ARL8A

Yes, studies have shown that ARL8A can interact with other organelles such as the Golgi apparatus and mitochondria. This suggests that ARL8A may have additional functions in cellular processes related to these organelles.

ARL8A interacts with the microtubule plus-end-directed kinesin motor proteins to facilitate the transport of lysosomes along microtubules. This interaction helps position lysosomes near the periphery of cells, facilitating efficient fusion with phagosomes or other vesicles.

Dysregulation of lysosome function and trafficking pathways, including those involving ARL8A, has been implicated in neurodegenerative diseases such as Alzheimer's and Parkinson's disease. Targeting ARL8A and related proteins could potentially provide therapeutic strategies to modulate lysosomal dysfunction and alleviate disease pathologies.

As of now, no genetic disorders or specific mutations in ARL8A have been identified. However, variations or alterations affecting the pathways regulated by ARL8A could potentially contribute to certain diseases or conditions.

ARL8A interacts with various proteins, including SKIP (SifA and kinesin-interacting protein) and VARP (VPS9-ankyrin repeat protein), which are involved in tethering and docking of phagosomes to lysosomes. Other known interacting partners include SKIPR-1, Hook1, and Dynactin.

Yes, ARL8A has been shown to play a role in autophagy, a cellular process responsible for the degradation of damaged organelles or proteins. It regulates the maturation and fusion of autophagosomes with lysosomes, aiding in the degradation of the autophagic cargo.

ARL8A is expressed in a variety of cell types, including both normal and cancer cells. Its expression levels may vary in different tissues and cell types, suggesting potential cell-specific functions or regulation.

Currently, there are no specific natural inhibitors or activators identified for ARL8A. However, studies are ongoing to discover small molecule compounds or modulators that can selectively target ARL8A activity for potential therapeutic applications.

Yes, ARL8A has been shown to be involved in immune responses by facilitating phagosome-lysosome fusion and degradation of engulfed pathogens in immune cells. Its interaction with proteins like SKIP and VARP in immune cells helps mediate the intracellular trafficking of phagosomes and regulate immune responses.

Currently, no specific diseases have been directly linked to ARL8A. However, dysregulation of lysosome-related processes, in which ARL8A is involved, can contribute to conditions such as lysosomal storage disorders and neurodegenerative diseases.

ARL8A has potential as a therapeutic target due to its involvement in various cellular processes and its role in diseases related to lysosomal dysfunction or membrane trafficking. However, more research is needed to fully understand its mechanisms and develop specific interventions.

Yes, ARL8A interacts with various proteins to carry out its cellular functions. It interacts with kinesin motor proteins, SKIP, and VARP, among others, to participate in organelle trafficking, immune responses, and phagosome-lysosome fusion.

Yes, ARL8A proteins are highly conserved across different species, including mammals, flies, worms, and plants. This suggests that ARL8A has important cellular functions that are preserved throughout evolution.