Functional aspects of protein mono-ADP-ribosylation.
Mono-ADP-ribosylation is the enzymatic transfer of ADP-ribose from NAD(+) to acceptor proteins. It is catalysed by cellular ADP-ribosyltransferases and certain bacterial toxins. There are two subclasses of cellular enzymes: the ectoenzymes that modify targets such as integrins, defensin and other cell surface molecules; and the intracellular enzymes that act on proteins involved in cell signalling and metabolism, such as the beta-subunit of heterotrimeric G proteins, GRP78/BiP and elongation factor 2. The genes that encode the ectoenzymes have been cloned and their protein products are well characterized, yet little is known about the intracellular ADP-ribosyltransferases, which may be part of a novel protein family with an important role in regulating cell function. ADP-ribosylation usually leads to protein inactivation, providing a mechanism to inhibit protein functions in both physiological and pathological conditions.
Department of Cell Biology and Oncology, Istituto di Ricerche Farmacologiche 'Mario Negri', Consorzio Mario Negri Sud, Via Nazionale, 66030 Santa Maria Imbaro, Chieti, Italy. corda@negrisud.it
Daniela
D
Corda
Maria
M
Di Girolamo
D000246:Adenosine Diphosphate Ribose / Q000378:metabolism*; D000818:Animals; D000091342:Endoplasmic Reticulum Chaperone BiP; D006801:Humans; D011506:Proteins / Q000378:metabolism*; D013379:Substrate Specificity
D000091342:Endoplasmic Reticulum Chaperone BiP; C000717247:HSPA5 protein, human; D011506:Proteins; D000246:Adenosine Diphosphate Ribose