IMR Press / FBL / Volume 20 / Issue 2 / DOI: 10.2741/4315

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on imrpress.com as a courtesy and upon agreement with Frontiers in Bioscience.

Review
From toxins to mammalian enzymes: the diverse facets of mono-ADP-ribosylation
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1 Institute of Protein Biochemistry, National Research Council, Via Pietro Castellino 111, 80131 Naples, Italy
Front. Biosci. (Landmark Ed) 2015, 20(2), 389–404; https://doi.org/10.2741/4315
Published: 1 January 2015
Abstract

The ADP-ribosylation of proteins is a phylogenetically ancient mechanism that involves the transfer of ADP-ribose from nicotinamide adenine dinucleotide (NAD+) to specific amino acids of target proteins post-translationally. In the first part of this review, we briefly describe ADP-ribosylation as the mechanism of action of toxins, while giving particular emphasis to a non-conventional ADP-ribosylation reaction that is mediated by the fungal toxin brefeldin A (BFA). This modification results in the loss of the membrane fission activity of the C-terminal binding protein (CtBP)1/ BFA-ADP-ribosylated substrate (BARS), thus blocking progression of cells into mitosis, with important implications for the design of new anticancer drugs. In addition, we summarize the most recent findings on mammalian, intracellular mono-ADP-ribosyl transferase enzymes, underlining the emerging functional roles in which they are involved, including immune responses, transcriptional regulation, stress responses, cell survival. The observation that several mono-ADP-ribosyl transferases, such as Parp-10, PARP-12, PARP-13, are involved in a range of physiological processes points at the multifunctional feature of these proteins.

Keywords
mono-ADP-ribosylation
Toxins
Brefeldin A
PARPs
Immune Response
Cell Survival
Stress
Review
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