ARL4D Human

ARL4D is a small GTP-binding protein that cycles between an inactive GDP-bound form and an active GTP-bound form. The rate of this cycling is regulated by guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs). Unlike some other GTP-binding proteins, ARL4D does not act as an allosteric activator of the cholera toxin catalytic subunit .

One of the unique features of ARL4D is its nuclear localization signal, which allows it to be transported into the nucleus. This protein also has an unusually high guanine nucleotide exchange rate, which is a characteristic shared with its close relatives ARL4A and ARL4C .

ARL4D plays a crucial role in membrane-associated intracellular trafficking. It recruits various cytohesin proteins (CYTH1, CYTH2, CYTH3, and CYTH4) to the plasma membrane in its GDP-bound form. This recruitment is essential for the proper functioning of these proteins in cellular signaling pathways .

Mutations in the ARL4D gene have been associated with Bardet-Biedl syndrome, a genetic disorder that affects multiple body systems and leads to symptoms such as vision loss, obesity, and kidney abnormalities . Additionally, ARL4D has been implicated in other diseases, including localized chondrosarcoma and X-linked spondyloepiphyseal dysplasia tarda .

Recombinant ARL4D proteins are produced using various expression systems, such as Escherichia coli (E. coli). These recombinant proteins are used in research to study the function and regulation of ARL4D, as well as its interactions with other proteins. They are also employed in blocking experiments with corresponding antibodies to investigate the role of ARL4D in different cellular processes .