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

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

Stable Identifier

R-HSA-8938073

Type

Reaction [transition]

Species

Homo sapiens

Compartment

cytosol

ReviewStatus

5/5

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

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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