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. 2022 Jun 30;13(6):575. doi: 10.1038/s41419-022-05030-1

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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. 7 — A In vitro kinase assay for PAK4-mediated phosphorylation of NEDD4-1 with vehicle (control) or PF3758309 (10 μM). C-PAK4, C-terminal kinase domain of PAK4. B Immunoblotting for NEDD4-1 with anti-phospho-serine/threonine (α-pS/T) and anti-phospho-tyrosine (α-pY) antibodies in vector- or myc-caPAK4–transfected cells. C Immunoblotting for NEDD4-1 in vector- or myc-caPAK4–transfected cells over 24 h following treatment with cycloheximide (CHX; 20 μg/ml). D In vitro ubiquitination assay to assess the catalytic activity of NEDD4-1 with vehicle (control) or PF3758309 (10 μM). E Immunoblotting after immunoprecipitation with anti-HA (NEDD4-1) with vehicle (control) or PF3758309 (10 μM). Each blot is representative of at least two experiments.