The H50Q mutation enhances αα-synuclein aggregation, secretion, and toxicity

Ossama Khalaf, Bruno Fauvet, Abid Oueslati, Igor Dikiy, Anne Laure Mahul-Mellier, Francesco Simone Ruggeri, Martial K. Mbefo, Filip Vercruysse, Giovanni Dietler, Seung Jae Lee, David Eliezer, Hilal A. Lashuel

Research output: Contribution to journalArticle

74 Citations (Scopus)

Abstract

Background: A new SNCA mutation, H50Q, has been linked to familial Parkinson disease (PD). Results: The H50Q mutation does not affect the structure, membrane binding, or subcellular localization of α-Syn but alters its pathogenic properties. Conclusion: The H50Q mutation increases α-Syn aggregation, secretion, and extracellular toxicity. Significance: α-Syn mutations contribute to the pathogenesis of PD via multiple mechanisms.

Original languageEnglish
Pages (from-to)21856-21876
Number of pages21
JournalJournal of Biological Chemistry
Volume289
Issue number32
DOIs
Publication statusPublished - 8 Aug 2014
Externally publishedYes

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Synucleins
Toxicity
Agglomeration
Membrane structures
Mutation
Parkinson Disease
Membranes

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Cite this

Khalaf, O., Fauvet, B., Oueslati, A., Dikiy, I., Mahul-Mellier, A. L., Ruggeri, F. S., ... Lashuel, H. A. (2014). The H50Q mutation enhances αα-synuclein aggregation, secretion, and toxicity. Journal of Biological Chemistry, 289(32), 21856-21876. https://doi.org/10.1074/jbc.M114.553297

The H50Q mutation enhances αα-synuclein aggregation, secretion, and toxicity. / Khalaf, Ossama; Fauvet, Bruno; Oueslati, Abid; Dikiy, Igor; Mahul-Mellier, Anne Laure; Ruggeri, Francesco Simone; Mbefo, Martial K.; Vercruysse, Filip; Dietler, Giovanni; Lee, Seung Jae; Eliezer, David; Lashuel, Hilal A.

In: Journal of Biological Chemistry, Vol. 289, No. 32, 08.08.2014, p. 21856-21876.

Research output: Contribution to journalArticle

Khalaf, O, Fauvet, B, Oueslati, A, Dikiy, I, Mahul-Mellier, AL, Ruggeri, FS, Mbefo, MK, Vercruysse, F, Dietler, G, Lee, SJ, Eliezer, D & Lashuel, HA 2014, 'The H50Q mutation enhances αα-synuclein aggregation, secretion, and toxicity', Journal of Biological Chemistry, vol. 289, no. 32, pp. 21856-21876. https://doi.org/10.1074/jbc.M114.553297
Khalaf O, Fauvet B, Oueslati A, Dikiy I, Mahul-Mellier AL, Ruggeri FS et al. The H50Q mutation enhances αα-synuclein aggregation, secretion, and toxicity. Journal of Biological Chemistry. 2014 Aug 8;289(32):21856-21876. https://doi.org/10.1074/jbc.M114.553297
Khalaf, Ossama ; Fauvet, Bruno ; Oueslati, Abid ; Dikiy, Igor ; Mahul-Mellier, Anne Laure ; Ruggeri, Francesco Simone ; Mbefo, Martial K. ; Vercruysse, Filip ; Dietler, Giovanni ; Lee, Seung Jae ; Eliezer, David ; Lashuel, Hilal A. / The H50Q mutation enhances αα-synuclein aggregation, secretion, and toxicity. In: Journal of Biological Chemistry. 2014 ; Vol. 289, No. 32. pp. 21856-21876.
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