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PMID: 12727863 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Review

Functional aspects of protein mono-ADP-ribosylation.

The EMBO journal ·Vol. 22 ·No. 9 ·2003-05-01 ·Pages 1953-8

Corda D, Di Girolamo M

Abstract

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.

MeSH Terms
Adenosine Diphosphate Ribose/metabolism Animals Endoplasmic Reticulum Chaperone BiP Humans Proteins/metabolism Substrate Specificity
Chemicals
Endoplasmic Reticulum Chaperone BiP HSPA5 protein, human Proteins Adenosine Diphosphate Ribose
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Corda Daniela
Department of Cell Biology and Oncology, Istituto di Ricerche Farmacologiche 'Mario Negri', Consorzio Mario Negri Sud, Via Nazionale, 66030 Santa Maria Imbaro, Chieti, Italy. [email protected]
Di Girolamo Maria
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
DOI
10.1093/emboj/cdg209
Email
[email protected]
Published
2003-05-01
Pages
1953-8
Language
English
Region
England
NLM ID
8208664
PMCID
PMC156081
Subset
IM
Grants
Telethon · E.0841 · Italy
External Links
PubMed source DOI: 10.1093/emboj/cdg209 PMC Full Text View journal details
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