ADP-ribosyltransferase 1 (ART1)

**ADP-ribosyltransferase 1 (ART1)** is a glycosylphosphatidylinositol (GPI)-anchored, membrane monomeric enzyme that catalyzes the transfer of ADP-ribose from NAD⁺ to arginine residues on target proteins. This mono-ADP-ribosylation is a key post-translational modification affecting protein function, localization, and interactions. ART1 modulates the activity of antimicrobial peptides (such as human neutrophil peptide-1), plays a role in muscle regeneration by activating satellite cells, and contributes to tumor progression and metastasis in colorectal cancer through angiogenic signaling pathways. ART1 belongs to the ARTC family (Cholera toxin-like mono-ADP-ribosyltransferases), is predominantly expressed as a cell surface enzyme, and is implicated in modifying diverse peptide and protein substrates in various tissues[1][3][5]. Improper regulation or overexpression of ART1 can drive disease progression, especially in cancer and inflammatory states.

Other names

GPI-linked NAD(P)(+)-arginine ADP-ribosyltransferase 1CD296ARTC1Mono(ADP-ribosyl)transferase 1RT6ADP-ribosyltransferase 2ADP-ribosyltransferase C2 and C3 toxin-like 1mono(ADP-ribosyl)transferase 1

Inhibition of arginine-specific ADP-ribosyltransferase blocks mono-ADP-ribosylation, interfering with regulatory functions in cell signaling and immune response. Inhibitor molecules can mimic impaired substrate or block access to arginine residues, preventing post-translational modification.