The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
N-terminal Acetylation Stabilizes N-terminal Helicity in Lipid- and Micelle-bound α-Synuclein and Increases Its Affinity for Physiological Membranes
Open accessAbstract
The Parkinson disease protein α-synuclein is N-terminally acetylated, but most in vitro studies have been performed using unacetylated α-synuclein. Binding to lipid membranes is considered key to the still poorly understood function of α-synuclein. We report the effects of N-terminal acetylation on α-synuclein binding to lipid vesicles of different composition and curvature and to micelles composed of the detergents β-octyl-glucoside (BOG) and SDS. In the presence of SDS, N-terminal acetylation results in a slightly increased helicity for the N-terminal ~10 residues of the protein, likely due to the stabilization of N-terminal fraying through the formation of a helix cap motif. In the presence of BOG, a detergent used in previous isolations of helical oligomeric forms of α-synuclein, the N-terminally acetylated protein adopts a novel conformation in which the N-terminal ~30 residues bind the detergent micelle in a partly helical conformation, whereas the remainder of the protein remains unbound and disordered. Binding of α-synuclein to lipid vesicles with high negative charge content is essentially unaffected by N-terminal acetylation irrespective of curvature, but binding to vesicles of lower negative charge content is increased, with stronger binding observed for vesicles with higher curvature. Thus, the naturally occurring N-terminally acetylated form of α-synuclein exhibits stabilized helicity at its N terminus and increased affinity for lipid vesicles similar to synaptic vesicles, a binding target of the protein in vivo. Furthermore, the novel BOG-bound state of N-terminally acetylated α-synuclein may serve as a model of partly helical membrane-bound intermediates with a role in α-synuclein function and dysfunction.
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Cites
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“acetylation (24, 25) or by an N-terminal fusion-protein remnant (26).”
BackgroundA soluble α-synuclein construct forms a dynamic tetramer
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α‐Synuclein produces a long‐lasting increase in neurotransmitter release
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Cited by
Structural disorder of monomeric α-synuclein persists in mammalian cells
Theillet, F.-X., Binolfi, A., Bekei, B., Martorana, A., Rose, H. M., Stuiver, M., Verzini, S., Lorenz, D., van Rossum, M., Goldfarb, D., et al. (2016) · Nature · doi:10.1038/nature16531 · Cited by 868
Cell Biology and Pathophysiology of α-Synuclein
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The Synaptic Function of α-Synuclein
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Dysregulated Lipid Metabolism and Its Role in α-Synucleinopathy in Parkinson’s Disease
Alecu, I., & Bennett, S. A. L. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00328 · Cited by 258
Exposure to bacterial endotoxin generates a distinct strain of α-synuclein fibril
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Self-citation
Metadata
- Authors
- Dikiy, I., & Eliezer, D.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2014-02
- Volume
- 289
- Issue
- 6
- Pages
- 3652-3665
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2038286309
- Cited by
- 188
- References
- 9
- FWCI
- 6.46
- Type
- journal article
- Language
- en
- Open access
- hybrid
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