α-Synuclein-induced deformation of small unilamellar vesicles
(2022) In QRB Discovery 3.- Abstract
Abstract α-Synuclein is a small neuronal protein that reversibly associates with lipid membranes. The membrane interactions are believed to be central to the healthy function of this protein involved in synaptic plasticity and neurotransmitter release. α-Synuclein has been speculated to induce vesicle fusion as well as fission, processes which are analogous to each other but proceed in different directions and involve different driving forces. In the current work, we analyse α-synuclein-induced small unilamellar vesicle deformation from a thermodynamics point of view. We show that the structures interpreted in the literature as fusion intermediates are in fact a stable deformed state and neither fusion nor vesicle clustering occurs. We... (More)
Abstract α-Synuclein is a small neuronal protein that reversibly associates with lipid membranes. The membrane interactions are believed to be central to the healthy function of this protein involved in synaptic plasticity and neurotransmitter release. α-Synuclein has been speculated to induce vesicle fusion as well as fission, processes which are analogous to each other but proceed in different directions and involve different driving forces. In the current work, we analyse α-synuclein-induced small unilamellar vesicle deformation from a thermodynamics point of view. We show that the structures interpreted in the literature as fusion intermediates are in fact a stable deformed state and neither fusion nor vesicle clustering occurs. We speculate on the driving force for the observed deformation and put forward a hypothesis that α-synuclein self-assembly on the lipid membrane precedes and induces membrane remodelling.
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- author
- Makasewicz, Katarzyna LU ; Wennmalm, Stefan ; Linse, Sara LU and Sparr, Emma LU
- organization
- publishing date
- 2022
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- fission, lipid membrane, membrane remodelling, α-Synuclein
- in
- QRB Discovery
- volume
- 3
- article number
- e10
- publisher
- Cambridge University Press
- external identifiers
-
- pmid:37529290
- scopus:85135595871
- ISSN
- 2633-2892
- DOI
- 10.1017/qrd.2022.9
- language
- English
- LU publication?
- yes
- id
- 75dcece9-7b84-46eb-b9fc-e040ed093bfa
- date added to LUP
- 2022-09-16 15:01:34
- date last changed
- 2024-04-16 11:56:58
@article{75dcece9-7b84-46eb-b9fc-e040ed093bfa,
abstract = {{<p>Abstract α-Synuclein is a small neuronal protein that reversibly associates with lipid membranes. The membrane interactions are believed to be central to the healthy function of this protein involved in synaptic plasticity and neurotransmitter release. α-Synuclein has been speculated to induce vesicle fusion as well as fission, processes which are analogous to each other but proceed in different directions and involve different driving forces. In the current work, we analyse α-synuclein-induced small unilamellar vesicle deformation from a thermodynamics point of view. We show that the structures interpreted in the literature as fusion intermediates are in fact a stable deformed state and neither fusion nor vesicle clustering occurs. We speculate on the driving force for the observed deformation and put forward a hypothesis that α-synuclein self-assembly on the lipid membrane precedes and induces membrane remodelling. </p>}},
author = {{Makasewicz, Katarzyna and Wennmalm, Stefan and Linse, Sara and Sparr, Emma}},
issn = {{2633-2892}},
keywords = {{fission; lipid membrane; membrane remodelling; α-Synuclein}},
language = {{eng}},
publisher = {{Cambridge University Press}},
series = {{QRB Discovery}},
title = {{α-Synuclein-induced deformation of small unilamellar vesicles}},
url = {{http://dx.doi.org/10.1017/qrd.2022.9}},
doi = {{10.1017/qrd.2022.9}},
volume = {{3}},
year = {{2022}},
}