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. 2020 Jun 17;14:577. doi: 10.3389/fnins.2020.00577

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Copyright © 2020 O’Hara, Pawar, Kalia and Kalia.

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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Contribution of mutant LRRK2 to cell-to-cell transmission of α-synuclein. Increased kinase activity of mutant LRRK2 can phosphorylate Rab35 affecting its interaction with its substrates, and eventually preventing the endosome-lysosmal degradation of α-synuclein aggregates. This in turn can increase the mobile cytosolic pools of α-synuclein aggregate seeds which can get released into the extracellular space in exosomes. These seeds can then be taken up into the cytosol of neighboring neurons where they can promote aggregation of α-synuclein monomers into oligomers and fibrils.