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. 2020 Apr 1;52(4):594–603. doi: 10.1038/s12276-020-0410-4

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© The Author(s) 2020

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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Fig. 1 — a–c Immunoprecipitation of PLCE1 with Rho GTPase, Rac1 (a), RhoA (b), and Cdc42 (c) in cultured podocytes. Immunoblotting showed that PLCE1 interacts with Rac1 and RhoA but not with Cdc42. d–e FLAG-PLCE1 expressed in HEK293 cells was precipitated by GST- Rac1 (d) and GST-RhoA (e). Ponceau red staining at the top shows the GST proteins used. f–i Costaining of PLCE1 with WT1 (f), SYNAPTOPODIN (g), Rac1 (h) and RhoA (i) using immunofluorescence in adult rat glomeruli. PLCE1 colocalized with Rac1 and RhoA in podocyte cell bodies. Immunoprecipitation (IP) and pulldown (PD) experiments are representative of more than three experiments.