ARF6 antibody
- Known as:
- ARF6 (anti-)
- Catalog number:
- orb10131
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Biorbyt biorb
- 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
- 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 - The molecular underpinnings of obesity-induced insulin resistance, a key driver of type 2 diabetes mellitus (T2DM), remain incompletely understood, limiting targeted therapies. While our prior work revealed that miR‑548ab impairs glucose homeostasis by downregulating GULP1, the precise mechanism by which GULP1 regulates insulin sensitivity, particularly through the GLUT4 trafficking machinery, is unknown. This study aimed to elucidate the novel function and molecular basis of GULP1 in controlling insulin-stimulated GLUT4 translocation and systemic glucose metabolism. - Source: PubMed
Publication date: 2026/07/11
Wen XinMei JinJiang YidanQian MeiyuWang JuanXu ShiboSu YuruiXu LiliLiu QinZhao MengyuanZhang HuiziWang JingzhouWang CuizheZhang Jun - Brain capillaries sense neural activity and direct blood flow to active regions-a process termed neurovascular coupling that underlies activity-dependent increases in local perfusion (functional hyperemia). A key contributor to functional hyperemic responses is the capillary endothelial cell (cEC) inward rectifier K (Kir2.1) channel, which, when activated by neuronal activity-derived extracellular K, initiates vasodilatory electrical signals that propagate through the vascular network. Kir2.1 channel function requires continual production of its lipid cofactor, phosphatidylinositol-4,5-bisphosphate (PIP), and is compromised in mouse models of cerebral small vessel (cSVD). Although decreased PIP availability is a common feature of cSVDs, mechanisms underlying PIP synthesis remain poorly understood. We hypothesized that Arf6, a small GTPase expressed in cECs that stimulates PIP production, is critical for this process. Using patch-clamp electrophysiology, we demonstrate that inhibiting Arf6 activity progressively decreased cEC Kir2.1 channel activity. This deficit manifested as loss of capillary-to-arteriole electrical signaling in isolated vessels and diminished functional hyperemia in vivo. Exogenously provided PIP restored Kir2.1 currents and functional hyperemia after Arf6 inhibition or genetic knockdown. Collectively, our data suggest that cEC Arf6 sustains Kir2.1 activity by maintaining PIP levels and demonstrate that diminished PIP synthesis is sufficient to impair functional hyperemia. Furthermore, we identify Arf6 as a mechanistic link between PIP production and endothelial electrical signaling, highlighting Arf6 as a potential therapeutic target for restoring functional hyperemia. - Source: PubMed
Publication date: 2026/07/07
Noterman-Soulinthavong Maria FSancho Maríade la Cruz Saúl HuertaYarboro MichaelMandalà MaurizioKoide MasayoBeaufort NathalieTodorov-Völgyi KatalinMoreland EmmaHill-Eubanks DavidDichgans MartinNelson Mark T - CMG2/ANTXR2 functions as a Collagen VI receptor required for extracellular matrix homeostasis and as the primary portal for anthrax toxin entry. Mutations in CMG2 cause Hyaline Fibromatosis Syndrome (HFS), a rare and often fatal genetic disorder characterized by excessive extracellular matrix accumulation, yet the molecular mechanisms regulating CMG2 function remain poorly understood. We show that CMG2 is controlled by ordered cycles of S-acylation and deacylation that regulate its folding, trafficking, and signalling competence. S-acylation by ZDHHC7 on two juxtamembrane cysteines protects CMG2 from ER-associated degradation by stabilizing folding intermediates, leading to a ~ 5-fold increase in folded receptors competent for ER exit. In the Golgi, ZDHHC3-dependent acylation of a third cysteine promotes Arf6-mediated CMG2 transport to the plasma membrane, where it exerts its functions. Ligand binding triggers recruitment of the thioesterase APT2, which enables release of CMG2 from the actin cytoskeleton and endocytosis, linking extracellular recognition to intracellular signalling and uptake. Inhibition of APT2 reduces Collagen VI turnover and strongly attenuates anthrax toxin toxicity in a zebrafish model, showing lipidation cycles as regulators of receptor function and potential therapeutic targets. - Source: PubMed
Publication date: 2026/07/06
Abrami LaurenceJoliot OctaveBlaskovic SanjaValentin GuillaumeHevia Covadonga FMercier VincentKunz BéatriceMesquita Francisco Svan der Goot F Gisou