Zhang Kun, Yuan Hui, Shi Lin
Department of Pediatric Cardiology, Shandong Provincial Hospital Affiliated to Shandong First Medical University, Jinan, China.
Front Immunol. 2025 Aug 18;16:1618424. doi: 10.3389/fimmu.2025.1618424. eCollection 2025.
Ubiquitination is a modification prevalent in eukaryotic cells. Disruptions in ubiquitination processes can have detrimental effects, potentially leading to diseases that endanger life. E3 ubiquitin ligases specifically recognize substrate proteins during ubiquitin modification, regulating intracellular protein levels and functions through the ubiquitin-proteasome pathway or TGF-β signal transduction. In recent years, substantial evidence has emerged, emphasizing the pivotal role that E3 ubiquitin ligases play in the development of pulmonary fibrosis. Advancing our understanding of how E3 ubiquitin ligases interact with pulmonary fibrosis could reveal new therapeutic targets and treatments for idiopathic pulmonary fibrosis (IPF), as well as innovative approaches in diagnosis and therapy. This review explores known regulatory mechanisms and identifies E3 ligases that have been implicated in IPF development.
泛素化是真核细胞中普遍存在的一种修饰。泛素化过程的破坏可能会产生有害影响,有可能导致危及生命的疾病。E3泛素连接酶在泛素修饰过程中特异性识别底物蛋白,通过泛素-蛋白酶体途径或转化生长因子-β信号转导调节细胞内蛋白质水平和功能。近年来,大量证据表明,E3泛素连接酶在肺纤维化的发展中起着关键作用。深入了解E3泛素连接酶如何与肺纤维化相互作用,可能会揭示特发性肺纤维化(IPF)的新治疗靶点和治疗方法,以及诊断和治疗的创新方法。本综述探讨了已知的调控机制,并确定了与IPF发展相关的E3连接酶。