WDR39 Antibody
- Known as:
- WDR39 Antibody
- Catalog number:
- XW-8073
- Product Quantity:
- 0.05 mg
- Category:
- -
- Supplier:
- Prosci
- Gene target:
- WDR39 Antibody
Related genes to: WDR39 Antibody
- Gene:
- CIAO1 NIH gene
- Name:
- cytosolic iron-sulfur assembly component 1
- Previous symbol:
- WDR39
- Synonyms:
- CIA1
- Chromosome:
- 2q11.2
- Locus Type:
- gene with protein product
- Date approved:
- 2005-01-18
- Date modifiied:
- 2018-05-21
Related products to: WDR39 Antibody
Related articles to: WDR39 Antibody
- Porcine reproductive and respiratory syndrome virus (PRRSV; ) is a major global threat to swine production, yet effective antiviral therapies are lacking. The leader protease Nsp1α is essential for viral replication and innate immune suppression, and its N-terminal zinc-finger (ZF) domain is critical for function, although its molecular role remains unclear. Here, we show that the ZF domain plays only a minor role in protease activity and that Nsp1α is largely inactive following release from the polyprotein. Using Mössbauer and UV/visible spectroscopy combined with chemoproteomics, we demonstrate that the ZF site binds not only Zn but also a [4Fe-4S] cluster. Notably, the Fe-S cluster, but not Zn, allosterically modulates residual protease activity. Nsp1α directly engages the cytosolic iron-sulfur cluster assembly machinery via CIAO1 and competes with the Fe-S carrier CIAO3, establishing the [4Fe-4S] cluster as a cofactor. These findings redefine Nsp1α as an Fe-S-dependent viral protein and reveal new opportunities for metal-targeted antiviral strategies. - Source: PubMed
Publication date: 2026/01/06
Quist TrentBuzuk AnastasiyaNguyen Henry ThanhTakeoka KenBak Daniel WWeerapana EranthiePerlstein Deborah LPandelia Maria-Eirini - Dihydropyrimidine dehydrogenase (DPD), encoded by DPYD, is a key enzyme in pyrimidine catabolism, and its deficiency leads to severe toxicity in patients treated with 5-fluorouracil (5-FU). While pathogenic DPYD variants account for many cases of DPD deficiency, they do not fully explain all instances of 5-FU sensitivity, suggesting additional genetic factors are involved. Recent studies have implicated variants in CIAO1, a gene encoding a subunit of the cytosolic iron-sulfur (Fe-S) cluster assembly targeting complex, in reducing DPD stability and function. In this study, we established a C. elegans model to assess DPD deficiency and 5-FU sensitivity. Using a dpyd-1 knockout and CRISPR-generated ciao-1 variants that mirror patient-derived variants (p.Trp184Cys, p.His193Tyr, and p.Arg65Trp), we provide the first in vivo evidence that pathogenic variants in CIA complex components can lead to DPD deficiency and, consequently, heightened 5-FU toxicity. Our findings highlight the critical role of CIAO1 in DPD function and 5-FU tolerance, expanding the genetic landscape of DPD deficiency and offering a robust platform for functional evaluation of pathogenic variants. - Source: PubMed
Li XiaoMenendez Perdomo Ivette Mvan Kuilenburg André B PTarailo-Graovac Maja - - Source: PubMed
Chen Chih-PingWu Fang-TzuPan Yen-TingWang Wayseen - The cytosolic iron-sulfur cluster assembly (CIA) targeting complex maturates over 30 cytosolic and nuclear Fe-S proteins, raising the question of how a single complex recognizes such a diverse set of clients. The discovery of a C-terminal targeting complex recognition (TCR) peptide in up to 25% of CIA clients provided a clue to substrate specificity, yet the molecular and energetic basis for this interaction remained unresolved. By integrating computational and biochemical approaches, we show that the TCR peptide binds a conserved interface between the Cia1 and Cia2 subunits of the targeting complex, even in the absence of the Fe-S cluster. Since this same site also mediates binding of predominantly apo-Nar1, the proposed Fe-S cluster carrier, we provide evidence for Nar1's role as a cluster trafficking protein in the CIA pathway. We further show that Cia1-Cia2 complex formation is essential for CIA function as substitutions disrupting this interface, including the disease-linked R65W Cia1 variant, impair TCR peptide-dependent client recruitment. Our findings also clarify the role of the poorly characterized human paralog Cia2a, proposed to act solely in iron regulatory protein 1 (IRP1) maturation. We find that a Cia1-Cia2a complex can bind the TCR peptide, suggesting a broader role for Cia2a in Fe-S protein biogenesis, as IRP1 lacks a TCR motif. Together, these findings define a well-conserved molecular mechanism for client recognition in the CIA pathway and uncover how CIA targeting complex assembly and client identification are mechanistically linked to human disease. - Source: PubMed
Publication date: 2025/09/09
Buzuk AnastasiyaMarquez Melissa DHo Jackson VLiu YaxiWang BeatriceQi Chen ChengPerlstein Deborah L - Gastric cancer is a global health challenge, necessitating the identification of novel biomarkers and therapeutic targets. The present study aimed to assess the role of cuproptosisrelated genes (CRGs) in gastric cancer, with the goal of establishing a predictive model consisting of key regulators with prognostic significance, thereby enabling the identification of key genes. Data from The Cancer Genome Atlas and Gene Expression Omnibus databases were used to analyze CRGs in stomach adenocarcinoma (STAD). Least absolute shrinkage and selection operator regression analysis was applied to create a risk model, and its predictive accuracy was confirmed for several clinical subgroups. Moreover, the prognostic value of essential regulators was evaluated through multiple analyses. A risk model with 15 CRGs was used to effectively predict STAD prognosis, demonstrating areas under the receiver operating characteristic curve values of 0.822, 0.811 and 0.922 for 1-, 3- and 5-year overall survival rates, respectively. The risk scores were associated with survival and tumor site. Among the CRGs, the gene for cytosolic iron-sulfur assembly component 1 () was revealed to be critical and associated with histological type, age and treatment outcome. Moreover, single-cell analysis demonstrated that is highly expressed in numerous types of cancer cells, and a high expression of was associated with upregulated transcription levels of immune checkpoints, increased tumor mutation load and decreased immune scores, highlighting its complex role in the tumor microenvironment. knockdown experiments were performed, and eliminating was associated with a reduction in the levels of iron-sulfur proteins and an increase in heat shock protein 70 expression, thereby inducing copper-dependent cell death. Furthermore, treatment with the drugs dasatinib and AT-9283 were associated with an inhibition of expression in gastric cancer cells, and decreased rates of tumor spread and invasion. Taken together, the findings of the present study suggest that is a promising biomarker both for assessing prognosis and evaluating the tumor immune microenvironment of gastric cancer. - Source: PubMed
Publication date: 2025/07/14
Qu JiayingYang ChunhuiZhou ShunchenZhao BosenTong QiangsongZheng Liduan