This website uses cookies to ensure you get the best experience on our website.
- Table of Contents
17 Q&As
Facts about ADP-ribosylation factor 6.
Involved in the regulation of dendritic spine growth, contributing to the regulation of dendritic branching and filopodia extension (PubMed:14978216). Plays an essential role in membrane trafficking, during junctional remodeling and epithelial polarization.
Human | |
---|---|
Gene Name: | ARF6 |
Uniprot: | P62330 |
Entrez: | 382 |
Belongs to: |
---|
small GTPase superfamily |
ADP-ribosylation factor 6; DKFZp564M0264
Mass (kDA):
20.082 kDA
Human | |
---|---|
Location: | 14q21.3 |
Sequence: | 14; NC_000014.9 (49893082..49897054) |
Ubiquitous, with higher levels in heart, substantia nigra, and kidney.
Cytoplasm, cytosol. Cell membrane; Lipid-anchor. Endosome membrane; Lipid-anchor. Recycling endosome membrane; Lipid-anchor. Cell projection, filopodium membrane; Lipid-anchor. Cell projection, ruffle. Cleavage furrow. Midbody, Midbody ring. Early endosome membrane; Lipid-anchor. Golgi apparatus, trans-Golgi network membrane; Lipid-anchor. Distributed uniformly on the plasma membrane, as well as throughout the cytoplasm during metaphase. Subsequently concentrated at patches in the equatorial region at the onset of cytokinesis, and becomes distributed in the equatorial region concurrent with cl
The ARF6 protein is found in many tissues, and the ARF6 marker helps scientists investigate the biological processes that are involved in cell signaling. The protein can be utilized by scientists for a variety of purposes such as membrane staining and colocalization analysis. The versatile protein can also be used for autoradiography, a popular method in detecting radioactive substances.
ARF6 is a protein on the cell surface that regulates the release of microvesicles. The ARF6 molecule is activated in cancer cells, which facilitates the release of microvesicles. It also has a correlation with the progression of cancer. The 10,000 g fraction contains the highest amount of ARF6 protein. The fraction contains both endogenous ARF6 mutant cells. In this fraction, ARF6 is highly abundant and microvesicles have a greater size than those of the parent LOX cells. The mutant ARF6 GTP does not accumulate on the shed vesicles.
Inactive ARF6 resides in the cytosol and in endosomes. GST-GGA3 ARF6 fusion protein GST determines the GTP-bound ARF6. All prostate cell lines were tested. PC-3 and LNCaP cells had higher levels of ARF6-GTP than PC-3 or CAHPV-10 cells. ARF6 protein was also confirmed by Western blotting and densitometry.
Additionally, immunofluorescence labeling LOX tumor cells shows local expression of phosphorylation of the MLC on the cell surface. ARF6 regulation is controlled by ERK. In this scenario, ARF6 promotes ERK activation. The ARF6 protein is a member of the Ras superfamily of GTPases. This protein is widely expressed in the tissues of PCa patients, however the number of studies published on the role of ARF6 in PCa is limited.
LOXARF6 cell lines were grown and probed for ARF6 and a-tubulin. The ARF6 bands are endogenous and HA tags are exogenous ARF6 respectively. Cells containing the GTP clones of LOXARF6 were allowed to penetrate into the medium and stained for cortactinand actin and b1 Integrin. The LOXARF6-GTP cells show an arborization phenotype when gelatin is relatively thick.
ARF6 is involved in cell invasion and has been proven to be connected to HGF signaling in invasive cells. PCa cells that are noninvasive expressed ARF6 exchange factor GEP100. These results demonstrate the importance of ARF6 activation in cancerous cells. However, further research is necessary to determine the purpose of ARF6. Therefore, membrane staining with the ARF6 marker will be an important step in the study of cancer cells.
Colocalization analyses were used to identify markers of recycling endosomes like ARF6 small GTPase or Rab11, for instance. These potential molecules have been identified as recycling endosomal within the literature, however, their intracellular distributions are not known. Colocalization analysis has been employed in a variety of studies to study the function of these proteins in recycling endosomes.
Recent studies have demonstrated that Arf6 regulates both the endocytosis and the recycling of HD Integrins. The knockdown of Arf6 reduces the process of endocytosis in synaptic vesicles and leads to the formation of large, endosome-like structures. HD formation requires dynamic shuttling Integrins A6b4.
We observed that synapses that had Arf6 deficient synapses showed higher SVs than synapses with Arf6. In these studies, we discovered that Arf6 activity regulates the abundance of docked SVs present in the synapses of neurons with Arf6-kD. This finding also demonstrates that Arf6 activity regulates the differential response of synapses to network activity.
These results suggest that a lack of Arf6 activation is enough to cause accumulation of total SVs, Elos, and SVs in the AZ. These results indicate that the Elos that accumulate Elos could be temporary structures, rather than stable organelles. We will continue to investigate these experiments to gain insights into their function. We are only at the beginning stages of our understanding of recycling.
The LOXARF6–GTP proteins were used to identify this gene order to determine whether it is activated. Western blot analysis identified bands that correspond to ARF6 and b1-integrin. This protein exhibits the same topological effects at different subcellular locations when ARF6-GTP is used as a marker. This allows researchers to confirm ARF6 mutants that have high levels of cellular expression.
The depletion of ARF6 affected EGFR budding and reduced ILV maturation. Furthermore, ARF6 has a role in late endosomal trafficking. These findings indicate that ARF6 is crucial for the exosome biogenesis. The ARF6 marker is a way to measure viral release indirectly. This protein is expressed in a variety of cell types, including mouse, human and worms.
To determine the relative protein content of a specimen, ARF6 and LAMP2 RNAi was used. The antibodies were purchased from Dharmacon Inc. They were used with a lysis buffer and anti-ARF6 antibodies. Also purchased were the PLD1 and 2 siGENOME Smartpools. The analysis was carried out in three independent studies.
ARF6 is responsible for the maturation of filopodia that are still in the embryo stage to mature spinal spines. ARF6 regulates synapses' development as well as axonal lengthenation. It also regulates the endocytosis of synaptic vesicles in presynaptic neurons. When ARF6 is decreased, neuronal activity decreases and the kainic acid-resistant ends grow.
To determine the effect of ARF6 silencing on cholesterol efflux, the ARF6 gene was expressed in cells. The overexpression of ARF6 did not alter the abundance of Abca1 or Lamp1 in cholesterol-loaded cells. In addition, the suppression of ARF6 did not affect the colocalization of Abca1 and Rab11.
Western blot analysis revealed that ARF6 was expressed in the mouse neuronal lineage. Long-term synaptic depression is caused by ARF6. ARF6 also regulates the activity of AMPA receptors. It also regulates neuronal maturation and migration. It is crucial to understand that this gene could be functionally redundant in certain human brains.
The ARF6 gene is a powerful tumor suppressor, and its increased expression can be a target for anti-cancer drugs. Boster Bio is a website dedicated to providing ELISA kits that are extremely sensitive to the ARF6 gene. It comes with a gene search tool and gene infographics that ensure you can quickly find your gene of choice. Below are a few of its most useful uses.
PMID: 1993656 by Tsuchiya M., et al. Molecular identification of ADP-ribosylation factor mRNAs and their expression in mammalian cells.
PMID: 14659046 by Lebeda R.A., et al. Sequence, genomic organization, and expression of the human ADP- ribosylation factor 6 (ARF6) gene: a class III ARF.