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. 2022 Aug 15;13:4788. doi: 10.1038/s41467-022-32541-4

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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 Surface representation of DLC1 illustrating the differences in the footprint of binding by p120RasGAP SH3 domain (purple) and RhoA (yellow, predicted), with residues that bind p120RasGAP colored teal. DLC1 residues mutated in this study are labeled. b RhoGAP activity of structurally-defined DLC1 mutants T1223D and L1267D are not inhibited by p120RasGAP SH3 domain. RhoA alone (teal) or RhoA plus the arginine finger mutant DLC1 R1114A (green) are included. Signal is plotted as % phosphate generated, normalized to activity of RhoA plus wild-type DLC1 (blue, 0 μM SH3). Data are presented as mean values (bars) +/− SD (error bars), and individual measurements are plotted (dots, n = 8). P values: WT 0 μM versus 10 μM SH3, P < 0.0001; T1223D 0 μM versus 10 μM SH3, P = 0.7747; L1267D 0 μM versus 10 μM SH3, P = 0.5663. c GTP hydrolysis by Ras (blue) is stimulated by p120RasRasGAP RasGAP domain (red) but is not inhibited by 1 μM (green) or 10 μM (purple) p120RasGAP SH3 domain. Data are presented as mean values (bars) +/− SD (error bars), and individual measurements are plotted (dots, n = 4). P values are: 0 μM versus 1 μM SH3: 0.3148; 0 μM versus 10 μM SH3: 0.9944; 1 μM versus 10 μM SH3: 0.4329. In b, c P values were calculated by ordinary one-way ANOVA analysis with Tukey’s multiple comparison test in GraphPad Prism. Significant differences are based on P values as indicated: ns: P ≥ 0.05; **** P < 0.0001. Source data are available as a Source Data file.