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
- 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 - Mitochondrial dysfunction is closely related to the pathogenesis of Parkinson’s disease (PD). Studies have shown that ubiquitination plays a crucial role in regulating mitochondrial dysfunction. As a ubiquitin ligase, RNF128 may influence mitochondrial function by modulating its ubiquitination activity. This study aimed to investigate the specific effect and mechanism of RNF128 on PD-induced mitochondrial dysfunction in neurons. Animal and cellular models of PD were established for experimental investigation by intraperitoneal injection of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) in mice and treatment of SH-SY5Y cells with 1-methyl-4-phenylpyridinium (MPP+). Motor function was evaluated via the rotarod test and pole climbing test; pathological brain tissue damage was detected via H&E staining; mitochondrial function was detected via MitoSOX Red staining, JC-1 staining, and ATP content determination. The binding of RNF128 and SIRT1 was detected via coimmunoprecipitation, and the expression levels of related proteins were detected via Western blotting and immunofluorescence. The result shows that RNF128 is highly expressed in PD. Knocking down RNF128 improves MPTP-induced motor dysfunction, increases the number of TH-positive neurons, and attenuates brain tissue damage in PD mice. At the cellular level, knocking down RNF128 led to reduced mitochondrial ROS levels and increased mitochondrial membrane potential and ATP levels, thereby ameliorating MPP+-induced mitochondrial dysfunction in neuronal cells. In terms of molecular mechanisms, the expression of SIRT1 is downregulated in PD, and RNF128 interacts with SIRT1 to increase the ubiquitination and degradation of SIRT1. Knocking down SIRT1 partially reverses the improvement in mitochondrial function achieved by knocking down RNF128. Overall, knocking down RNF128 improves mitochondrial dysfunction by increasing SIRT1 expression, thereby alleviating neuronal injury in PD. - Source: PubMed
Publication date: 2026/03/22
Dong JianengZhang LifenGao YanqinChen YutingTian ChunhuaWang ChunxiangHuang HuaiXu Zhenghu - Regulatory T cells (Tregs) play a central role in immune homeostasis and the preservation of immunological self-tolerance. Treg activity depends on prolonged IL-2 receptor (IL-2R) signaling, and impairment or loss of this function has been linked to the development of autoimmune diseases. This review evaluates the hypothesis that disrupted IL-2R signaling, due to enhanced desensitization, impairs Treg suppressive function and contributes to autoimmunity. In mice and humans, desensitization of IL-2R signaling by the cullin-RING ligase 5 (CRL5) complex leads to reduced persistence of phosphorylated JAK1 (pJAK1) and its downstream effector pSTAT5, a transcription factor critical for Treg function. Activation of CRL5 requires neddylation-a post-translational modification in which the ubiquitin-like NEDD8 is conjugated to lysine 724 on cullin-5 (CUL5), the scaffold protein of CRL5. Neddylation permits untethering of the RING-box protein RBX, enabling E2 enzyme-mediated ubiquitination and proteasomal degradation of pJAK1 via recruitment by suppressor of cytokine signaling 3 (SOCS3). This process, known as IL-2R signal desensitization, is antagonized in Tregs by the E3 ligase GRAIL (Gene Related to Anergy in Lymphocytes, RNF128), which mono-ubiquitinates Lys724 to block neddylation, preventing CRL5 activation and pJAK1 degradation. An imbalance between neddylation and mono-ubiquitination at Lys724 compromises IL-2R signaling and promotes autoimmune pathology, and studies show GRAIL expression is diminished in Tregs from autoimmune patients and mouse models, leading to reduced pSTAT5 activity and impaired suppressive capacity. Pharmacologic inhibition of neddylation with pathway inhibitors (NAEi) restores IL-2R signaling and Treg function, highlighting the therapeutic potential of targeting this regulatory axis to preserve immune tolerance. - Source: PubMed
Publication date: 2025/10/15
Marty Saci-ElodieYip LindaWang FangyuanKumar ManojFathman C Garrison - - Source: PubMed
Publication date: 2025/10/18
He Tian ShengCai KuntaiLai WeilingYu JinggeQing FurongShen AoSui LinaHe WenjiWang WeihuaXiao QiuxiangLei XiongGuo TianfuLiu Zhiping