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TitleA novel alpha-synuclein K58N missense variant in a patient with Parkinson's disease.
Journal, issue, pagesmedRxiv, Year 2025
Publish dateFeb 14, 2025
AuthorsMohammed Al-Azzani / Sandrina Weber / Nagendran Ramalingam / Maria Ramón / Liana Shvachiy / Gonçalo Mestre / Michael Zech / Kevin Sicking / Alain Ibáñez de Opakua / Vidyashree Jayanthi / Leslie Amaral / Aishwarya Agarwal / Aswathy Chandran / Susana R Chaves / Juliane Winkelmann / Claudia Trenkwalder / Maike Schwager / Silke Pauli / Ulf Dettmer / Claudio O Fernández / Janin Lautenschläger / Markus Zweckstetter / Ruben Fernandez Busnadiego / Brit Mollenhauer / Tiago Fleming Outeiro /
PubMed AbstractMutations and multiplications in the SNCA , encoding alpha-synuclein (aSyn), are associated with familial forms of Parkinson's disease (PD). We report the identification of a novel missense mutation ...Mutations and multiplications in the SNCA , encoding alpha-synuclein (aSyn), are associated with familial forms of Parkinson's disease (PD). We report the identification of a novel missense mutation (NM_000345.4, cDNA 174G>C; protein K58N) in a PD patient using whole exome sequencing, and describe comprehensive molecular and cellular analysss of the effects of this novel mutation. The patient exhibited typical sporadic PD with early onset and a benign disease course. Biophysical studies revealed that the K58N substitution causes local structural effects, disrupts binding to membranes, and enhances aSyn in vitro aggregation. K58N aSyn produces fewer inclusions per cell, and fails to undergo condensate formation. The mutation increases the cytoplasmic distribution of the protein, and has minimal effect on the dynamic reversibility of serine-129 phosphorylation. In total, the identification of this novel mutation advances our understanding of aSyn biology and pathobiology.
External linksmedRxiv / PubMed:39990587 / PubMed Central
MethodsEM (single particle)
Resolution3.0 - 3.7 Å
Structure data

52166

9hgs

EMDB-52166, PDB-9hgs:
In vitro grown G14R Alpha-Synuclein Fibrils
Method: EM (single particle) / Resolution: 3.0 Å

52458

9hxa

EMDB-52458, PDB-9hxa:
In vitro grown K58N Alpha-Synuclein Fibrils
Method: EM (single particle) / Resolution: 3.7 Å

Source
  • homo sapiens (human)
KeywordsPROTEIN FIBRIL / Alpha-Synuclein / G14R Mutation / Fibrils / Cryo-EM / Protein Aggregation / Amyloid Structure / K58N Mutation

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