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

81 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

    Fingerprint

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., Mbefo, M. K., Vercruysse, F., Dietler, G., Lee, S. J., Eliezer, D., & 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