ARF6 Antibody
- Known as:
- ARF6 Antibody
- Catalog number:
- csb-pa001996esr1hu
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- CusAb
- Gene target:
- ARF6 Antibody
Related genes to: ARF6 Antibody
- Gene:
- ARF6 NIH gene
- Name:
- ADP ribosylation factor 6
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 14q21.3
- Locus Type:
- gene with protein product
- Date approved:
- 1994-02-01
- Date modifiied:
- 2015-11-19
Related products to: ARF6 Antibody
Related articles to: ARF6 Antibody
- Conventional vaccine adjuvants often lack cell-type specificity and readily trigger excessive systemic inflammation, limiting their clinical application. Immunometabolic signaling centered on the ARF6 (ADP-ribosylation factor 6)-SUCNR1 (Succinate receptor 1) axis governs neutrophil recruitment and subsequent B-cell activation at vaccination sites, offering a promising target to balance adjuvant potency and biosafety. Separately published single-gene data confirm two opposing functions for the two mediators: ARF6 overactivation amplifies local pathological inflammation, whereas succinate-stimulated SUCNR1 drives neutrophil infiltration and humoral immune priming. However, direct paired evidence verifying their bidirectional crosstalk within immunization microenvironments remains limited. This review systematically integrates current research on ARF6 and SUCNR1 immunometabolism to outline a hypothetical dual-regulatory adjuvant strategy: local, transient partial silencing of pathological ARF6 activity via ARF6-targeted ASOs (antisense oligonucleotides) paired with localized succinate delivery to sustain protective SUCNR1 signaling. We summarize the molecular basis of this "one inhibition, one activation" paradigm, alongside ASO chemical modification, myeloid-targeted design, and nanocarrier delivery solutions that resolve the unique ARF6 endocytosis paradox. We further dissect unresolved translational risks, including concentration-dependent succinate inflammatory effects, carrier immunogenicity, and potential impairment of baseline neutrophil migration upon ARF6 suppression. Overall, this work synthesizes fragmented mechanistic data to construct a testable neutrophil-centered adjuvant framework, and highlights outstanding technical and biosafety hurdles that require dedicated preclinical validation to support future adjuvant development. - Source: PubMed
Publication date: 2026/08/04
Wang YangyangChen Ye - Alzheimer's disease (AD) is a progressive neurodegenerative disorder characterized by the buildup of aggregated amyloid-beta (Aβ) peptides. We previously demonstrated that Aβ is produced from APP following its lysosomal internalization via macropinocytosis. However, the regulation of APP macropinocytosis in neuronal cells remained uncharacterized. Arf6 and the Rho GTPases Rac1, Cdc42 and RhoA are known to regulate macropinocytosis in response to signaling at the cell surface. Fe65, an adaptor protein known to interact with APP, may link APP to these regulatory elements. We hypothesized that APP binding/crosslinking recruits Fe65, which recruits/activates Arf6 and then Rac1, Cdc42, and RhoA, driving APP macropinocytosis. We found that antibody-mediated binding/crosslinking APP resulted in the transient recruitment of Fe65 and Arf6 to APP within 30 s of APP binding/crosslinking. Rac1, Cdc42, and RhoA were also recruited at 30 s, but remained recruited through 2 min. The mutation of the APP 'YENPTY' sequence and Arf6 inhibition by NAV-2729 prevented the recruitment of Rac1, Cdc42, and RhoA. Together, these observations are the first to demonstrate that a network of regulatory proteins is recruited to bound/crosslinked APP and regulates its macropinocytosis. Targeting these regulatory proteins to modulate APP trafficking to the lysosome could be a therapeutic strategy to reduce Aβ production in AD. - Source: PubMed
Publication date: 2026/07/29
Krupa Jordan MMedapati Manoj ReddyNaqvi Abdul MHallam Ryan DTsang Adrianna RSeah ClaudiaWhitehead Shawn NPasternak Stephen H - Transcription factor SNAI1 guides plasticity and invasiveness in cancer. Using a complete SNAI1 knockout in mesenchymal, triple-negative breast cancer cells, unbiased genome-wide transcriptomic analysis revealed a marked under-expression of integrin-based adhesion and endocytic components. Utilizing this knockout cell model, complementary breast cancer cell models and functional screening of multiple differentially expressed genes, we found that the pioneering transcription factor FOXA1, whose expression is repressed by SNAI1, associates with several key mediators of the cellular phenotype. FOXA1 represses the small GTPase ARF6 and its exchange factor PSD4. In addition, some of the integrin and matrix metalloproteinase genes are regulated by the