N-Terminal Acetylation of α-Synuclein Slows down Its Aggregation Process and Alters the Morphology of the Resulting Aggregates.


Journal

Biochemistry
ISSN: 1520-4995
Titre abrégé: Biochemistry
Pays: United States
ID NLM: 0370623

Informations de publication

Date de publication:
06 09 2022
Historique:
pubmed: 10 8 2022
medline: 9 9 2022
entrez: 9 8 2022
Statut: ppublish

Résumé

Parkinson's disease is associated with the aberrant aggregation of α-synuclein. Although the causes of this process are still unclear, post-translational modifications of α-synuclein are likely to play a modulatory role. Since α-synuclein is constitutively N-terminally acetylated, we investigated how this post-translational modification alters the aggregation behavior of this protein. By applying a three-pronged aggregation kinetics approach, we observed that N-terminal acetylation results in a reduced rate of lipid-induced aggregation and slows down both elongation and fibril-catalyzed aggregate proliferation. An analysis of the amyloid fibrils produced by the aggregation process revealed different morphologies for the acetylated and non-acetylated forms in both lipid-induced aggregation and seed-induced aggregation assays. In addition, we found that fibrils formed by acetylated α-synuclein exhibit a lower β-sheet content. These findings indicate that N-terminal acetylation of α-synuclein alters its lipid-dependent aggregation behavior, reduces its rate of in vitro aggregation, and affects the structural properties of its fibrillar aggregates.

Identifiants

pubmed: 35944093
doi: 10.1021/acs.biochem.2c00104
pmc: PMC9454101
doi:

Substances chimiques

Amyloid 0
Lipids 0
Protein Aggregates 0
alpha-Synuclein 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

1743-1756

Subventions

Organisme : Medical Research Council
ID : MR/W01632X/1
Pays : United Kingdom

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Auteurs

Rosie Bell (R)

Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, U.K.

Rebecca J Thrush (RJ)

Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, U.K.

Marta Castellana-Cruz (M)

Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, U.K.

Marc Oeller (M)

Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, U.K.

Roxine Staats (R)

Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, U.K.

Aishwarya Nene (A)

Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, U.K.

Patrick Flagmeier (P)

Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, U.K.

Catherine K Xu (CK)

Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, U.K.

Sandeep Satapathy (S)

Department of Cell Biology, Blavantik Institute, Harvard Medical School, Boston, Massachusetts 02115, United States.

Celine Galvagnion (C)

Department of Drug Design and Pharmacology, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen DK-2100, Denmark.

Mark R Wilson (MR)

School of Chemistry and Molecular Bioscience, Molecular Horizons Institute, University of Wollongong, Wollongong, NSW 2522, Australia.

Christopher M Dobson (CM)

Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, U.K.

Janet R Kumita (JR)

Department of Pharmacology, University of Cambridge, Cambridge CB2 1PD, U.K.

Michele Vendruscolo (M)

Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, U.K.

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Classifications MeSH