Toward a unified nomenclature for mammalian ADP-ribosyltransferases
Hottiger, Michael O ; Hassa, Paul O ; Lüscher, Bernhard ; Schüler, Herwig LU
and Koch-Nolte, Friedrich
(2010)
In Trends in Biochemical Sciences
35(4).
p.19-208
- Abstract
ADP-ribosylation is a post-translational modification of proteins catalyzed by ADP-ribosyltransferases. It comprises the transfer of the ADP-ribose moiety from NAD+ to specific amino acid residues on substrate proteins or to ADP-ribose itself. Currently, 22 human genes encoding proteins that possess an ADP-ribosyltransferase catalytic domain are known. Recent structural and enzymological evidence of poly(ADP-ribose)polymerase (PARP) family members demonstrate that earlier proposed names and classifications of these proteins are no longer accurate. Here we summarize these new findings and propose a new consensus nomenclature for all ADP-ribosyltransferases (ARTs) based on the catalyzed reaction and on structural features. A unified... (More)
ADP-ribosylation is a post-translational modification of proteins catalyzed by ADP-ribosyltransferases. It comprises the transfer of the ADP-ribose moiety from NAD+ to specific amino acid residues on substrate proteins or to ADP-ribose itself. Currently, 22 human genes encoding proteins that possess an ADP-ribosyltransferase catalytic domain are known. Recent structural and enzymological evidence of poly(ADP-ribose)polymerase (PARP) family members demonstrate that earlier proposed names and classifications of these proteins are no longer accurate. Here we summarize these new findings and propose a new consensus nomenclature for all ADP-ribosyltransferases (ARTs) based on the catalyzed reaction and on structural features. A unified nomenclature would facilitate communication between researchers both inside and outside the ADP-ribosylation field.
(Less)
- author
- Hottiger, Michael O
; Hassa, Paul O
; Lüscher, Bernhard
; Schüler, Herwig
LU
and Koch-Nolte, Friedrich
- publishing date
- 2010-04
- type
- Contribution to journal
- publication status
- published
- keywords
- ADP Ribose Transferases/chemistry, Animals, Catalytic Domain/genetics, Humans, Mammals/genetics, Poly(ADP-ribose) Polymerases/chemistry, Protein Processing, Post-Translational, Terminology as Topic
- in
- Trends in Biochemical Sciences
- volume
- 35
- issue
- 4
- pages
- 12 pages
- publisher
- Elsevier
- external identifiers
-
- pmid:20106667
- scopus:77951023118
- ISSN
- 0968-0004
- DOI
- 10.1016/j.tibs.2009.12.003
- language
- English
- LU publication?
- no
- id
- 5d34e617-2955-4081-a5f5-d7e58836549e
- date added to LUP
- 2024-11-21 18:01:22
- date last changed
- 2025-07-19 00:27:18
@article{5d34e617-2955-4081-a5f5-d7e58836549e,
abstract = {{<p>ADP-ribosylation is a post-translational modification of proteins catalyzed by ADP-ribosyltransferases. It comprises the transfer of the ADP-ribose moiety from NAD+ to specific amino acid residues on substrate proteins or to ADP-ribose itself. Currently, 22 human genes encoding proteins that possess an ADP-ribosyltransferase catalytic domain are known. Recent structural and enzymological evidence of poly(ADP-ribose)polymerase (PARP) family members demonstrate that earlier proposed names and classifications of these proteins are no longer accurate. Here we summarize these new findings and propose a new consensus nomenclature for all ADP-ribosyltransferases (ARTs) based on the catalyzed reaction and on structural features. A unified nomenclature would facilitate communication between researchers both inside and outside the ADP-ribosylation field.</p>}},
author = {{Hottiger, Michael O and Hassa, Paul O and Lüscher, Bernhard and Schüler, Herwig and Koch-Nolte, Friedrich}},
issn = {{0968-0004}},
keywords = {{ADP Ribose Transferases/chemistry; Animals; Catalytic Domain/genetics; Humans; Mammals/genetics; Poly(ADP-ribose) Polymerases/chemistry; Protein Processing, Post-Translational; Terminology as Topic}},
language = {{eng}},
number = {{4}},
pages = {{19--208}},
publisher = {{Elsevier}},
series = {{Trends in Biochemical Sciences}},
title = {{Toward a unified nomenclature for mammalian ADP-ribosyltransferases}},
url = {{http://dx.doi.org/10.1016/j.tibs.2009.12.003}},
doi = {{10.1016/j.tibs.2009.12.003}},
volume = {{35}},
year = {{2010}},
}