ARF6B

Currently, there are no known specific drugs or inhibitors that exclusively target ARF6B. However, some studies have explored the use of general ARF inhibitors or modulators to investigate the functions of ARF6 and potentially impact ARF6B as well.

ARF6B has been shown to exhibit GTP-independent functions as well. For example, it can interact with other proteins to directly modulate actin cytoskeleton dynamics independent of its GTPase activity.

Yes, ARF6B interacts with various proteins and regulators to carry out its functions. For instance, ARF6B can interact with ARF nucleotide-binding site opener (ARNO)/cytohesin family of guanine nucleotide exchange factors (GEFs) to facilitate GDP-GTP exchange. It can also interact with different effectors, such as different classes of ARF6 effector proteins, to orchestrate specific cellular processes.

ARF6B is a splice variant of ARF6 with a slightly different amino acid sequence, resulting from alternative splicing of the ARF6 gene. It shares many functional similarities with ARF6A but may have distinct roles or regulation in specific cellular processes.

Yes, ARF6B can regulate immune cell functions. It has been shown to modulate immune cell adhesion, migration, phagocytosis, and antigen presentation.

Yes, ARF6B can regulate membrane trafficking in neuronal cells. It is involved in processes such as synaptic vesicle recycling, dendritic spine formation, and axonal growth.

Yes, ARF6B can interact with various signaling pathways. For instance, it has been shown to modulate the activity of small GTPases, such as Rac1 and RhoA, which are pivotal in regulating cytoskeletal dynamics and cell signaling.

Although limited information is available, some studies suggest that ARF6B may participate in cellular stress responses, such as oxidative stress, by modulating the trafficking and signaling of stress-related proteins.

There is emerging evidence suggesting that ARF6B may have a role in cancer progression and metastasis. It has been implicated in promoting invasive behavior, epithelial-to-mesenchymal transition (EMT), and metastatic dissemination of cancer cells.

ARF6B can undergo post-translational modifications, including palmitoylation and phosphorylation, which can regulate its membrane association and signaling functions.

There is limited information available regarding the direct involvement of ARF6B in insulin signaling or glucose metabolism. However, its close homolog, ARF6, has been implicated in insulin-stimulated glucose uptake in muscle cells.

ARF6B has several downstream effectors that mediate its cellular functions. These include proteins involved in actin cytoskeleton remodeling, endosomal trafficking machinery, membrane remodeling proteins, and signaling molecules such as PI3K and ERK.

Yes, ARF6B has been shown to play a role in neuronal development. It regulates processes such as neurite outgrowth, axon guidance, and synapse formation.

Yes, ARF6B has been implicated in the regulation of cell polarity. It can influence the localization and trafficking of polarity proteins, such as Par proteins and Cdc42, during processes like cell migration and epithelial polarization.

The involvement of ARF6B in diseases is relatively less studied compared to ARF6A. However, alterations in ARF6B expression or function could potentially contribute to pathologies associated with dysregulated membrane trafficking, cell adhesion, or cytoskeletal dynamics, such as cancer, neurodegenerative disorders, or cardiovascular diseases. Further research is needed to establish specific disease associations.

Currently, there is limited information on genetic mutations or polymorphisms specifically in ARF6B associated with diseases. However, variations in the ARF6 gene, which encodes ARF6B as a splice variant, have been linked to certain pathologies, highlighting potential implications for ARF6B as well.

Yes, ARF6B can interact with various membrane receptors, including receptor tyrosine kinases and G protein-coupled receptors, to modulate their endocytic trafficking, signaling, and downstream cellular responses.

Yes, studies have implicated ARF6B in the regulation of cell migration and invasion processes, particularly in cancer cells. It can modulate the expression and trafficking of adhesion molecules, like integrins, which are crucial for cell motility and invasion.