Front. Physiol. Frontiers in Physiology Front. Physiol. 1664-042X Frontiers Media S.A. 1641354 10.3389/fphys.2025.1641354 Physiology Correction Correction: Endothelial AIP1 regulates vascular remodeling by suppressing NADPH Oxidase-2 Zhang et al. 10.3389/fphys.2025.1641354 Zhang Jiqin 1 2 † Chen Chaofei 1 2 † Li Li 1 Zhou Huanjiao J. 2 Li Fenghe 2 Zhang Haifeng 2 Yu Luyang 3 Chen Yuxin 4 * Min Wang 1 2 * 1 Center for Translational Medicine, The First Affiliated Hospital, Sun Yat-sen University, Guangzhou, China 2 Department of Pathology and The Vascular Biology and Therapeutics Program, Yale University School of Medicine, New Haven, CT, United States 3 Institute of Genetics, Institute of Genetics and Regenerative Biology, College of Life Sciences, Zhejiang University, Hangzhou, China 4 Department of Laboratory Medicine, Nanjing Drum Tower Hospital, Nanjing University Medical School, Nanjing, China

Edited and reviewed by: Geoffrey A. Head, Baker Heart and Diabetes Institute, Australia

 *Correspondence: Yuxin Chen, yuxin_chen2015@163.com; Wang Min, wang.min@yale.edu

These authors have contributed equally to this work

 04 08 2025 2025 16 1641354 04 06 2025 22 07 2025 Copyright © 2025 Zhang, Chen, Li, Zhou, Li, Zhang, Yu, Chen and Min. 2025 Zhang, Chen, Li, Zhou, Li, Zhang, Yu, Chen and Min

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 A Correction on Endothelial AIP1 regulates vascular remodeling by suppressing NADPH Oxidase-2 by Zhang J, Chen C, Li L, Zhou HJ, Li F, Zhang H, Yu L, Chen Y and Min W (2018). Front. Physiol. 9:396. doi: 10.3389/fphys.2018.00396 AIP1 NOX2 reactive oxygen species vascular remodeling neointimal hyperplasia section-at-acceptance Redox Physiology

There was a mistake in Figure 5H as published. The NOX2 blot in the IP:p47 bracket was misplaced. A revised Figure 5 with the corrected Figure 5H appears below.

AIP1 blocks NOX2 activity in EC by disrupting the formation of an active NOX2 complex. (A) Association of AIP1 with p47phox. HAEC were transfected with control siRNA or AIP1 siRNA. Twenty four hour post-transfection, cells were either left untreated or treated with TNFα (10 ng/ml) for 15 min. AIP1-p47phox and NOX2-p47phox complexes were determined by a co-immunoprecipitation assay followed by Western blot as indicated. (B) Schematic diagram for AIP1 structural domains and expression constructs. PH, PH domain; C2, PKC conserved domain; GAP, GTPase-activating protein domain; PER, period-like domain; PRR, proline-rich region; CC/LZ, coiled coil/leucine-zipper domain. Various AIP1 N-terminal truncates (F1PH and AIP1-N) and C-terminal truncates (AIP1-C; C-PR, C-1PR) constructed with a Flag-tagged at the N-terminus are shown. (C,D) AIP1 via its PRR binds to p47phox. Various AIP1 truncates were co-transfected with HA-tagged p47phox into HAEC cells as indicated. Associations of AIP1 truncates with p47phox were determined by co-immunoprecipitation with anti-HA (for p47phox) followed by Western blot with anti-Flag (for AIP1 truncates). Immunoprecipitated AIP1 truncates are indicated. (E) Schematic diagram for the p47phox structural domains and expression constructs. PX, phosphoinositide-binding structural domain; SH3, Src homology 3 domain that binding to proline-rich region (PRR); AIR, autoinhibitory region; PPR, proline-rich region (PRR). 1phoxC: a mutant with the deletion of both AIR and PPR; 1SH3: a mutant with the deletion of the two SH3 domains. (F) p47phox via the SH domains bind to AIP1. HA-tagged p47phox truncates were co-transfected with FLAG-tagged AIP1-C into HAEC as indicated. Associations of p47phox truncates with AIP1-C were determined by co-immunoprecipitation with anti-HA (p47phox) followed by Western blot with anti-Flag (AIP1-C). AIP1-C and IgG in the immunoprecipitation are indicated. (G,H) AIP1 prevents/disrupts NOX2-p47phox complex formation. HAEC were infected with lentivirus with empty vector (EV), AIP1-F (E) and with a truncate (F), and cells were left untreated or treated with TNFα (10 ng/ml for 15 min). Cell lysates were subjected to co-immunoprecipitation assays with anti-p47phox followed by Western blot with anti-NOX2. All experiments were repeated three times.

A multi-panel figure shows various biochemical analyses involving proteins AIP1, NOX2, and p47. Panel A displays Western blots after siRNA treatment, indicating the presence of these proteins under TNF stimulation. Panel B consists of diagrams depicting domain structures of AIP1 and its variants. Panel C through D show immunoprecipitation and Western blot results, highlighting interactions and molecular weights of truncated AIP1 proteins with p47. Panel E presents domain diagrams of p47 and its variants. Panel F shows Western blots of truncated proteins. Panels G and H depict additional interaction analyses under TNF stimulation using Western blotting.

The original article has been updated.

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