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. 2024 Aug 22;15:7239. doi: 10.1038/s41467-024-51310-z

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© The Author(s) 2024

Open Access This article is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License, which permits any non-commercial use, sharing, 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 licence, and indicate if you modified the licensed material. You do not have permission under this licence to share adapted material derived from this article or parts of it. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by-nc-nd/4.0/.

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Fig. 4 — a A recombinant GST-tagged peptide containing amino acids 700-720 of human DENND5A sequence was generated for use in pulldown experiments. The bolded residue corresponds to Arg710 that is affected in the cohort (R710H). b Table indicating the number of peptides corresponding to MUPP1 and PALS1 found bound to each GST fusion peptide used in the pulldown/mass spectrometry experiment. c Overexpressed human MUPP1- and PALS1-FLAG bind to GST-tagged DENND5A peptides. Results were reproduced in 3 independent experiments. d Residues 700–720 are shown in red in a space-fill model (left) and magnified view (right) of the predicted DENND5A protein structure from AlphaFold. Dotted lines indicate hydrogen bonds. e The interface between the DENN and RUN1 domains of DENND5A comprises many charged residues. f GST pulldown experiments show that FLAG-DENN and GST-RUN1/PLAT physically interact. g Co-immunoprecipitations between GFP-DENND5A and MUPP1- and PALS1-FLAG show that DENND5A only binds the polarity proteins when the intramolecular DENN-RUN1 interaction is disrupted. Source data for (b, c) and (f, g) are provided as a Source Data file.