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Regulation of poly(ADP-Ribose) polymerase 1 functions by post-translational modifications.

Author information

Affiliations

  • 1. Institute of Bioinformatics and Medical Engineering, Jiangsu University of Technology, Changzhou 213001, China.
      Authors
    • Piao L 1
    (1 author)
  • 2. Division of Molecular Modification and Cancer Biology, National Cancer Center Research Institute, 5-1-1 Tsukiji, Chuo-ku, Tokyo 104-0045 Japan.
      Authors
    • Fujioka K 2
    (1 author)
  • 3. Department of Bioengineering, School of Engineering, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8656 Japan.
      Authors
    • Nakakido M 3
    (1 author)
  • 4. Division of Molecular Modification and Cancer Biology, National Cancer Center Research Institute, 5-1-1 Tsukiji, Chuo-ku, Tokyo 104-0045 Japan,
      Authors
    • Hamamoto R 4
    (1 author)

ORCIDs linked to this article

Frontiers in Bioscience (Landmark Edition), 01 Jan 2018, 23(1):13-26
https://doi.org/10.2741/4578 PMID: 28930534 

Review

Abstract 

The poly(ADP-ribose) polymerases (PARPs) catalyze poly(ADP-ribosyl)ation, a post-translational modification of proteins. This  consists of the attachment of mono- or poly-adenosine diphosphate (ADP)-ribose units from nicotinamide adenine dinucleotide (NAD+) to specific polar residues of target proteins. PARP1 is the most abundant and best-characterized member of the family of PARP enzymes. PARP1 plays key roles in DNA repair, as well as a wide variety of cellular processes, including transcriptional regulation, chromatin modulation, cellular signaling pathway, inflammation, cellular stress responses and so on. Hence, PARP1 inhibitors have become a promising therapeutic approach for human diseases including cancer. Recent studies indicate that post-translational modifications (PTMs) such as phosphorylation, acetylation, and methylation are crucial for the regulation of PARP1 activity, and dysregulation of modifications on PARP1 is observed in human cancer. In this review, we describe the importance of PTMs to regulate the activity of PARP1, and the involvement of dysregulation of PTMs in human cancer.

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Read article at publisher's site: https://doi.org/10.2741/4578

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