TY - JOUR
T1 - The H50Q mutation enhances αα-synuclein aggregation, secretion, and toxicity
AU - Khalaf, Ossama
AU - Fauvet, Bruno
AU - Oueslati, Abid
AU - Dikiy, Igor
AU - Mahul-Mellier, Anne Laure
AU - Ruggeri, Francesco Simone
AU - Mbefo, Martial K.
AU - Vercruysse, Filip
AU - Dietler, Giovanni
AU - Lee, Seung Jae
AU - Eliezer, David
AU - Lashuel, Hilal A.
PY - 2014/8/8
Y1 - 2014/8/8
N2 - 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.
AB - 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.
U2 - 10.1074/jbc.M114.553297
DO - 10.1074/jbc.M114.553297
M3 - Article
C2 - 24936070
AN - SCOPUS:84905852264
SN - 0021-9258
VL - 289
SP - 21856
EP - 21876
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 32
ER -