Structural and functional characterization of two alpha-synuclein strains
10.1038/ncomms3575
Crossref journal-article
Springer Science and Business Media LLC
Nature Communications (297)
Authors 11
  1. Luc Bousset (first)
  2. Laura Pieri (additional)
  3. Gemma Ruiz-Arlandis (additional)
  4. Julia Gath (additional)
  5. Poul Henning Jensen (additional)
  6. Birgit Habenstein (additional)
  7. Karine Madiona (additional)
  8. Vincent Olieric (additional)
  9. Anja Böckmann (additional)
  10. Beat H. Meier (additional)
  11. Ronald Melki (additional)
References 51 Referenced 787
  1. Ross, C. A. & Poirier, M. A. Protein aggregation and neurodegenerative disease. Nat. Med. 10 Suppl, S10-7 (2004). / Nat. Med. by CA Ross (2004)
  2. Goedert, M. Alpha-synuclein and neurodegenerative diseases. Nat. Rev. Neurosci. 2, 492–501 (2001). (10.1038/35081564) / Nat. Rev. Neurosci. by M Goedert (2001)
  3. Spillantini, M. G., Crowther, R. A., Jakes, R., Hasegawa, M. & Goedert, M. 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). (10.1073/pnas.95.11.6469) / Proc. Natl Acad. Sci. USA by MG Spillantini (1998)
  4. Lee, H. J., Choi, C. & Lee, S. J. Membrane-bound alpha-synuclein has a high aggregation propensity and the ability to seed the aggregation of the cytosolic form. J. Biol. Chem. 277, 671–678 (2002). (10.1074/jbc.M107045200) / J. Biol. Chem. by HJ Lee (2002)
  5. Jensen, P. H., Nielsen, M. S., Jakes, R., Dotti, C. G. & Goedert, M. Binding of alpha-synuclein to brain vesicles is abolished by familial Parkinson’s disease mutation. J. Biol. Chem. 273, 26292–26294 (1998). (10.1074/jbc.273.41.26292) / J. Biol. Chem. by PH Jensen (1998)
  6. Uversky, V. N. & Eliezer, D. Biophysics of Parkinson’s disease: structure and aggregation of alpha-synuclein. Curr. Protein Pept. Sci. 10, 483–499 (2009). (10.2174/138920309789351921) / Curr. Protein Pept. Sci. by VN Uversky (2009)
  7. Goldberg, M. S. & Lansbury, P. T. Jr. Is there a cause-and effect relationship between alpha-synuclein fibrilization and Parkinson’s disease? Nat. Cell Biol. 2, E115–E119 (2000). (10.1038/35017124) / Nat. Cell Biol. by MS Goldberg (2000)
  8. Caughey, B. & Lansbury, P. T. Jr Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu. Rev. Neurosci. 26, 267–298 (2003). (10.1146/annurev.neuro.26.010302.081142) / Annu. Rev. Neurosci. by B Caughey (2003)
  9. Winner, B. et al. in vivo demonstration that alpha-synuclein oligomers are toxic. Proc. Natl Acad. Sci. USA 108, 4194–4199 (2011). (10.1073/pnas.1100976108) / Proc. Natl Acad. Sci. USA by B Winner (2011)
  10. Danzer, K. M. et al. Different species of alpha-synuclein oligomers induce calcium influx and seeding. J. Neurosci. 27, 9220–9232 (2007). (10.1523/JNEUROSCI.2617-07.2007) / J. Neurosci. by KM Danzer (2007)
  11. Pieri, L., Madiona, K., Bousset, L. & Melki, R. Fibrillar alpha-synuclein and huntingtin exon 1 assemblies are toxic to the cells. Biophys. J. 102, 2894–2905 (2012). (10.1016/j.bpj.2012.04.050) / Biophys. J. by L Pieri (2012)
  12. Prusiner, S. B. Cell biology. A unifying role for prions in neurodegenerative diseases. Science 336, 1511–1513 (2012). (10.1126/science.1222951) / Science by SB Prusiner (2012)
