The number of α-synuclein proteins per vesicle gives insights into its physiological function

Mohammad Amin Abolghassemi Fakhree, Niels Zijlstra, C.C. Raiss, Remco Siero, H. Grabmayr, A.R. Bausch, Christian Blum, Mireille Maria Anna Elisabeth Claessens

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Abstract

Although it is well established that the protein α-synuclein (αS) plays an important role in Parkinson’s disease, its physiological function remains largely unknown. It has been reported to bind membranes and to play a role in membrane remodeling processes. The mechanism by which αS remodels membranes is still debated; it may either affect its physical properties or act as a chaperone for other membrane associated proteins. To obtain insight into the role of αS in membrane remodeling we investigated the number of αS proteins associated with single small vesicles in a neuronal cell model. Using single-molecule microscopy and photo-bleaching approaches, we most frequently found 70 αS-GFPs per vesicle. Although this number is high enough to modulate physical membrane properties, it is also strikingly similar to the number of synaptobrevins, a putative interaction partner of αS, per vesicle. We therefore hypothesize a dual, synergistic role for αS in membrane remodeling
Original languageEnglish
Article number30658
JournalScientific reports
Volume6
Issue number30658
DOIs
Publication statusPublished - 2016

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Synucleins
Membranes
Proteins
Protein S
R-SNARE Proteins
Parkinson Disease
Membrane Proteins

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title = "The number of α-synuclein proteins per vesicle gives insights into its physiological function",
abstract = "Although it is well established that the protein α-synuclein (αS) plays an important role in Parkinson’s disease, its physiological function remains largely unknown. It has been reported to bind membranes and to play a role in membrane remodeling processes. The mechanism by which αS remodels membranes is still debated; it may either affect its physical properties or act as a chaperone for other membrane associated proteins. To obtain insight into the role of αS in membrane remodeling we investigated the number of αS proteins associated with single small vesicles in a neuronal cell model. Using single-molecule microscopy and photo-bleaching approaches, we most frequently found 70 αS-GFPs per vesicle. Although this number is high enough to modulate physical membrane properties, it is also strikingly similar to the number of synaptobrevins, a putative interaction partner of αS, per vesicle. We therefore hypothesize a dual, synergistic role for αS in membrane remodeling",
author = "{Abolghassemi Fakhree}, {Mohammad Amin} and Niels Zijlstra and C.C. Raiss and Remco Siero and H. Grabmayr and A.R. Bausch and Christian Blum and Claessens, {Mireille Maria Anna Elisabeth}",
year = "2016",
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language = "English",
volume = "6",
journal = "Scientific reports",
issn = "2045-2322",
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The number of α-synuclein proteins per vesicle gives insights into its physiological function. / Abolghassemi Fakhree, Mohammad Amin; Zijlstra, Niels; Raiss, C.C.; Siero, Remco; Grabmayr, H.; Bausch, A.R.; Blum, Christian; Claessens, Mireille Maria Anna Elisabeth.

In: Scientific reports, Vol. 6, No. 30658, 30658, 2016.

Research output: Contribution to journalArticleAcademicpeer-review

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AU - Abolghassemi Fakhree, Mohammad Amin

AU - Zijlstra, Niels

AU - Raiss, C.C.

AU - Siero, Remco

AU - Grabmayr, H.

AU - Bausch, A.R.

AU - Blum, Christian

AU - Claessens, Mireille Maria Anna Elisabeth

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AB - Although it is well established that the protein α-synuclein (αS) plays an important role in Parkinson’s disease, its physiological function remains largely unknown. It has been reported to bind membranes and to play a role in membrane remodeling processes. The mechanism by which αS remodels membranes is still debated; it may either affect its physical properties or act as a chaperone for other membrane associated proteins. To obtain insight into the role of αS in membrane remodeling we investigated the number of αS proteins associated with single small vesicles in a neuronal cell model. Using single-molecule microscopy and photo-bleaching approaches, we most frequently found 70 αS-GFPs per vesicle. Although this number is high enough to modulate physical membrane properties, it is also strikingly similar to the number of synaptobrevins, a putative interaction partner of αS, per vesicle. We therefore hypothesize a dual, synergistic role for αS in membrane remodeling

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