Front. Pharmacol.Frontiers in PharmacologyFront. Pharmacol.1663-9812Frontiers Media S.A.171028110.3389/fphar.2025.1710281PharmacologyCorrectionCorrection: Post-translational modifications in sepsis-induced acute kidney injury: mechanisms and perspectivesSong et al.10.3389/fphar.2025.1710281SongLin12†JiangWei12†LiuKe3WangJing12GongWeilei4YuJiangquan12*ZhengRuiqiang12*1Northern Jiangsu People’s Hospital Affiliated to Yangzhou University, Yangzhou, China2Intensive Care Unit, Northern Jiangsu People’s Hospital, Yangzhou, China3Yangzhou University Hospital, Yangzhou, China4School of Pharmaceutical Sciences and Institute of Materia Medica, Shandong First Medical University and Shandong Academy of Medical Sciences, Jinan, China
Edited and reviewed by:Edgar Jaimes, Memorial Sloan Kettering Cancer Center, United States
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A Correction on Post-translational modifications in sepsis-induced acute kidney injury: mechanisms and perspectives by Song L, Jiang W, Liu K, Wang J, Gong W, Yu J and Zheng R (2025). Front. Pharmacol. 16:1625139. doi: 10.3389/fphar.2025.1625139acute kidney injurysepsis, post-translational modificationssepsis-induced acutekidney injuryinflammationsection-at-acceptanceRenal Pharmacology
There was a mistake in the order of the Figures 2–5 as published. The figures and their corresponding figure captions for these results were all misaligned. The corrected figures and their captions appear below.
Pathogenesis associated with Phosphorylation and sepsis-induced acute kidney injury. A significant production of inflammatory cytokines occurs within the glomeruli and renal tubular interstitium. The interaction between TLR4 and LPS activates the phosphorylation of P38 MAPK and NF-κB, while Lyn inhibits the phosphorylation of STAT3, thereby diminishing levels of inflammatory mediators. Moreover, the suppression of calpain activation can curtail P38 phosphorylation, reduce ROS, and consequently mitigate endothelial cell apoptosis. Additionally, DNA-PKcs can induce the phosphorylation of Fis1, resulting in mitochondrial dysfunction and subsequent cell apoptosis.
Diagram illustrating the inflammatory pathway initiated by Gram-negative bacteria. LPS from bacteria activates TLR4, leading to a cascade involving p38 MAPK, STAT3, IκBα, and NF-κB P65. This triggers pathways resulting in NO, ROS production, and Fis1 activity affecting mitochondria, with calpain activation related to inflammation.
Pathogenesis associated with ubiquitination and sepsis-induced acute kidney injury. CD36 promotes ferroptosis in proximal tubular cells by regulating the ubiquitination of FSP1. The interaction between BAP1 and BRCA1 enhances the stability of BRCA1 protein through deubiquitination, thereby inhibiting NF-κB. Furthermore, FOXQ1, deubiquitinated by USP10, ameliorates cellular inflammation and apoptosis. Additionally, USP10 interacts with SIRT6 to suppress its ubiquitination, alleviating oxidative stress.
Diagram illustrating the molecular pathways involving CD36, BAP1, BRCA1, FOXQ1, USP10, SIRT6, and NRF2. CD36 interacts with Fis1 and affects mitochondria, leading to apoptosis. BAP1, BRCA1, and FOXQ1 influence NF-kB P65, causing inflammation. USP10 and SIRT6 interact, leading to NRF2 activation and affecting ROS levels. Each molecule and interaction is depicted with arrows, demonstrating the flow and impact on apoptosis, inflammation, and reactive oxygen species (ROS).
Pathogenesis associated with acetylation and sepsis-induced acute kidney injury. The sirtuin family comprises the most prevalent deacetylases, with SIRT1 mediating the acetylation of HMGB1 and SIRT3 facilitating the acetylation of TFAM. Moreover, elevated levels of acetylated P53 in RTECs hinder autophagy.
Diagram illustrating cellular processes with three main pathways. SIRT1 influences HMGB1, leading to apoptosis. SIRT3 interacts with TFAM and DNA-PKcs in a mitochondrion, affecting inflammation. P53, acetylated, is involved in autophagy.
Pathogenesis associated with lactylation and sepsis-induced acute kidney injury. In SA-AKI, elevated levels of lactate and histone lactylation, particularly the increased lactylation of H3K18, activate RhoA protein, thereby triggering inflammation and apoptosis. Additionally, lactate mediates the lactylation of Fis1, promoting mitochondrial fission and exacerbating cellular apoptosis.
Diagram illustrating lactate's effect on cellular processes. Increased lactate levels influence H3K18a, activating RhoA, and affect mitochondria via Lac and Fis1. This leads to apoptosis and inflammation.
There was a mistake in the caption of Figure 5 as published. Instead of “Pathogenesis associated with Ubiquitination and sepsis-induced acute kidney injury” it should be “Pathogenesis associated with lactylation and sepsis-induced acute kidney injury”. The corrected caption of Figure 5 appears below.
The original article has been updated.
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