  13. Brundin, P., Melki, R. & Kopito, R. Prion-like transmission of protein aggregates in neurodegenerative diseases. Nat. Rev. Mol. Cell Biol. 11, 301–307 (2010). (10.1038/nrm2873) / Nat. Rev. Mol. Cell Biol. by P Brundin (2010)
  14. Aguzzi, A. & Rajendran, L. The transcellular spread of cytosolic amyloids, prions, and prionoids. Neuron 64, 783–790 (2009). (10.1016/j.neuron.2009.12.016) / Neuron by A Aguzzi (2009)
  15. Conway, K. A., Harper, J. D. & Lansbury, P. T. Accelerated in vitro fibril formation by a mutant alpha-synuclein linked to early-onset Parkinson disease. Nat. Med. 4, 1318–1320 (1998). (10.1038/3311) / Nat. Med. by KA Conway (1998)
  16. Wood, S. J. et al. alpha-synuclein fibrillogenesis is nucleation-dependent. Implications for the pathogenesis of Parkinson’s disease. J. Biol. Chem. 274, 19509–19512 (1999). (10.1074/jbc.274.28.19509) / J. Biol. Chem. by SJ Wood (1999)
  17. Uversky, V. N., Li, J. & Fink, A. L. Evidence for a partially folded intermediate in alpha-synuclein fibril formation. J. Biol. Chem. 276, 10737–10744 (2001). (10.1074/jbc.M010907200) / J. Biol. Chem. by VN Uversky (2001)
  18. Desplats, P. et al. Inclusion formation and neuronal cell death through neuron-to-neuron transmission of alpha-synuclein. Proc. Natl Acad. Sci. USA 106, 13010–13015 (2009). (10.1073/pnas.0903691106) / Proc. Natl Acad. Sci. USA by P Desplats (2009)
  19. Hansen, C. et al. alpha-Synuclein propagates from mouse brain to grafted dopaminergic neurons and seeds aggregation in cultured human cells. J. Clin. Invest. 121, 715–725 (2011). (10.1172/JCI43366) / J. Clin. Invest. by C Hansen (2011)
  20. Luk, K. C. et al. Pathological alpha-synuclein transmission initiates Parkinson-like neurodegeneration in nontransgenic mice. Science 338, 949–953 (2012). (10.1126/science.1227157) / Science by KC Luk (2012)
  21. Kordower, J. H., Chu, Y., Hauser, R. A., Freeman, T. B. & Olanow, C. W. Lewy body-like pathology in long-term embryonic nigral transplants in Parkinson’s disease. Nat. Med. 14, 504–506 (2008). (10.1038/nm1747) / Nat. Med. by JH Kordower (2008)
  22. Li, J. Y. et al. Lewy bodies in grafted neurons in subjects with Parkinson’s disease suggest host-to-graft disease propagation. Nat. Med. 14, 501–503 (2008). (10.1038/nm1746) / Nat. Med. by JY Li (2008)
  23. Mougenot, A. L. et al. Prion-like acceleration of a synucleinopathy in a transgenic mouse model. Neurobiol. Aging 33, 2225–2228 (2012). (10.1016/j.neurobiolaging.2011.06.022) / Neurobiol. Aging by AL Mougenot (2012)
  24. Luk, K. C. et al. Intracerebral inoculation of pathological alpha-synuclein initiates a rapidly progressive neurodegenerative alpha-synucleinopathy in mice. J. Exp. Med. 209, 975–986 (2012). (10.1084/jem.20112457) / J. Exp. Med. by KC Luk (2012)
  25. Braak, H. et al. Staging of brain pathology related to sporadic Parkinson’s disease. Neurobiol. Aging 24, 197–211 (2003). (10.1016/S0197-4580(02)00065-9) / Neurobiol. Aging by H Braak (2003)
  26. Bruce, M., Fraser, H., McBride, P., Scott, J. & Dickinson, A. The basis of strain variation in scrapie. InPrion Diseases of Humans and Animals 497–508 (1992).
