{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPellino‐1 is a signal‐responsive E3 ubiquitin ligase that plays a central role in innate immune receptor signaling. It was first shown to mediate IL‑1 receptor/Toll‑like receptor signaling by interacting with IRAK family kinases and TRAF6 to activate NF‑κB and induce proinflammatory gene expression, while its engagement with regulatory proteins such as Smad6 and DEAF1 helps mediate anti‐inflammatory effects and interferon‐β production. Moreover, Pellino‑1 exhibits highly specific phosphothreonine–peptide binding preferences that underpin its substrate selectivity in these pathways, and genetic variants of the gene have been associated with altered risks for inflammatory conditions including Kawasaki disease and systemic lupus erythematosus (SLE), with additional regulation conferred by microRNAs that target its transcript."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "11"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its immunomodulatory functions, Pellino‑1 governs cell death and oncogenic processes by directing distinct ubiquitination events. It mediates lysine‑63–linked ubiquitination of RIPK1 to promote necroptosome formation and, in a kinase‑dependent manner, safeguards against RIPK3 hyperactivation by targeting active RIPK3 for proteasome‑dependent degradation. Furthermore, Pellino‑1 modulates tumor cell survival and responsiveness through its ability to stabilize key oncoproteins – for instance, by ubiquitinating factors that enhance epithelial–mesenchymal transition (via Snail/Slug in lung adenocarcinoma), promoting chemoresistance through cIAP2 stabilization, and by affecting the subcellular localization of Mdmx to activate p53. Additional reports have implicated Pellino‑1 in lymphomagenesis via modification of BCL6, as well as in maintaining genomic integrity by perturbing mitotic checkpoint components such as BubR1 and by participating in the DNA damage response through ATM‐dependent recruitment and NBS1 ubiquitination."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "12", "end_ref": "23"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nPellino‑1 functions extend into the regulation of tissue injury responses and the development of diverse human diseases. In models of septic acute kidney injury, Pellino‑1 is implicated in tubular cell death via DAPK1‐dependent phosphorylation events, while in cardiomyocytes it influences fibrotic remodeling by modulating exosomal microRNA content. Altered Pellino‑1 expression – whether through genetic polymorphisms or regulation by microRNAs such as miR‑590‑5p, miR‑301a‑3p, and others – has been linked to autoimmune disorders (including SLE and premature ovarian insufficiency), neurodegenerative diseases such as Alzheimer’s and Parkinson’s, as well as in malignancies of the colorectum and pancreas. These diverse roles clearly underscore Pellino‑1 as a nexus bridging immune receptor signaling, cell death, genomic stability and tissue homeostasis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "24", "end_ref": "36"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Zhengfan Jiang, H Jan Johnson, Huiqing Nie, et al. 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