transcriptional FOXA1 signal. Accordingly, SNAI1 knockout cells presented poor adhesion to collagen type I or fibronectin, formed defective invadopodia and focal adhesions with weakened FAK/SRC signaling. SNAI1 knockout cells performed ineffective receptor-mediated internalization, including nanoparticle and extracellular vesicle (EV) uptake, exhibited reduced lysosomal content, lacked multivesicular bodies enriched in intraluminal vesicles and showed decreased EV secretion. Gain-of-function experiments demonstrated that SNAI1 has an impact on the PSD4/ARF6 signaling module, using FOXA1 as an intermediate factor to regulate EV release by tumor cells. We propose that the SNAI1-FOXA1 transcriptional mechanism operates at the level of membrane and vesicular trafficking control, which interlinks cell plasticity, adhesion and invasiveness through the extracellular environment, with the associated process of EV secretion. - Source: PubMed
Publication date: 2026/08/12
Tsirigoti ChrysoulaAli Mohamad MoustafaMorén AnitaJohansson StaffanMunson Michael JHeldin Carl-HenrikMoustakas AristidisRodrigues-Junior Dorival Mendes - In our recent study (Watthanakitphibun et al., 2026), we reported remarkable membrane modifications in the basolateral cell domains of attenuated epithelial cells in dilated distal tubules and collecting ducts in the renal cortex, predominantly in the former, induced by unilateral ureteral obstruction (UUO). These modifications included the disappearance of typical basal infoldings and the appearance of ellipsoidal membrane sacs containing thin cytoplasmic processes along the basolateral cell membranes and within the cellular interior. We thus suggested that they represent a temporal sequence of membrane addition sources to compensate for the increased cell surface area associated with cell attenuation. To support the proposed temporal sequence of these membrane modifications, the present study examined the expression and localization of EFA6D, a molecule that plays a pivotal role in activating Arf6, whose involvement in membrane dynamics is well established, in the renal cortical tubules of adult mice under UUO. While EFA6D was faintly expressed in normal kidneys, western blotting revealed enhanced expression on UUO day 1, with significantly higher levels on days 3 and 5. Double immunofluorescence microscopy showed EFA6D immunoreactivity localized in attenuated cells of dilated distal tubules dominantly and of collecting ducts less dominantly, but not significantly in proximal tubules. In ultrastructure, EFA6D was mainly localized in the ellipsoidal membrane sacs and clusters of small vesicles beneath the apical membranes in the attenuated epithelial cells. Our findings on the expression and cellular interior localization of EFA6D support the proposed temporal sequence of events: disappearance of basal infolding, followed by membrane sac formation, and subsequent membrane addition. This sequence promotes cell surface expansion associated with cell attenuation during tubule/duct dilation induced by UUO. - Source: PubMed
Publication date: 2026/07/22
Watthanakitphibun ApussaraKhrongyut SuthankamonSakagami HiroyukiChomphoo SurangKondo HisatakeHipkaeo Wiphawi - Obesity and type 2 diabetes mellitus (T2DM) represent pandemic metabolic illnesses hallmarked by defective pancreatic β-cell function and blunted insulin release. As a conserved small GTPase (guanosine triphosphatase), ADP-ribosylation factor 6 (ARF6) governs fundamental cellular events encompassing vesicle trafficking, cytoskeleton remodeling and lipid metabolic turnover. Emerging data confirm that ARF6 acts as a master rheostat of glucose-stimulated insulin secretion (GSIS) in β-cells through downstream cell division control protein 42/Ras-related C3 botulinum toxin substrate 1 (Cdc42/Rac1) cascades. Pathogenic ARF6 hyperactivation triggers a cascade of β-cell lesions: mitochondrial impairment, autophagic suppression and exacerbated inflammatory signaling, accelerating the progression of obesity and T2DM. First-line therapeutics ranging from GLP-1 (Glucagon-like peptide-1) receptor agonists and metformin to SGLT2 (Sodium-Glucose Cotransporter 2) inhibitors partially restore metabolic homeostasis by rectifying aberrant ARF6-dependent signaling axes. This review comprehensively delineates ARF6's canonical cellular roles, mechanistic bridges connecting ARF6 to β-cell failure and metabolic deterioration, and functional crosstalk between ARF6 and established anti-metabolic pharmacotherapies. We further address unresolved research gaps and prospective translational avenues, offering actionable perspectives to advance ARF6 as a tractable therapeutic target for obesity and T2DM management. - Source: PubMed
Publication date: 2026/07/21
Wang Yangyang