Ask about this productRelated genes to: Arf4 antibody
- Gene:
- ARF4 NIH gene
- Name:
- ADP ribosylation factor 4
- Previous symbol:
- ARF2
- Synonyms:
- -
- Chromosome:
- 3p14.3
- Locus Type:
- gene with protein product
- Date approved:
- 1992-07-09
- Date modifiied:
- 2015-11-19
Related products to: Arf4 antibody
Related articles to: Arf4 antibody
- Sepsis-associated acute lung injury (S-ALI) represents a significant clinical challenge due to its high incidence and mortality rates. Macrophages play a central and dual role in the pathogenesis of S-ALI, they serve as a critical component of the innate immune defense against pathogen invasion, while simultaneously contributing to the propagation of excessive inflammatory responses and tissue damage. Consequently, modulation of macrophage function has emerged as a promising therapeutic strategy for S-ALI. Accumulating evidence indicates that heme oxygenase-1 (HO-1, encoded by HMOX1) exerts endogenous protective effects in S-ALI. Our prior studies demonstrated that HO-1 ameliorates S-ALI by modulating oxidative stress in macrophages. Furthermore, emerging reports suggest that HO-1 may also mitigate this pathological process through regulation of Golgi stress; however, the underlying molecular mechanisms remain poorly defined. In this study, using both in vivo and in vitro models of S-ALI, we demonstrate that HO-1 in alveolar macrophages directly interacts with the transcriptional activation domain (TAD) of CREB3, leading to the degradation of the CREB3/ARF4 signaling pathway. Moreover, activated CREB3 suppresses HO-1 gene transcription, establishing a negative feedback regulatory loop. This mechanism effectively restricts CREB3 trafficking from the endoplasmic reticulum to the Golgi apparatus and its subsequent nuclear translocation, thereby preventing excessive activation of CREB3-dependent signaling pathways during S-ALI and attenuating Golgi stress. Additionally, clinical analyzes reveal that the expression levels of HO-1, CREB3, and ARF4 in peripheral blood mononuclear cells (PBMCs) from sepsis patients are significantly elevated compared to those in non-septic controls and positively correlate with APACHE II and SOFA scores. These markers demonstrate significant positive associations with established severity indices, suggesting that HO-1, CREB3, and ARF4-either individually or in combination-may serve as potential novel biomarkers for the diagnosis of sepsis, the assessment of disease severity, and the prediction of clinical outcomes. Collectively, these findings indicate that HO-1 alleviates Golgi stress in macrophages by inhibiting the CREB3/ARF4 axis, thus improving cellular functional homeostasis, and highlight their potential as both a diagnostic biomarker and a therapeutic target in sepsis. - Source: PubMed
Publication date: 2026/04/10
Kong ChangZhang YuanLi XiangyunRen GuangzhenGuo ChenxuLi MenghanLiu WeiqiangZhang DongchaoLi ChengyuShi JiaGong LirongYu Jianbo - Ferroptosis, characterized by iron-dependent lipid peroxidation, has emerged as a pivotal cell death pathway in various diseases, yet its regulation during viral infection remains elusive. Here, we reveal that Newcastle disease virus (NDV) exploits the Golgi apparatus as a central hub to orchestrate ferroptotic cell death in tumor cells. NDV infection provokes robust Golgi stress and Golgiphagy, leading to the selective degradation of ARF1 (ARF GTPase 1), a GA-resident regulator of redox homeostasis, which in turn triggers a cascade of reactive oxygen species accumulation, lipid peroxidation, and ferroptosis. Mechanistically, we show that this process is dependent on the activation of the Golgi stress response and macroautophagy/autophagy-lysosome pathway. Importantly, inhibition of Golgi stress by exogenous spermine not only alleviates NDV-induced ferroptosis, but also demonstrates antiviral and cytoprotective effects, underscoring the translational potential of targeting the Golgi stress axis. Our findings uncover a previously unappreciated axis of virus-host interaction centering on Golgi stress and ferroptosis and suggest that modulation of organelle-specific stress responses represents a promising therapeutic strategy in both antiviral and cancer contexts.: AMPK: AMP-activated