain on pancreatic bile salt-dependent lipase: role in secretion Structure 12 2004 1437 1447 (Pubitemid 39092088)
    • (2004) Structure , vol.12 , Issue.8 , pp. 1437-1447
    • Aubert-Jousset, E.1    Garmy, N.2    Sbarra, V.3    Fantini, J.4    Sadoulet, M.-O.5    Lombardo, D.6
  • 28
    • 0032806603 scopus 로고    scopus 로고
    • Selection of ganglioside GM1-binding peptides by using a phage library
    • DOI 10.1016/S0014-5793(99)00962-X, PII S001457939900962X
    • Matsubara T., Ishikawa D., Taki T., Okahata Y., and Sato T. Selection of ganglioside GM1-binding peptides by using a phage library FEBS Lett. 456 1999 253 256 (Pubitemid 29352303)
    • (1999) FEBS Letters , vol.456 , Issue.2 , pp. 253-256
    • Matsubara, T.1    Ishikawa, D.2    Taki, T.3    Okahata, Y.4    Sato, T.5
  • 29
    • 33746925586 scopus 로고    scopus 로고
    • Binding of amyloid β-peptide to ganglioside micelles is dependent on histidine-13
    • DOI 10.1042/BJ20060293
    • Williamson M.P., Suzuki Y., Bourne N.T., and Asakura T. Binding of amyloid β-peptide to ganglioside micelles is dependent on histidine-13 Biochem. J. 397 2006 483 490 (Pubitemid 44187506)
    • (2006) Biochemical Journal , vol.397 , Issue.3 , pp. 483-490
    • Williamson, M.P.1    Suzuki, Y.2    Bourne, N.T.3    Asakura, T.4
  • 30
    • 70350196379 scopus 로고    scopus 로고
    • Surface chemistry of Alzheimer's disease: A Langmuir monolayer approach
    • Thakur G., Micic M., and Leblanc R.M. Surface chemistry of Alzheimer's disease: A Langmuir monolayer approach Colloids Surf., B 74 2009 436 456
    • (2009) Colloids Surf., B , vol.74 , pp. 436-456
    • Thakur, G.1    Micic, M.2    Leblanc, R.M.3
  • 31
    • 0023263405 scopus 로고
    • Local anesthetics and pressure: A comparison of dibucaine binding to lipid monolayers and bilayers
    • DOI 10.1016/0005-2736(87)90400-7
    • Seelig A. Local anesthetics and pressure: a comparison of dibucaine binding to lipid monolayers and bilayers Biochim. Biophys. Acta 899 1987 196 204 (Pubitemid 17086618)
    • (1987) Biochimica et Biophysica Acta - Biomembranes , vol.899 , Issue.2 , pp. 196-204
    • Seelig, A.1
  • 32
    • 0033784943 scopus 로고    scopus 로고
    • Reconstitution of sphingolipid-cholesterol plasma membrane microdomains for studies of virus-glycolipid interactions
    • Hammache D., Piéroni G., Maresca M., Ivaldi S., Yahi N., and Fantini J. Reconstitution of sphingolipid-cholesterol plasma membrane microdomains for studies of virus-glycolipid interactions Methods Enzymol. 312 2000 495 506
    • (2000) Methods Enzymol. , vol.312 , pp. 495-506
    • Hammache, D.1    Piéroni, G.2    Maresca, M.3    Ivaldi, S.4    Yahi, N.5    Fantini, J.6
  • 34
    • 0031755752 scopus 로고    scopus 로고
    • Peripheral-type benzodiazepine receptor function in cholesterol transport. Identification of a putative cholesterol recognition/interaction amino acid sequence and consensus pattern
    • Li H., and Papadopoulos V. Peripheral-type benzodiazepine receptor function in cholesterol transport. Identification of a putative cholesterol recognition/interaction amino acid sequence and consensus pattern Endocrinology 139 1998 4991 4997 (Pubitemid 28533447)
    • (1998) Endocrinology , vol.139 , Issue.12 , pp. 4991-4997
    • Li, H.1    Papadopoulos, V.2
  • 35
    • 77952305288 scopus 로고    scopus 로고
    • Cholesterol interaction with proteins that partition into membrane domains: An overview
    • Epand R.M., Thomas A., Brasseur R., and Epand R.F. Cholesterol interaction with proteins that partition into membrane domains: an overview Subcell. Biochem. 51 2010 253 278
    • (2010) Subcell. Biochem. , vol.51 , pp. 253-278
    • Epand, R.M.1    Thomas, A.2    Brasseur, R.3    Epand, R.F.4
  • 36
    • 4444317733 scopus 로고    scopus 로고
