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This study suggests that simultaneous blockade of Arf1 and Ras activation in prostate cancer cells is a potential targeted therapeutic strategy for preventing prostate cancer development.
Silencing of ARF1 impaired RAC1 recruitment to leading edge in neutrophil chemotaxis.
Data show that only ADP-ribosylation factor 1 (ARF1) promoter hypermethylation was significantly associated with epidermal growth factor receptor (show EGFR Proteins) gene (EGFR (show EGFR Proteins)) gene amplification in glioblastoma.
The zebrafish-metastasis model confirms that the ARF1 gene depletion suppresses breast cancer cells to metastatic disseminate throughout fish body.
ARF1 is a critical regulator in prostate cancer progression
our findings demonstrate that ARF1 is a molecular switch for cancer progression and thus suggest that limiting the expression/activation of this GTPase (show RACGAP1 Proteins) could help improve outcome for breast cancer patients.
changes in distinct lipid ratios may converge on ARF1 to increase SBP-1/SREBP-1 (show SREBF1 Proteins) activity.
Experiments using a mutant form of ARF1 affecting GTP (show AK3 Proteins) hydrolysis suggest that ARF1[GTP (show AK3 Proteins)] is functionally required for the tubules to form.
ARNO-ARF1 regulates formation of podosomes by inhibition of RhoA/myosin-II and promotion of actin core assembly.
Activation of ARF1 dissociates ADRP (show PLIN2 Proteins) from lipid droplets. A constitute active form of ARF1 (ARF1Q71I) promotes HCV assembly. ADRP (show PLIN2 Proteins) played a positive role in Hepatitis C virus replication and negative role in Hepatitis C virus assembly.
The authors found that Arf1 occupies contrasting molecular environments within the Coat Protein (show GOLPH3 Proteins) Complex I, leading them to hypothesize that some Arf1 molecules may regulate vesicle assembly while others regulate coat disassembly.
ARF1 may be a plausible inter-player that mediates the transition to osteoclast fusion at multiple steps during osteoclast differentiation.
Increased gene dosage of Ink4a, Arf1 and p53 (show TP53 Proteins) delays age-associated central nervous system functional decline.
ARF1/TBCE (show TBCE Proteins)-mediated cross-talk that coordinates COPI formation and tubulin (show TUBB Proteins) polymerization at the Golgi.
These data establish for the first time that the Arf1 gene is indispensable for mouse embryonic development after implantation.
Arf modulates LRP6 (show LRP6 Proteins) phosphorylation for the transduction of Wnt (show WNT2 Proteins)/beta-catenin (show CTNNB1 Proteins) signaling.
Down-regulation of ADP-ribosylation factor results in corneal neovascularization regression.
ARF1-dependent trafficking of procathepsin B and the maturation of autophagosomes results in cathepsin B-mediated trypsinogen activation induced by caerulein.
Egr1 mediates p53-independent c-Myc-induced apoptosis via a noncanonical ARF-dependent transcriptional mechanism
A senescence rescue screen identifies BCL6 as an inhibitor of anti-proliferative p19(ARF)-p53 signaling
findings reveal a novel signalling pathway involved in development of the semicircular canal system, and suggest a previously unrecognized role for NCS-1 (show NCS1 Proteins) in mitochondrial function via its association with several mitochondrial proteins.
Vascular endothelial growth factor receptor-2 (show KDR Proteins) activates ADP-ribosylation factor 1 to promote endothelial nitric-oxide synthase (show NOS3 Proteins) activation and nitric oxide release from endothelial cells
Data show that AP-1 (show JUN Proteins) recruitment to the cell membrane was found to be dependent on myristoylated ADP-ribosylation factor (ARF1), GTP (show AK3 Proteins) or nonhydrolyzable GTP (show AK3 Proteins)-analogs, tyrosine signals, and small amounts of phosphoinositides.
NCS-1 (show NCS1 Proteins)-ARF1 interaction provides evidence for functional cross-talk between Ca(2 (show CA2 Proteins)+)-dependent and ARF-dependent pathways in TGN (show TG Proteins) to plasma membrane traffic
The ARF1 machinery also might produce movement- and fission-promoting forces through actin polymerization.
Binding of cargo signal peptides to AP-1 (show JUN Proteins) induces a conformational change in its core domain that greatly enhances its interaction with Arf-1-GTP (show AK3 Proteins).
Study shows that ARF DNA-binding domains ahomodimerize to generate cooperative DNA binding, which is critical for in vivo ARF5 (show ARF5 Proteins)/MP function. Strikingly, DNA-contacting residues are conserved between ARFs, and found that monomers have the same intrinsic specificity; ARF1 and ARF5 (show ARF5 Proteins) homodimers, however, differ in spacing tolerated between binding sites.
Data indicate that ArfGAP domain8 (AGD8) and ARF-GAP domain 9 (AGD9), are involved in the recruitment of Arf1-GDP to the Golgi apparatus .
ADP-ribosylation factor 1 (ARF1) is a member of the human ARF gene family. The family members encode small guanine nucleotide-binding proteins that stimulate the ADP-ribosyltransferase activity of cholera toxin and play a role in vesicular trafficking as activators of phospholipase D. The gene products, including 6 ARF proteins and 11 ARF-like proteins, constitute a family of the RAS superfamily. The ARF proteins are categorized as class I (ARF1, ARF2 and ARF3), class II (ARF4 and ARF5) and class III (ARF6), and members of each class share a common gene organization. The ARF1 protein is localized to the Golgi apparatus and has a central role in intra-Golgi transport. Multiple alternatively spliced transcript variants encoding the same protein have been found for this gene.
ADP-ribosylation factor 1
, adp-ribosylation factor 1