PARPs transfer ADP-D-ribose to proteins (poly(ADP-ribosyl)ation)

Stable Identifier
R-HSA-8938073
Type
Reaction [transition]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
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Poly (ADP-ribose) polymerases (PARPs) catalyse the poly(ADP-ribosyl)ation posttranslational modification of proteins. At least 18 human members share homology with the catalytic domain of the founding member, PARP1. PARPs cleave the glycosidic bond of NAD+ between nicotinamide (NAM) and ribose followed by the covalent modification of mainly glutamate residues on acceptor proteins with an ADP-ribosyl unit, with subsequent ADP-ribosyl unit additions linked by glycosidic ribose-ribose bonds. NAM can be utilised in the NAD+ regeneration process. Poly(ADP-ribosyl)ation is important in many biological processess including DNA repair, regulation of chromosome structure, transcriptional regulation, mitosis and apoptosis. PARPs can localise to either the cytosol or the nucleus. The cytosolic PARPs described here are PARP9, PARP10 and PARP16 (Yan et al. 2013, Yu et al. 2005, Di Paolo et al. 2012). PARP4, PARP6, PARP8 and PARP14 may also be located in the cytosol with the same functionality.
Literature References
PubMed ID Title Journal Year
15674325 PARP-10, a novel Myc-interacting protein with poly(ADP-ribose) polymerase activity, inhibits transformation

Austen, M, Cerni, C, Grötzinger, J, Yu, M, Walsemann, G, Mehraein, Y, Lesniewicz, K, Lüscher-Firzlaff, J, Schamberger, C, Vervoorts, J, Schreek, S, Kremmer, E, Kraft, R, Lüscher, B, Mertsching, J, Poreba, E

Oncogene 2005
22701565 PARP16/ARTD15 is a novel endoplasmic-reticulum-associated mono-ADP-ribosyltransferase that interacts with, and modifies karyopherin-ß1

Di Tullio, G, Buccione, R, Micaroni, M, Di Girolamo, M, Di Paola, S

PLoS ONE 2012
23230272 BAL1 and its partner E3 ligase, BBAP, link Poly(ADP-ribose) activation, ubiquitylation, and double-strand DNA repair independent of ATM, MDC1, and RNF8

Manis, J, Yan, Q, Wang, Z, Shipp, MA, Xu, R, Zhu, L, Cheng, X

Mol. Cell. Biol. 2013
Participants
Participates
Catalyst Activity

NAD+ ADP-ribosyltransferase activity of PARPs [cytosol]

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