Front. Cell Dev. Biol. Frontiers in Cell and Developmental Biology Front. Cell Dev. Biol. 2296-634X Frontiers Media S.A. 1605628 10.3389/fcell.2025.1605628 Cell and Developmental Biology Correction Correction: Loss of CDYL results in suppression of CTNNB1 and decreased endometrial receptivity Zhou et al. 10.3389/fcell.2025.1605628 Zhou Xiaowei 1 † Xu Bufang 1 † Zhang Dan 1 Jiang Xiaoping 2 Chang Hsun-Ming 3 Leung Peter C. K. 3 Xia Xiaoyu 4 5 * Zhang Aijun 1 5 * 1 Department of Reproductive Medical Center, Ruijin Hospital, School of Medicine, Shanghai Jiao Tong University, Shanghai, China 2 Department of Obstetrics and Gynecology, Chinese People’s Armed Police Force Shanghai Corps Hospital, Shanghai, China 3 Department of Obstetrics and Gynaecology, BC Children’s Hospital Research Institute, The University of British Columbia, Vancouver, BC, Canada 4 Department of Histoembryology, Genetics and Developmental Biology, School of Medicine, Shanghai Jiao Tong University, Shanghai, China 5 Shanghai Key Laboratory of Reproductive Medicine, Shanghai Jiao Tong University, Shanghai, China

Edited and reviewed by: Claudia Tanja Mierke, Leipzig University, Germany

 *Correspondence: Xiaoyu Xia, zpxiaxy@shsmu.edu.cn; Aijun Zhang, zhaj1268@163.com

These authors have contributed equally to this work

 25 06 2025 2025 13 1605628 03 04 2025 16 06 2025 Copyright © 2025 Zhou, Xu, Zhang, Jiang, Chang, Leung, Xia and Zhang. 2025 Zhou, Xu, Zhang, Jiang, Chang, Leung, Xia and Zhang

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 A Correction on Loss of CDYL results in suppression of CTNNB1 and decreased endometrial receptivity by Zhou X, Xu B, Zhang D, Jiang X, Chang H-M, Leung PCK, Xia X and Zhang A (2020). Front. Cell Dev. Biol. 8:105. doi: 10.3389/fcell.2020.00105 recurrent implantation failure chromodomain Y like catenin beta 1 migration endometrial receptivity section-at-acceptance Cell Adhesion and Migration

In the published article, there was an error in Figure 3C. The authors have identified that the image for the CDYL-sh1 48h treatment was inadvertently duplicated from the CDYL-sh3 24h treatment due to an error during figure preparation. The corrected Figure 3C and its caption appear below.

CDYL knockdown suppressed the cell migration capability in Ishikawa cells. The CDYL-knockdown efficiency was shown by Western blot analysis (A) and densitometric quantification (B). (C) Wound healing assay was used to examine the effect of CDYL silencing on cell migration. (D) The histograms show the quantitated percentage of wound closure. Bar = 100 µm. N = 3. All data are presented as mean ± SD. *P < 0.05; **P < 0.01; ***P < 0.001.

Western blot analysis and graphs illustrate the effect of CDYL knockdown. Panel A shows protein bands for CDYL and GAPDH across different samples (NC, CDYL-sh1, CDYL-sh2, CDYL-sh3). Panel B is a bar graph representing relative CDYL protein amounts. Panel C displays cell migration in wound healing assays at 0, 24, and 48 hours for NC, CDYL-sh1, and CDYL-sh3. Panel D is a bar graph showing wound closure percentages at 24 and 48 hours, highlighting statistical significance with asterisks.

In the published article, there was an error in Figure 5F. Although the Western blot for CDYL in Figure 5F was performed on the same experimental day, it was not run on the same membrane as CTNNB1 and GAPDH, due to an error during figure preparation. The corrected Figure 5F and its caption appear below.

The decreased expression of CTNNB1 after CDYL knockdown in Ishikawa cells, EECs, and ESCs. (A) DEGs involved in the endometrial receptivity and implantation were validated by RT-qPCR. Protein expression levels of CDYL and CTNNB1 were decreased after CDYL silencing in Ishikawa cells (B,C), EECs (D,E), and ESCs (F,G) shown by Western blot and densitometric quantification. N ≥ 3. All data are presented as mean ± SD. *P < 0.05; **P < 0.01; ***P < 0.001.

Panel of graphs and Western blots analyzing mRNA and protein expression in Ishikawa, EEC, and ESC cells. Graph A shows relative mRNA expression of genes such as CTNNB1 and EPHA2. Panels B, D, and F present Western blot results for proteins CDYL and CTNNB1 against GAPDH. Graphs C, E, and G display relative protein amounts for CDYL and CTNNB1 under NC, CDYL-sh1, and CDYL-sh3 conditions. Error indicators and significance are marked, with variations in expression levels across different cell treatments.

The authors apologize for these errors and state that this does not change the scientific conclusions of the article in any way. The original article has been updated.

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