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. 2020 Jan 23;13:1399. doi: 10.3389/fnins.2019.01399

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Copyright © 2020 Bernal-Conde, Ramos-Acevedo, Reyes-Hernández, Balbuena-Olvera, Morales-Moreno, Argüero-Sánchez, Schüle and Guerra-Crespo.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Alpha-synuclein interactions in the nucleus, Golgi apparatus, and the endoplasmic reticulum. (1) Human wild type alpha-synuclein (hWT α-syn) can retain methyltransferases in the cytoplasm, thus altering DNA methylation of the SNCA gene. (2) hWT α-syn can also interact with H3K9me1/2 to increase mono- and dimethylation in the DNA. (3) p.A53T and p.A30P monomers bind to HDACS and inhibit histone deacetylation. (4) Decreased epigenetic regulation on the SNCA gene promotes its up-regulation, increasing α-syn transcription and further accumulation. (5) Prefibrillar α-syn can disrupt postraductional processing of dopamine transporter (DAT) in the Golgi apparatus (GA), diminishing its presence in the membrane. (6) α-syn oligomers impair autophagosome formation in the GA. (7) p.A53T monomers inhibit vesicles transport from endoplasmic reticulum (ER) to GA. (8) pS129-α-syn monomers increase unfolded protein response (UPR) activity in the ER. (9) p.A53T and p.A30P monomers increase levels of stress in the ER. (10) α-syn oligomers and fibrils affect SERCA complex in the ER, diminishing cytosolic levels of Ca²⁺. Created with BioRender.