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. 2019 Oct 10;9:14527. doi: 10.1038/s41598-019-50742-8

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© The Author(s) 2019

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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Characterisation of anionic lipids binding to PDK1 PH domain in vitro (A). Lipid protein-overlay assays showing the binding of WT-PH^PDK1 and mutants to a selection of lipids spotted on nitrocellulose. (B) PH^PDK1 wild type and mutants’ affinity for PtdSer. (C) Confocal images of WT-PH^PDK1 association to GUVs of different compositions. (D) WT-PH^PDK1 and mutant T513E-PH^PDK1 diffusion on GUVs of different composition. (E) Representative autocorrelation curves from sFCS experiments, each corresponds to one GUV. N > 8. Box: 2xSEM (Standard Error of the Mean); Whiskers: 80% population. Mann-Whitney test *p < 0.05.