Ask about this productRelated genes to: USP18 antibody
- Gene:
- USP18 NIH gene
- Name:
- ubiquitin specific peptidase 18
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 22q11.2
- Locus Type:
- gene with protein product
- Date approved:
- 1999-11-16
- Date modifiied:
- 2018-02-28
Related products to: USP18 antibody
Related articles to: USP18 antibody
- Diabetic cardiomyopathy (DCM) is a multidimensional myocardial remodeling disorder driven by interconnected metabolic, inflammatory, ferroptotic, autophagic and fibrotic programs, yet the post-translational mechanisms that convert diabetic stress into persistent injury remain incompletely integrated. Ubiquitin-specific proteases (USPs) regulate substrate stability, ubiquitin-chain architecture and signaling-complex dynamics and therefore represent an important proteostatic layer in DCM. Rather than assigning fixed protective or maladaptive identities to individual enzymes, this review organizes current evidence according to specific USP-substrate axes and their cellular and disease contexts. Predominantly protective axes include USP28-PPARα/Mfn2, USP8-Parkin, USP13-NLRP3, USP20-p62/STING, USP18-dependent stabilization of Notch1 or FOXC2, and the endothelial USP33-ATG7/FIS1 pathway. Predominantly injurious axes include USP38-ACAD11, USP14-VDAC1 and USP24-associated ferroptotic and autophagy-disruptive signaling. USP7 exemplifies substrate-dependent bidirectionality: USP7-PGC1β promotes metabolic dysfunction, whereas USP7-NRF2 supports GPX4-dependent ferroptosis resistance during empagliflozin treatment. By integrating these axes across pathological modules and cardiac cell types, this review reframes DCM as a disorder of context-dependent proteostatic maladaptation and highlights substrate-resolved USP regulation as a priority for future mechanistic and translational investigation. - Source: PubMed
Publication date: 2026/09/18
Meng XiangyunGuo ShumingLin HuiLi RuchaoPeng WeiSun LingangShi XiaoweiYang Lixia - ISG15 is a type I interferon (IFN-I)-inducible ubiquitin-like protein that restrains IFN-I signaling. Classical ISG15 deficiency is thought to cause disease mainly by disrupting USP18 stabilization, which leads to sustained IFN-I signaling and interferon-driven autoinflammation. Whether patient-derived C-terminal ISG15 variants can impair IFN-I negative feedback through altered C-terminal functional presentation has remained unclear. - Source: PubMed
Publication date: 2026/09/17
Zhang WanyuChen XiongbinLi YuluYao XingfengHuang JinyanGao YijiuXing WenluLu DanDeng MengyueShu ZhouMao Huawei - Traumatic brain injury (TBI) is a leading cause of mortality and morbidity and a major contributor to loss of working capacity in young adults. Current therapeutic options for TBI remain limited. This study aimed to assess the potential role and therapeutic value of ubiquitin-specific protease 18 (USP18) in TBI. - Source: PubMed
Publication date: 2026/09/29
Zhao YangyangLei PanLi YulongLiu ChengxiZhang YichenZeng ChuanSun YangyangChen XinhuiYuan RaoraoFan HengyiCheng ShiqiZhang Yan - Sequential exposure to heterologous noxious stimuli such as histological chorioamnionitis (HCA) and hyperoxia may elicit variable immune responses, resulting in distinct disease manifestations in the neonate. However, the molecular mechanisms underlying innate immune dysregulation in these contexts remain poorly characterized. - Source: PubMed
Publication date: 2026/09/15
Sequeira Gomes RochelleGayen Nee' Betal SuhitaAddya SankarGayen SaurabhZubair NidaChan Joanna S YAghai Zubair H - Osteoporosis (OP) is a systemic metabolic disease associated with inflammation and apoptosis of osteoblasts. Ubiquitin-specific protease 18 (USP18) has been shown to participate in the progression of bone metabolic disorders; however, its role in osteoblast injury remains unclear. A rat OP model was established via bilateral ovariectomy (OVX). Pathological changes were observed using H&E and Masson staining, and Western blotting was used to detect the expression of related proteins. In vitro, an inflammatory injury model was constructed by inducing MC3T3-E1 mouse osteoblasts with 1 µg/mL LPS. CCK-8, EdU, flow cytometry, and Co-IP were utilized to validate the role of USP18 in osteoblast injury. OVX-treated rat femoral tissue samples exhibited severe inflammatory cell infiltration and bone damage. USP18 expression was significantly downregulated in OP rats and in LPS-stimulated osteoblasts. Overexpression of USP18 significantly increased cell viability and proliferation; upregulated the expression of osteogenesis-related protein markers (Runx2, ALP, and OCN); and reduced the levels of inflammatory factors (TNF-α and IL-6) and apoptotic proteins (Bax and cleaved caspase-3), thereby ameliorating LPS-induced osteoblast injury. Mechanistic studies revealed that USP18 binds to TAK1, removes K63-linked ubiquitination modifications on TAK1, and inhibits the activation of the p38/JNK-MAPK pathway. Notably, the MAPK activator anisomycin or TAK1 overexpression weakened the protective effects of USP18 on osteoblasts. USP18 inhibits MAPK pathway activation by deubiquitinating TAK1 and alleviates LPS-induced inflammation and apoptosis in osteoblasts. Furthermore, USP18 overexpression mitigates OP progression. - Source: PubMed
Publication date: 2026/09/25
Chen GuopingLiang JinlongCui YiWei JiahengXu Yongqing