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. 2022 Jul 8;13:3955. doi: 10.1038/s41467-022-31645-1

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© The Author(s) 2022

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. 5 — a Western blotting analysis of the distribution of activated AKT1 in cytosolic or membrane fractions from DMSO or GSK591-treated CHLA20 cells in the absence or presence of EGF. b The presence of activated AKT1 in cytosolic and membrane fractions from scramble or PRMT5 knockdown cells with or without EGF stimulation. c Colocalization of AKT1 wild type or R15K mutant with plasma membrane by immunofluorescence visualized under confocal microscopy in CHLA 20 cells in the absence or presence of EGF. Scale bars, 100 μm. d The binding to phosphatidylserine (PS) of AKT1 wild type or R15K mutant was examined by the presence of HA-tagged protein in the eluate or flowthrough fraction after incubation with phosphatidylserine coated agarose beads by Western blotting. Top, elution from PS beads; middle, flowthrough after incubation; bottom, HA-tagged protein eluted from anti-HA beads. e The association of AKT1 wild type or R15K mutant with PDK1 or mTORC2 was analyzed by Western blotting in CHLA20 with or without EGF stimulation. Exogenous AKT1 wild type or R15K mutant was pulldown by HA beads, and the precipitants were analyzed by Western blotting for PDK1 and SIN1. f The interaction of AKT1 with PDK1 and mTORC2 was measured by immunoprecipitation of endogenous AKT1 followed by Western blotting against PDK1 and SIN1 in SK-N-BE(2) and NGP cells with or without PRMT5 knockdown. g The recruitment of PDK1 and mTORC2 was examined in DMSO or GSK591-treated CHLA20 and NGP cells. a–g Representative results from three independent experiments. Uncropped immunoblots are provided in the Source Data file.