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Residues 2 to 7 of α-synuclein regulate amyloid formation via lipid-dependent and lipid-independent pathways

Citation

Dewison, Katherine and Radford, Sheena E. (2024) Residues 2 to 7 of α-synuclein regulate amyloid formation via lipid-dependent and lipid-independent pathways. University of Leeds. [Dataset] https://doi.org/10.5518/1422

Dataset description

Here, the role of residues 2-7 in the N-terminal region of αSyn are investigated in terms of their ability to regulate amyloid fibril formation in vitro and in vivo. Deletion of these residues (αSynΔN7) slows the rate of fibril formation in vitro and reduces the capacity of the protein to be recruited by wild-type (αSynWT) fibril seeds, despite cryo-EM showing a fibril structure consistent with those of full-length αSyn. Strikingly, fibril formation of αSynΔN7 is not induced by liposomes, despite the protein binding to liposomes with similar affinity to αSynWT. A Caenorhabditis elegans model also showed that αSynΔN7::YFP forms few puncta and lacks motility and lifespan defects typified by expression of αSynWT::YFP.

Subjects: C000 - Biological sciences > C700 - Molecular biology, biophysics & biochemistry
Divisions: Faculty of Biological Sciences > Astbury Centre for Structural Molecular Biology
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LocationType
https://doi.org/10.1101/2024.05.24.595537Publication
License: Creative Commons Attribution 4.0 International (CC BY 4.0)
Date deposited: 29 May 2024 20:05
URI: https://archive.researchdata.leeds.ac.uk/id/eprint/1282

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