» Articles » PMID: 30481609

PARP Family Enzymes: Regulation and Catalysis of the Poly(ADP-ribose) Posttranslational Modification

Overview
Date 2018 Nov 28
PMID 30481609
Citations 95
Authors
Affiliations
Soon will be listed here.
Abstract

Poly(ADP-ribose) is a posttranslational modification and signaling molecule that regulates many aspects of human cell biology, and it is synthesized by enzymes known as poly(ADP-ribose) polymerases, or PARPs. A diverse collection of domain structures dictates the different cellular roles of PARP enzymes and regulates the production of poly(ADP-ribose). Here we primarily review recent structural insights into the regulation and catalysis of two family members: PARP-1 and Tankyrase. PARP-1 has multiple roles in the cellular response to DNA damage and the regulation of gene transcription, and Tankyrase regulates a diverse set of target proteins involved in cellular processes such as mitosis, genome integrity, and cell signaling. Both enzymes offer interesting modes of regulating the production and the target site selectivity of the poly(ADP-ribose) modification.

Citing Articles

Poly ADP-Ribosylation in a Plant Pathogenic Oomycete : A Key Controller of Growth and Host Plant Colonisation.

Samarskaya V, Koblova S, Suprunova T, Rogozhin E, Spechenkova N, Yakunina S J Fungi (Basel). 2025; 11(1).

PMID: 39852448 PMC: 11766942. DOI: 10.3390/jof11010029.


Subcellular NAD pools are interconnected and buffered by mitochondrial NAD.

Hoyland L, VanLinden M, Niere M, Stromland O, Sharma S, Dietze J Nat Metab. 2024; 6(12):2319-2337.

PMID: 39702414 DOI: 10.1038/s42255-024-01174-w.


Discovery of PARP1-Sparing Inhibitors for Protein ADP-Ribosylation.

Stephens E, Chen L, Ansari A, Shen K, Zhang L, Guillen S ACS Med Chem Lett. 2024; 15(11):1940-1946.

PMID: 39563804 PMC: 11571001. DOI: 10.1021/acsmedchemlett.4c00395.


An NAD with Dually Modified Adenine for Labeling ADP-Ribosylation-Specific Proteins.

Zhang L, Zhang X, Ansari A, Zhang Y Tetrahedron. 2024; 168.

PMID: 39553786 PMC: 11563119. DOI: 10.1016/j.tet.2024.134361.


Dispensability of HPF1 for cellular removal of DNA single-strand breaks.

Hrychova K, Burdova K, Polackova Z, Giamaki D, Valtorta B, Brazina J Nucleic Acids Res. 2024; 52(18):10986-10998.

PMID: 39162207 PMC: 11472159. DOI: 10.1093/nar/gkae708.


References
1.
Bae J, Donigian J, Hsueh A . Tankyrase 1 interacts with Mcl-1 proteins and inhibits their regulation of apoptosis. J Biol Chem. 2002; 278(7):5195-204. DOI: 10.1074/jbc.M201988200. View

2.
De Rycker M, Venkatesan R, Wei C, Price C . Vertebrate tankyrase domain structure and sterile alpha motif (SAM)-mediated multimerization. Biochem J. 2003; 372(Pt 1):87-96. PMC: 1223374. DOI: 10.1042/BJ20021450. View

3.
Pion E, Bombarda E, Stiegler P, Ullmann G, Mely Y, de Murcia G . Poly(ADP-ribose) polymerase-1 dimerizes at a 5' recessed DNA end in vitro: a fluorescence study. Biochemistry. 2003; 42(42):12409-17. DOI: 10.1021/bi0344432. View

4.
De Rycker M, Price C . Tankyrase polymerization is controlled by its sterile alpha motif and poly(ADP-ribose) polymerase domains. Mol Cell Biol. 2004; 24(22):9802-12. PMC: 525485. DOI: 10.1128/MCB.24.22.9802-9812.2004. View

5.
Bryant H, Schultz N, Thomas H, Parker K, Flower D, Lopez E . Specific killing of BRCA2-deficient tumours with inhibitors of poly(ADP-ribose) polymerase. Nature. 2005; 434(7035):913-7. DOI: 10.1038/nature03443. View