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.
Corda
Daniela
D
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
Di Girolamo
Maria
M
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