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. 2018 Feb 27;17:34. doi: 10.1186/s12944-018-0684-x

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© The Author(s). 2018

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided 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 Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Fig. 1 — Phos-tag analysis of LRRK2 Y1699C mediated Rab8a phosphorylation. a 293 T cells were transfected with MYC-LRRK2 (Wild type or Y1699C), and FLAG-Rab8a (WT or T72A mutant). Anti-FLAG M2 beads were used for immunoprecipitation. The immunoprecipitated products were detected by using antibody against FLAG. Phosphorylation of overexpressed Rab8a was analysed by a Phos-tag assay (top panel). Equal levels of expression of FLAG-Rab8a and MYC-LRRK2 were confirmed by immunoblotting on normal gels using an anti-FLAG (second panel from the top) and anti-MYC (third panel from the top) antibodies respectively. Actin was used as a loading control (bottom panel). L represents light chain. ○ represents phosphorylated Rab8a. ● represents non-phosphorylated Rab8a. Similar results were obtained in at least two separate experiments. b The expression level of Rab8a and LRRK2 in adipocytes. c The phosphorylation of endogenous Rab8a in adipocytes. Differentiated adipocytes were transfected with LRRK2 (Y1699C)