AMPylation Mouse Polyclonal Antibody

AMPylation, also known as adenylylation, is a reversible post-translational modification of proteins. In this process, a class of enzymes called "AMPylases" covalently attaches an AMP (adenosine monophosphate) group from ATP to serine, threonine, or tyrosine residues on target proteins. This dynamic process is precisely regulated by "writers" (AMPylases) and "erasers" (de-AMPylases), thereby fine-tuning the function of the modified proteins. AMPylation was first discovered in 1967 in the regulation of bacterial glutamine synthetase, and its biological significance is profound. It is not only exploited by pathogenic bacteria to hijack host cell signaling to promote infection, but also plays critical physiological roles in humans—for example, the ER-localized enzyme FICD regulates the activity of the chaperone BiP in response to unfolded protein stress. Recent studies have further revealed that AMPylation plays important roles in various physiopathological processes, including metabolic regulation, neurodevelopment, diabetes, and cancer metastasis.