Correction: Post-translational modifications in sepsis-induced acute kidney injury: mechanisms and perspectives

Lin Song^1,2Wei Jiang^1,2Ke Liu³训费 Wang^1,2Lei wei Gong⁴Jiangquan Yu^1,2*Ruiqiang Zheng^1,2*

• ¹Northern Jiangsu People’s Hospital Affiliated to Yangzhou University, Yangzhou, China
• ²Intensive Care Unit, Northern Jiangsu People’s Hospital, Yangzhou, China
• ³Yangzhou University Hospital, Yangzhou, China
• ⁴School of Pharmaceutical Sciences & Institute of Materia Medica, Shandong First Medical University & Shandong Academy of Medical Sciences, Jinan, China

Correction: Post-translational modifications in sepsis-induced acute kidney injury: mechanisms and perspectives Error in figure/table Wrong content There was a mistake in figure2,3,4,5 as published. The figures and their corresponding figure captions for these results are all misaligned. The corrected figures appears below. [insert correct figure/table] The original version of this article has been updated. Figure2 Figure3 Figure 4 Figure5 Figure/table caption There was a mistake in the caption of figure/table [insert figure/table number] as published. The figures and their corresponding figure captions for these results are all misaligned. The corrected caption of figure/table [insert figure/table number] appears below. "[insert correct caption]" Figure 2 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. Figure 3 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, Figure 4 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. Figure5 Pathogenesis associated with Ubiquitination 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. Figure 2 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. Figure 3 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. Figure 4 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. Figure5 Pathogenesis associated with Ubiquitination 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.