Ask about this productRelated genes to: NUDT16L1 Blocking Peptide
- Gene:
- NUDT16L1 NIH gene
- Name:
- nudix hydrolase 16 like 1
- Previous symbol:
- -
- Synonyms:
- SDOS
- Chromosome:
- 16p13.3
- Locus Type:
- gene with protein product
- Date approved:
- 2005-01-25
- Date modifiied:
- 2015-11-13
Related products to: NUDT16L1 Blocking Peptide
Related articles to: NUDT16L1 Blocking Peptide
- Spermatogonial stem cells (SSCs) are essential for maintaining sperm production but are highly susceptible to damage from testicular ischemia-reperfusion (IR) injury, a common consequence of conditions like testicular torsion. This injury leads to oxidative stress, disruption of the blood-testis barrier (BTB), and germ cell death. While the transcription factor EGR1 is known to promote SSC survival in laboratory settings, its protective mechanisms within a living organism remained unclear. This study aimed to identify the downstream targets through which EGR1 confers protection against IR injury. Through bioinformatic analysis, a potential binding site for EGR1 was discovered in the promoter of the Nudt16L1 gene. A series of experiments, including chromatin immunoprecipitation and luciferase reporter assays, confirmed that EGR1 directly binds to this site and activates Nudt16L1 expression. In a mouse model of testicular IR injury, overexpression of EGR1 was found to alleviate tissue damage, improve sperm motility, and preserve the integrity of the BTB. Crucially, when Nudt16L1 was experimentally silenced, the protective benefits of EGR1 were lost. Conversely, overexpressing Nudt16L1 alone was sufficient to mimic EGR1's protective effects, reducing reactive oxygen species and preventing cell death in SSCs subjected to oxygen-glucose deprivation/reperfusion, an in vitro model of IR. In conclusion, this research identifies Nudt16L1 as a critical downstream effector of EGR1. The EGR1-Nudt16L1 signaling axis protects SSCs from IR injury by mitigating oxidative stress, maintaining BTB integrity, and inhibiting apoptosis. These findings highlight this pathway as a promising therapeutic target for preventing infertility resulting from testicular torsion and similar ischemic events. - Source: PubMed
Weng YimingWang YanqiuXiang JunWu DenglongLe Wei - The N7-methylguanosine (m7G) modification is known as a common post-transcriptional modification of RNA that has been found to be involved in the pathogenesis of various diseases. However, its role in osteoarthritis (OA) remains largely unknown. This study aimed to identify the genes associated with m7G modification in OA and further investigate their diagnostic value and immune infiltrates. - Source: PubMed
Publication date: 2025/10/07
Sun HongChen KunhaoXiong ZhilinZhuang YongLiu MiaoNing XuYang Hua - The ubiquitin chains perform diverse biological functions through different linkages. However, the understanding of non-canonical K29-linked ubiquitin chains is relatively limited. Exploring the physiological functions of K29-linked ubiquitin chains beyond degradation is crucial for deciphering the ubiquitin chain code, which is essential for understanding cellular physiology. The unfolded protein response (UPR) serves as a crucial mechanism for cells to cope with endoplasmic reticulum stress and involves comprehensive and precise regulation. Ubiquitin, as a regulator of protein function, has potential regulatory functions other than guiding protein degradation in the UPR. Here, a close association is revealed between K29-linked ubiquitin chains and transcriptional regulation during the UPR. After UPR induction, the K29-linked ubiquitination of the SMC1A and SMC3 proteins in the cohesin complex increases. The transcription of cell proliferation-related genes, such as SERTAD1 and NUDT16L1, is regulated by the K29-linked ubiquitination of cohesin. Overall, the upregulation of K29-linked ubiquitination of cohesin during the UPR disrupts the formation of the transcription initiation complex, resulting in the transcriptional downregulation of cell proliferation-related genes. - Source: PubMed
Publication date: 2025/08/30
Zhang QiushuangTeng XucongDai YicongWu YuncongHou HongweiLi Jinghong - Fibro-adipogenic progenitor cells (FAPs) support muscle tissue homeostasis, regulate muscle growth, injury repair, and fibrosis, and activate muscle progenitor cell differentiation to promote regeneration. We aimed to investigate the effects of co-culturing FAPs with muscle satellite cells (MuSCs) on myogenic differentiation. Proteomic profiling of co-culture supernatants identified significant DCX, IMP2A, NUDT16L1, SLC38A2, and IL-6 upregulation. Comparative transcriptomics of mono-cultured versus co-cultured MuSCs revealed differential expression of oxidative stress-related genes (, , , , , and ). Pathway enrichment analyses highlighted cell cycle regulation, TNF signaling, and ferroptosis. Gene ontology analysis of MuSCs indicated significant gene enrichment in myosin-related components. Combined transcriptomic and proteomic analyses demonstrated HO-1 downregulation at the transcriptional and translational levels, with altered pathways being predominantly related to myosin filament, muscle system process, and muscle contraction cellular components. HO-1 knockdown reduced intracellular iron accumulation in MuSCs, suppressing iron-dependent autophagy. This alleviated oxidative stress and promoted myogenic differentiation. Exogenous IL-6 (0.1 ng/mL) downregulated HO-1 expression, initiating an identical regulatory cascade, while HO-1 overexpression reversed the IL-6-mediated reduction in the expression of the autophagy markers LC3 and ATG5, suppressing myogenic enhancement. This establishes the co-culture-induced IL-6/HO-1 axis as a core regulator of iron-dependent oxidative stress and autophagy during myogenic differentiation. - Source: PubMed
Publication date: 2025/08/10
Zhang MengyuanLiu SiyuWang YonghengShan ShanCang Ming - Tudor Interacting Repair Regulator (TIRR) is an RNA-binding protein (RBP) that interacts directly with 53BP1, restricting its access to DNA double-strand breaks (DSBs) and its association with p53. We utilized iCLIP to identify RNAs that directly bind to TIRR within cells, identifying the long non-coding RNA NEAT1 as the primary RNA partner. The high affinity of TIRR for NEAT1 is due to prevalent G-rich motifs in the short isoform (NEAT1_1) region of NEAT1. This interaction destabilizes the TIRR/53BP1 complex, promoting 53BP1's function. NEAT1_1 is enriched during the G1 phase of the cell cycle, thereby ensuring that TIRR-dependent inhibition of 53BP1's function is cell cycle-dependent. TDP-43, an RBP that is implicated in neurodegenerative diseases, modulates the TIRR/53BP1 complex by promoting the production of the NEAT1 short isoform, NEAT1_1. Together, we infer that NEAT1_1, and factors regulating NEAT1_1, may impact 53BP1-dependent DNA repair processes, with implications for a spectrum of diseases. - Source: PubMed
Publication date: 2024/09/30
Kilgas SusanSyed AleemToolan-Kerr PatrickSwift Michelle LRoychoudhury ShrabastiSarkar AniruddhaWilkins SarahQuigley MikaylaPoetsch Anna RBotuyan Maria VictoriaCui GaofengMer GeorgesUle JernejDrané PascalChowdhury Dipanjan