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. 2021 May 11;11(5):718. doi: 10.3390/biom11050718

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© 2021 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).

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Proposed model of the interaction between αSyn and VDAC on the cytosolic surface of mitochondria. Monomeric αSyn binds VDAC and modulates its electrophysiological activity promoting the transition from the open to the closed state. No information is available so far about αSyn oligomers or fibrils and VDAC. The OMM β-barrel proteins, VDAC and TOM40, promote the αSyn translocation from cytosol to IMS of mitochondria, where it is believed responsible of the impairment of electron transport system complex I/III activity. Moreover, αSyn is involved in the modulation of calcium influx into mitochondria from endoplasmic reticulum (ER). Original figure created with Smart Servier Medical Art tools (https://smart.servier.com, 2021).