Physiological relevance of the endogenous mono(ADP-ribosyl)ation of cellular proteins.
The mono(ADP-ribosyl)ation reaction is a post-translational modification that is catalysed by both bacterial toxins and eukaryotic enzymes, and that results in the transfer of ADP-ribose from betaNAD+ to various acceptor proteins. In mammals, both intracellular and extracellular reactions have been described; the latter are due to glycosylphosphatidylinositol-anchored or secreted enzymes that are able to modify their targets, which include the purinergic receptor P2X7, the defensins and the integrins. Intracellular mono(ADP-ribosyl)ation modifies proteins that have roles in cell signalling and metabolism, such as the chaperone GRP78/BiP, the beta-subunit of heterotrimeric G-proteins and glutamate dehydrogenase. The molecular identification of the intracellular enzymes, however, is still missing. A better molecular understanding of this reaction will help in the full definition of its role in cell physiology and pathology.
Di Girolamo
Maria
M
Department of Cell Biology and Oncology, Consorzio Mario Negri Sud, Santa Maria Imbaro, Chieti, Italy. mdigirolamo@negrisud.it
Dani
Nadia
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Stilla
Annalisa
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Corda
Daniela
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D036002:ADP Ribose Transferases / Q000737:chemistry / Q000378:metabolism* / Q000502:physiology; D000818:Animals; D000091342:Endoplasmic Reticulum Chaperone BiP; D006801:Humans; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000378:metabolism*; D015398:Signal Transduction; D013379:Substrate Specificity
D000091342:Endoplasmic Reticulum Chaperone BiP; C000717247:HSPA5 protein, human; D011506:Proteins; D036002:ADP Ribose Transferases