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Functional aspects of protein mono‐ADP‐ribosylation
Author(s) -
Corda Daniela,
Di Girolamo Maria
Publication year - 2003
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/cdg209
Subject(s) - biology , adp ribosylation , adp ribosylation factor , computational biology , genetics , microbiology and biotechnology , biochemistry , enzyme , nad+ kinase , golgi apparatus , cell
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 β‐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.