  27. Ohhashi, Y., Ito, K., Toyama, B. H., Weissman, J. S. & Tanaka, M. Differences in prion strain conformations result from non-native interactions in a nucleus. Nat. Chem. Biol. 6, 225–230 (2010). (10.1038/nchembio.306) / Nat. Chem. Biol. by Y Ohhashi (2010)
  28. Tanaka, M., Collins, S. R., Toyama, B. H. & Weissman, J. S. The physical basis of how prion conformations determine strain phenotypes. Nature 442, 585–589 (2006). (10.1038/nature04922) / Nature by M Tanaka (2006)
  29. Petkova, A. T. et al. Self-propagating, molecular-level polymorphism in Alzheimer’s beta-amyloid fibrils. Science 307, 262–265 (2005). (10.1126/science.1105850) / Science by AT Petkova (2005)
  30. van Raaij, M. E., Segers-Nolten, I. M. & Subramaniam, V. Quantitative morphological analysis reveals ultrastructural diversity of amyloid fibrils from alpha-synuclein mutants. Biophys. J. 91, L96–L98 (2006). (10.1529/biophysj.106.090449) / Biophys. J. by ME van Raaij (2006)
  31. Hoyer, W. et al. Dependence of alpha-synuclein aggregate morphology on solution conditions. J. Mol. Biol. 322, 383–393 (2002). (10.1016/S0022-2836(02)00775-1) / J. Mol. Biol. by W Hoyer (2002)
  32. Paleologou, K. E. et al. Detection of elevated levels of soluble alpha-synuclein oligomers in post-mortem brain extracts from patients with dementia with Lewy bodies. Brain 132, 1093–1101 (2009). (10.1093/brain/awn349) / Brain by KE Paleologou (2009)
  33. Heise, H. et al. Molecular-level secondary structure, polymorphism, and dynamics of full-length alpha-synuclein fibrils studied by solid-state NMR. Proc. Natl Acad. Sci. USA 102, 15871–15876 (2005). (10.1073/pnas.0506109102) / Proc. Natl Acad. Sci. USA by H Heise (2005)
  34. Gath, J. et al. Solid-state NMR sequential assignments of alpha-synuclein. Biomol. NMR Assign. 6, 51–55 (2012). (10.1007/s12104-011-9324-3) / Biomol. NMR Assign. by J Gath (2012)
  35. Gath, J. et al. Solid-state NMR sequential assignments of a new polymorph of α-synuclein. Biomol. NMR Assign in press.
  36. Lv, G. et al. Structural comparison of mouse and human alpha-synuclein amyloid fibrils by solid-state NMR. J. Mol. Biol. 420, 99–111 (2012). (10.1016/j.jmb.2012.04.009) / J. Mol. Biol. by G Lv (2012)
  37. Karpinar, D. P. et al. Pre-fibrillar alpha-synuclein variants with impaired beta-structure increase neurotoxicity in Parkinson’s disease models. EMBO J. 28, 3256–3268 (2009). (10.1038/emboj.2009.257) / EMBO J. by DP Karpinar (2009)
  38. Comellas, G., Lemkau, L. R., Zhou, D. H., George, J. M. & Rienstra, C. M. Structural intermediates during alpha-synuclein fibrillogenesis on phospholipid vesicles. J. Am. Chem. Soc. 134, 5090–5099 (2012). (10.1021/ja209019s) / J. Am. Chem. Soc. by G Comellas (2012)
  39. Cornilescu, G., Delaglio, F. & Bax, A. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 13, 289–302 (1999). (10.1023/A:1008392405740) / J. Biomol. NMR by G Cornilescu (1999)
  40. Der-Sarkissian, A., Jao, C. C., Chen, J. & Langen, R. Structural organization of alpha-synuclein fibrils studied by site-directed spin labeling. J. Biol. Chem. 278, 37530–37535 (2003). (10.1074/jbc.M305266200) / J. Biol. Chem. by A Der-Sarkissian (2003)
  41. Chen, M., Margittai, M., Chen, J. & Langen, R. Investigation of alpha-synuclein fibril structure by site-directed spin labelling. J. Biol. Chem. 282, 24970–24979 (2007). (10.1074/jbc.M700368200) / J. Biol. Chem. by M Chen (2007)
