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. 2022 Jan 15;10:4. doi: 10.1186/s40364-021-00346-0

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© The Author(s) 2021

Open AccessThis 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/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 2 — The process of phosphatidylserine exposure on the surface of apoptotic cells. This figure schematically shows the structure of caspase-dependent scramblase Xkr8 and flippase (ATP11A /ATP11C related to CDC50A). When cell apoptosis occurs, caspase 3 or caspase 7 cleaves Xkr8 to activate its scramblase activity [20, 21]. Meanwhile, caspase 3 or caspase 7 cleaves ATP11A and ATP11C to inactivate their flippase activity, resulting in the loss of lipid asymmetry and PtdSer exposure. Then the macrophages will engulf the apoptotic cells. This form of PtdSer exposure is irreversible [22]