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ADP-Ribosylation Factors (ARF)
Browse products name by alphabetical order:
|Cat. #||Product Name||Price|
|A24001||ADP-Ribosylation Factor 6, ARF6 (2-13)||Inquiry|
|A24003||ADP-Ribosylation Factor 1, ARF1 (2-17)||Inquiry|
ADP-ribosylation factor (ARF) is widely present on the membrane of eukaryotic cells and belongs to the small G protein Ras family. It is a GTP-binding protein with molecular weight of 20×103. ARF was first discovered in 1982 and its name was based on its ability to act as a cofactor for cholera toxin-catalyzed Gs protein ADP ribosylation. At present, ARF is related to the Golgi complex and plays an important role in vesicle transport, phospholipid metabolism, endocytosis, actin rearrangement, and cytoskeletal maintenance, and exerts biological functions in intracellular material transport and signal transduction. The ARF is composed of an alpha helix at the N-terminus and two identical effector domain regions, Switch 1 and Switch 2. In recent years, researchers have found that its abnormal expression is closely related to the occurrence of a variety of tumors.
Mechanism of action
It was first discovered in yeast that ARF is involved in the physiological function of the Golgi apparatus. ARF controls the formation of vesicles in the Golgi apparatus and is a key component of the vesicle transport pathway. ARF is primarily involved in endosome fusion, nuclear membrane assembly, and formation of clathrin-coated vesicles. During vesicle transport from the endoplasmic reticulum to the Golgi apparatus, ARF needs to bind to another type of coat protein COP to form COP-coated vesicles. Therefore, the functions of ARF in vesicle transport include the formation of vesicles by exo-protein binding and the promotion of fusion of vesicles with the target membrane.
Application of ADP-Ribosylation Factors
ARF is associated with the formation and development of digestive tract tumors, such as esophageal cancer, gastric cancer, colorectal cancer, liver cancer, and pancreatic cancer. It is related to tumor malignancy, invasion, and prognosis. It’s necessary to figure out how to regulate the expression of target genes by ARF to control the growth of digestive tract tumors. The inhibition of the expression of ARF in tumors is an attractive idea for the treatment of tumors.
1. Hiroi, T. (2009). Regulation of epithelial junctions by proteins of the ADP-ribosylation factor family. Front Biosci, 14, 717-730.
2. Randazzo, P. A., Nie, Z., Miura, K., & Hsu, V. W. (2000). Molecular aspects of the cellular activities of ADP-ribosylation factors. Science Signaling, 2000(59), re1-re1.