  42. Miake, H., Mizusawa, H., Iwatsubo, T. & Hasegawa, M. Biochemical characterization of the core structure of alpha-synuclein filaments. J. Biol. Chem. 277, 19213–19219 (2002). (10.1074/jbc.M110551200) / J. Biol. Chem. by H Miake (2002)
  43. Freundt, E. C. et al. Neuron-to-neuron transmission of alpha-synuclein fibrils through axonal transport. Ann. Neurol. 72, 517–524 (2012). (10.1002/ana.23747) / Ann. Neurol. by EC Freundt (2012)
  44. Uversky, V. N. A protein-chameleon: conformational plasticity of alpha-synuclein, a disordered protein involved in neurodegenerative disorders. J. Biomol. Struct. Dyn. 21, 211–234 (2003). (10.1080/07391102.2003.10506918) / J. Biomol. Struct. Dyn. by VN Uversky (2003)
  45. Braak, H., Ghebremedhin, E., Rub, U., Bratzke, H. & Del Tredici, K. Stages in the development of Parkinson’s disease-related pathology. Cell Tissue Res. 318, 121–134 (2004). (10.1007/s00441-004-0956-9) / Cell Tissue Res. by H Braak (2004)
  46. Ghee, M., Melki, R., Michot, N. & Mallet, J. PA700, the regulatory complex of the 26S proteasome, interferes with alpha-synuclein assembly. FEBS J. 272, 4023–4033 (2005). (10.1111/j.1742-4658.2005.04776.x) / FEBS J. by M Ghee (2005)
  47. Schuck, P. Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling. Biophys. J. 78, 1606–1619 (2000). (10.1016/S0006-3495(00)76713-0) / Biophys. J. by P Schuck (2000)
  48. Schuck, P., Perugini, M. A., Gonzales, N. R., Howlett, G. J. & Schubert, D. Size-distribution analysis of proteins by analytical ultracentrifugation: strategies and application to model systems. Biophys. J. 82, 1096–1111 (2002). (10.1016/S0006-3495(02)75469-6) / Biophys. J. by P Schuck (2002)
  49. Seshadri, S., Khurana, R. & Fink, A. L. Fourier transform infrared spectroscopy in analysis of protein deposits. Methods. Enzymol. 309, 559–576 (1999). (10.1016/S0076-6879(99)09038-2) / Methods. Enzymol. by S Seshadri (1999)
  50. Schägger, H. & Von Jagow, G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100kDa. Anal. Biochem. 166, 368–379 (1987). (10.1016/0003-2697(87)90587-2) / Anal. Biochem. by H Schägger (1987)
  51. Reutelingsperger, C. P. & van Heerde, W. L. Annexin V, the regulator of phosphatidylserine-catalyzed inflammation and coagulation during apoptosis. Cell Mol. Life Sci. 53, 527–532 (1997). (10.1007/s000180050067) / Cell Mol. Life Sci. by CP Reutelingsperger (1997)
Dates
Type When
Created 11 years, 10 months ago (Oct. 10, 2013, 6:46 a.m.)
Deposited 2 years, 7 months ago (Jan. 5, 2023, 8:20 p.m.)
Indexed 57 minutes ago (Aug. 26, 2025, 11:25 p.m.)
Issued 11 years, 10 months ago (Oct. 10, 2013)
Published 11 years, 10 months ago (Oct. 10, 2013)
Published Online 11 years, 10 months ago (Oct. 10, 2013)
Funders 0

None

@article{Bousset_2013, title={Structural and functional characterization of two alpha-synuclein strains}, volume={4}, ISSN={2041-1723}, url={http://dx.doi.org/10.1038/ncomms3575}, DOI={10.1038/ncomms3575}, number={1}, journal={Nature Communications}, publisher={Springer Science and Business Media LLC}, author={Bousset, Luc and Pieri, Laura and Ruiz-Arlandis, Gemma and Gath, Julia and Jensen, Poul Henning and Habenstein, Birgit and Madiona, Karine and Olieric, Vincent and Böckmann, Anja and Meier, Beat H. and Melki, Ronald}, year={2013}, month=oct }