protein kinase; ARF1: ARF GTPase 1; ARF4: ARF GTPase 4; ATG7: autophagy related 7; BFA: brefeldin A; CGAS: cyclic GMP-AMP synthase; CHX: cycloheximide; CQ: chloroquine; CREB3: cAMP responsive element binding protein 3; DFO: deferoxamine; ER: endoplasmic reticulum; Fe: ferrous ions, GA: Golgi apparatus; GOLGA2/GM130: golgin A2; GPX4: glutathione peroxidase 4; GSH: glutathione; GSR: Golgi stress response; HCMV: human cytomegalovirus; HSV-1: herpes simplex virus 1; Lip-1: Liproxstatin-1; MAP1LC3/LC3: microtubule associated protein 1 light chain 3; MDA: malondialdehyde; mtDNA: mitochondrial DNA; MTOR: mechanistic target of rapamycin kinase; NDV: Newcastle disease virus; NCOA4: nuclear receptor coactivator 4; PUFA: polyunsaturated fatty acid; ROS: reactive oxygen species; Rot: rotenone; SLC7A11: solute carrier family 7 member 11; SERPINH1/HSP47: serpin family H member 1; TFE3: transcription factor binding to IGHM enhancer 3; WT: wild-type. - Source: PubMed
Publication date: 2026/04/10
Kan XianjinYang MengqingXie GuangleiYin YuncongJiang HuiYuan YanmeiSun YingjieDing Chan - Metastasis is the leading cause of death related to breast cancer. Premetastatic niches (PMNs), which are remodelled by the primary tumours in distant organs, are essential for the colonisation of disseminated cancer cells. The vascular niche is among the most pivotal PMNs in breast cancer lung metastasis, and the underlying mechanism remains unclear. Here, we report that breast cancer cells secrete dipeptidyl peptidase 3 (DPP3) via small extracellular vesicles (sEVs) to promote lung metastasis. Mechanistically, circulating DPP3 upregulates RAPGEF4 to activate the Rap1 signalling pathway in the lung endothelial cells through the DPP3-PFKP-YBX1 axis and promotes angiogenesis to remodel the vascular niche, thereby increasing lung metastasis. In addition, ARF4 recognises ISGylated DPP3, which facilitates its packaging into sEVs in breast cancer cells. Finally, treatment with losartan pharmacologically inhibits the ISGylation of DPP3, preventing its secretion via sEVs. In summary, our findings demonstrate that DPP3, which is encapsulated in sEVs and secreted by breast cancer cells, regulates angiogenesis in the lung and remodels vascular niches to promote breast cancer lung metastasis, making it a potential target for the diagnosis and treatment of breast cancer metastasis. - Source: PubMed
Li XuHu ShengYuan ZiqiFu XiaoyuZhang XiaohuiLiu LiuWang ChaoqunYan WeiLi Juanjuan - Arfs are small Ras-superfamily proteins important for regulating membrane trafficking including the recruitment of vesicular coats as well as a diverse range of other functions. There are five Arfs in humans: two Class I Arfs (Arf1 and Arf3), two Class II Arfs (Arf4 and Arf5) and one Class III Arf (Arf6), with Class I and Class II Arfs present on the Golgi apparatus among other locations. These Golgi Arfs (Arf1, Arf3, Arf4 and Arf5) are highly similar in sequence, and knockout studies have established a complex pattern of redundancy, with Arf4 alone able to support cell survival in tissue culture. Moreover, adding to the complexity, functions of Arfs on distinct membranes can involve non-overlapping sets of effectors (e.g., COPI on -Golgi membranes and clathrin adaptors on -Golgi network). The three classes of Arfs are found in most metazoans, suggesting biologically important specialization the details of which are beginning to emerge. This review examines recent studies using siRNA and CRISPR/Cas9 knockouts of mammalian Arfs combined with functional assays of the secretory pathway in the context of detailed localization of fluorescently-tagged Arfs by fluorescent and super-resolution microscopy and the existing literature using more conventional techniques. We suggest that specificity of effector recruitment involves additional membrane determinants which need to be considered in future studies. - Source: PubMed
Publication date: 2025/07/31
Dejgaard Selma YilmazPresley John F - - Source: PubMed
Li Ming-YuanDeng KaoCheng Xiao-HeSiu Lewis Yu-LamGao Zhuo-RanNaik Trupti ShivaprasadStancheva Viktoriya GCheung Peter Pak-HangTeo Qi-Wenvan Leur Sophie WWong Ho-HimLan YunLam Tommy Tsan-YukSun Meng-XuZhang Na-NaZhang YueCao Tian-ShuYang FanDeng Yong-QiangSanyal SumanaQin Cheng-Feng