Ask about this productRelated genes to: RNF128 Blocking Peptide
- Gene:
- RNF128 NIH gene
- Name:
- ring finger protein 128
- Previous symbol:
- -
- Synonyms:
- FLJ23516, GRAIL
- Chromosome:
- Xq22.3
- Locus Type:
- gene with protein product
- Date approved:
- 2003-05-21
- Date modifiied:
- 2019-02-28
Related products to: RNF128 Blocking Peptide
Related articles to: RNF128 Blocking Peptide
- - Source: PubMed
Publication date: 2026/07/24
Cao LeiYang WeiWang ChaofanLiu ChanghaoQi WenqianRen RuiqingZhang JieYu ShutingLi QianCai LiangyuZhang XinyuWang XiaohongSui WenhaiZhang MengZhang Cheng - RNF128, also known as GRAIL, is a well-studied E3 ubiquitin ligase involved in the induction and maintenance of T cell anergy. It contains PA_GRAIL_like domain, HRD1 domain and RING-H2_like domain. Recent studies have shown that RNF128 is involved in the regulation of innate immunity in mammals. It should be noted that zebrafish, possess two RNF128 paralogs, RNF128a and RNF128b. We focused on RNF128a, which shares the closest sequence homology with mammalian RNF128; however, its role in fish has not yet been elucidated. In this paper, we demonstrated that RNF128a acts as a positive regulator of innate immunity in Zebrafish. Zebrafish RNF128a responds to multiple stimuli including SVCV (Spring Viremia of Carp Virus), poly(I:C), B-DNA, LPS, and is characterized by the heightened sensitivity to SVCV. Notably, Zebrafish RNF128a up-regulates the expression of IFN1, ISG15, MX, as well as the inflammatory cytokines such as IL-6 and TNFα in response to SVCV. Mechanistically, Zebrafish RNF128a interacts with TBK1 through its protease-associated (PA) domain. However, the subcellular localization of RNF128a is associated with its HRD1 domain. In addition, Zebrafish RNF128a is localized to both early endosome RAB5 and late endosome RAB7 but rarely in Golgi apparatus and endoplasmic reticulum. Structurally, only full-length RNF128a promotes the K63-linked ubiquitination of TBK1, while none of the truncation mutants retains this activity. Our study identified Zebrafish RNF128a as an E3 ligase that catalyzes K63-linked ubiquitination and activates TBK1, and delineated its essential role in the antiviral innate immune response in zebrafish. - Source: PubMed
Publication date: 2026/07/22
Jiang ZeyinHu JihuanZhang HongyingCai FengLiu XuefengXu XiaowenHu Chengyu - Coordination between innate immune signaling and glucose metabolism is fundamental to organismal homeostasis, yet despite decades of study linking immunity and metabolism, the mechanisms by which metabolic cells restrain antiviral innate signaling while preserving glycolytic competence during overnutrition remain poorly defined. Here we identify Tetherin (BST2) as a unique cell-intrinsic immunometabolic checkpoint that couples restraint of type I interferon (IFN-I) signaling to preservation of glycolytic capacity in adipocytes. Tetherin localizes to endoplasmic reticulum and organizes an interactome enriched for antiviral sensing regulators and glycolytic control nodes in adipocytes. Mechanistically, Tetherin directly engages the ubiquitin-dependent degradation machinery NDFIP1 and RNF128 to terminate IRF3 activation, thereby limiting pro-inflammatory, anti-glycolytic signaling and protecting adipocytes from metabolic dysfunction. In parallel, multiomics integration reveals that Tetherin also acts as a scaffold that binds and spatially organizes and activates PFKFB3 to increase glycolytic capacity and restrain MAVS-IRF3 innate immune signalling. In vivo, adipocyte-specific loss of Tetherin amplifies high sucrose diet and high-fat-diet-induced glucose intolerance and liver steatosis, whereas overexpression of human Tetherin in adipocyte suppresses obesity-driven interferon signaling, restores glycolytic pathway, and improves metabolic homeostasis. Orthogonal perturbations in cancer and insulinoma cells further confirm an immunometabolic role for Tetherin. Together, these findings define Tetherin as a dual node immunometabolic checkpoint that couples restraint of antiviral innate inflammatory signaling to maintenance of glycolytic competence, thereby safeguarding adipocyte metabolic homeostasis. - Source: PubMed
Publication date: 2026/07/07
Cho Chung HwanJang YoungUkWarnock AidanYildiz RamazanJhang JingDavi KajalBrisnovali Niki FHuhn VictoriaWang PengBevaqua RominaGoedeke LeighSchotsaert Michael ABerisa MirelaPuleston DanielRajbhandari Prashant - Metabolic dysfunction-associated steatotic liver disease (MASLD) progresses from simple steatosis to metabolic dysfunction-associated steatohepatitis (MASH), yet its therapeutic development has been hampered by pathological complexity and heterogeneity. - Source: PubMed
Publication date: 2026/03/30
Cao LeiYang WeiWang ChaofanLiu ChanghaoQi WenqianRen RuiqingZhang JieYu ShutingLi QianCai LiangyuZhang XinyuWang XiaohongSui WenhaiZhang MengZhang Cheng - Bone mineral density (BMD) is a critical indicator of osteoporosis (OP). Utilizing the latest multi-omics quantitative trait loci (QTLs) data, we aim to identify novel candidates associated with heel BMD (hBMD). - Source: PubMed
Publication date: 2026/03/24
Yang XuenaLiu HuanXu KeHe DanCheng ShiqiangPan ChuyuLiu LiWei WenmingZhao BoyueHui JingniWen YanJia YumengCheng BolunXu PengZhang Feng