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. 2018 Feb 22;8:3455. doi: 10.1038/s41598-018-21931-8

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© The Author(s) 2018

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Deletion of predicted FADD binding domain in LRRK2 ARM prevents recruitment of LRRK2 to FADD complexes. Full-length mutant R1441C-LRRK2, or R1441C-LRRK2 lacking the predicted FADD binding domain (specifically, the residues within this motif with the highest identity, 538-547), was co-transfected with V5-FADD in HEK293T cells. Following 48 h of expression cells were fixed and immunostained for Flag (LRRK2) and V5 (FADD), together with DAPI. Over-expression of FADD leads to its localization to so-called Death Effector Filaments (DEFs) that subsequently recruits LRRK2. Deletion of the motif predicted to mediate binding to FADD (ΔFBD; FADD-binding domain) prevents this recruitment, leaving mutant LRRK2 diffusely localized in the cytoplasm.