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. 2021 Sep 2;11:17546. doi: 10.1038/s41598-021-97006-y

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© The Author(s) 2021

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 licence, and indicate if changes were made. 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/4.0/.

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Phosphorylation of paxillin Y31 and Y118 is required for paxillin interactions with Erk1/2 and DRP1. (A–D) HLMVECs were transfected with wild type paxillin or paxillinY31F mutant plasmids, interactions of paxillin with DRP1 and Erk1/2 was assessed by IP experiment. Data were presented as means ± SD, **p < 0.01, LPS wild type paxillin versus LPS paxillinY31F mutant; ***p < 0.005, LPS wild type paxillin versus LPS paxillinY31F mutant, n = 3. E–H, HLMVECs were transfected with wild type paxillin or paxillinY118F mutant plasmids, interactions of paxillin with DRP1 and Erk1/2 was assessed by IP experiment. Data were presented as means ± SD, **p < 0.01, LPS wild type paxillin versus LPS paxillinY118F mutant; ***p < 0.005, LPS wild type paxillin versus LPS paxillinY181F mutant, n = 3.