    • Cholesterol and the activity of bacterial toxins
    • DOI 10.1016/j.femsle.2004.07.059, PII S0378109704005841
    • Palmer M. Cholesterol and the activity of bacterial toxins FEMS Microbiol. Lett. 238 2004 281 289 (Pubitemid 39195152)
    • (2004) FEMS Microbiology Letters , vol.238 , Issue.2 , pp. 281-289
    • Palmer, M.1
  • 38
    • 42749095305 scopus 로고    scopus 로고
    • Driving force of binding of amyloid β-protein to lipid bilayers
    • Ikeda K., and Matsuzaki K. Driving force of binding of amyloid β-protein to lipid bilayers Biochem. Biophys. Res. Commun. 370 2008 525 529
    • (2008) Biochem. Biophys. Res. Commun. , vol.370 , pp. 525-529
    • Ikeda, K.1    Matsuzaki, K.2
  • 39
    • 72649096531 scopus 로고    scopus 로고
    • Up-and-down topological mode of amyloid β-peptide lying on hydrophilic/hydrophobic interface of ganglioside clusters
    • Utsumi M., Yamaguchi Y., Sasakawa H., Yamamoto N., Yanagisawa K., and Kato K. Up-and-down topological mode of amyloid β-peptide lying on hydrophilic/hydrophobic interface of ganglioside clusters Glycoconjugate J. 26 2009 999 1006
    • (2009) Glycoconjugate J. , vol.26 , pp. 999-1006
    • Utsumi, M.1    Yamaguchi, Y.2    Sasakawa, H.3    Yamamoto, N.4    Yanagisawa, K.5    Kato, K.6
  • 42
    • 0033973421 scopus 로고    scopus 로고
    • NACP/α-synuclein-positive filamentous inclusions in astrocytes and oligodendrocytes of Parkinson's disease brains
    • Wakabayashi K., Hayashi S., Yoshimoto M., Kudo H., and Takahashi H. NACP/α-synuclein-positive filamentous inclusions in astrocytes and oligodendrocytes of Parkinson's disease brains Acta Neuropathol. 99 2000 14 20 (Pubitemid 30093433)
    • (2000) Acta Neuropathologica , vol.99 , Issue.1 , pp. 14-20
    • Wakabayashi, K.1    Hayashi, S.2    Yoshimoto, M.3    Kudo, H.4    Takahashi, H.5
  • 44
    • 0031715982 scopus 로고    scopus 로고
    • Protein structure alignment by incremental combinatorial extension (CE) of the optimal path
    • Shindyalov I.N., and Bourne P.E. Protein structure alignment by incremental combinatorial extension (CE) of the optimal path Protein Eng. 11 1998 739 747 (Pubitemid 28434482)
    • (1998) Protein Engineering , vol.11 , Issue.9 , pp. 739-747
    • Shindyalov, I.N.1    Bourne, P.E.2
  • 45
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • DOI 10.1002/elps.1150181505
    • Guex N., and Peitsch M.C. SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modelling Electrophoresis 18 1997 2714 2723 (Pubitemid 28059943)
    • (1997) Electrophoresis , vol.18 , Issue.15 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 46
    • 15744362063 scopus 로고    scopus 로고
    • Structure and dynamics of micelle-bound human α-synuclein
    • DOI 10.1074/jbc.M411805200
    • Ulmer T.S., Bax A., Cole N.B., and Nussbaum R.L. Structure and dynamics of micelle-bound human α-synuclein J. Biol. Chem. 280 2005 9595 9603 (Pubitemid 40409655)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.10 , pp. 9595-9603
    • Ulmer, T.S.1    Bax, A.2    Cole, N.B.3    Nussbaum, R.L.4
  • 47
    • 0032483035 scopus 로고    scopus 로고
    • Solution structure of amyloid β-peptide(1-40) in a water-micelle environment. Is the membrane-spanning domain where we think it is?
    • DOI 10.1021/bi972979f, PII S0006296097029796
    • Coles M., Bicknell W., Watson A.A., Fairlie D.P., and Crai D.J. Solution structure of amyloid β-peptide(1-40) in a water-micelle environment. Is the membrane-spanning domain where we think it is? Biochemistry 37 1998 11064 11077 (Pubitemid 28368933)
    • (1998) Biochemistry , vol.37 , Issue.31 , pp. 11064-11077
    • Coles, M.1    Bicknell, W.2    Watson, R.A.3    Fairlie, D.P.4    Craik, D.J.5


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