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. 2017 Nov 15;18:33. doi: 10.1186/s12860-017-0149-5

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© The Author(s). 2017

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. 8 — PPP1R42 interacts with Nek2 and inhibits Nek2 activity in vitro. (a) PPP1R42 was overexpressed with either Nek2 or AurA in ARPE-19 cells, grown for 24 h (C, cycling) then the cells were induced to assemble cilia (SS, serum starved) followed by disassembly (+S, serum added back). Protein complexes were immunoprecipitated with anti-PPP1R42 antibody, or no antibody as negative control (−C), and the blots probed for Nek2 or AurA. Immunoprecipitates were treated with λ-phosphatase and probed with Nek2 antibody (a, right panel). (b) Protein complexes were immunoprecipitated from untransfected ARPE-19 cells with anti-AurA and anti-Nek2 antibodies and probed for PPP1R42. (c) Nek2 kinase activity was assayed in the presence of 50, 150 and 300 nM recombinant R42 protein and activity calculated as a percentage of untreated Nek2 activity