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. 2021 Nov 25;12:6869. doi: 10.1038/s41467-021-27244-1

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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 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. 6 — a The molecular model of LPCAT3/araCoA viewed from the lumen side of the ER membrane. The residues and DOPC molecules at the non-contact dimeric interface, as well as the araCoA molecules, were shown as stick model. b, c A close view of the dimeric interface at two angles. d The crosslinking assay on membrane-bound cLPCAT3. The wild type cLPCAT3 and the double mutants of the dimeric interface, T126K/L372K and Y144K and H391K, were treated with the crosslinking reagents DSS at the concentrations as indicated before solubilized from the membranes of the Expi293 cells overexpressing the corresponding proteins. Shown were the representative results from three independent experiments.