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. 2021 Aug 9;14:686995. doi: 10.3389/fnmol.2021.686995

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Copyright © 2021 Tejido, Pakravan and Bosch.

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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Summary of the acetylation sites in FUS and its potential effects on FUS-ALS pathology [based on the results obtained in the study of Arenas et al. (2020)]. Acetylation of the FUS RRM (K315/316) by both acetylation mimetics and HDAC pan-inhibition (using a DACi cocktail) decreased FUS ability to bind to RNA. Prevention of RNA binding reduces cytoplasmic inclusions and FUS colocalization with stress granules. Thus, FUS acetylation on RRM sites has a positive effect on FUS-ALS pathology. On the other hand, FUS NLS region (K510 site) proved to be acetylated by acetylation mimetics, CBP or pan-HDAC inhibition. Acetylation of the K510 residue results in the loss of affinity with Transportin-1 leading to increased FUS mislocalization. Thus, FUS acetylation on the NLS site has a negative effect on FUS-ALS pathology.