Functions of ADP-ribose transferases in the maintenance of telomere integrity

被引:0
作者
Daniela Muoio
Natalie Laspata
Elise Fouquerel
机构
[1] Hillman Cancer Center,UPMC Cancer Institute and Department of Pharmacology and Chemical Biology at the University of Pittsburgh
[2] Thomas Jefferson University,Department of Biochemistry and Molecular Biology
来源
Cellular and Molecular Life Sciences | 2022年 / 79卷
关键词
ART; PARP; Telomeres; Genome stability;
D O I
暂无
中图分类号
学科分类号
摘要
The ADP-ribose transferase (ART) family comprises 17 enzymes that catalyze mono- or poly-ADP-ribosylation, a post-translational modification of proteins. Present in all subcellular compartments, ARTs are implicated in a growing number of biological processes including DNA repair, replication, transcription regulation, intra- and extra-cellular signaling, viral infection and cell death. Five members of the family, PARP1, PARP2, PARP3, tankyrase 1 and tankyrase 2 are mainly described for their crucial functions in the maintenance of genome stability. It is well established that the most describedrole of PARP1, 2 and 3 is the repair of DNA lesions while tankyrases 1 and 2 are crucial for maintaining the integrity of telomeres. Telomeres, nucleoprotein complexes located at the ends of eukaryotic chromosomes, utilize their unique structure and associated set of proteins to orchestrate the mechanisms necessary for their own protection and replication. While the functions of tankyrases 1 and 2 at telomeres are well known, several studies have also brought PARP1, 2 and 3 to the forefront of telomere protection. The singular quality of the telomeric environment has highlighted protein interactions and molecular pathways distinct from those described throughout the genome. The aim of this review is to provide an overview of the current knowledge on the multiple roles of PARP1, PARP2, PARP3, tankyrase 1 and tankyrase 2 in the maintenance and preservation of telomere integrity.
引用
收藏
相关论文
共 50 条
  • [21] Poly(ADP-ribose) metabolism in human parasitic protozoa
    Fernandez Villamil, Silvia H.
    Vilchez Larrea, Salome C.
    ACTA TROPICA, 2020, 208
  • [22] Poly(ADP-ribose)polymerase inhibition decreases angiogenesis
    Rajesh, Mohanraj
    Mukhopadhyay, Partha
    Godlewski, Grzegorz
    Batkai, Sandor
    Hasko, Gyorgy
    Liaudet, Lucas
    Pacher, Pal
    BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2006, 350 (04) : 1056 - 1062
  • [23] The rise and fall of poly(ADP-ribose): An enzymatic perspective
    Pascal, John M.
    Ellenberger, Tom
    DNA REPAIR, 2015, 32 : 10 - 16
  • [24] Poly(ADP-ribose) polymerase localizes to the centrosomes and chromosomes
    Kanai, M
    Uchida, M
    Hanai, S
    Uematsu, N
    Uchida, K
    Miwa, M
    BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2000, 278 (02) : 385 - 389
  • [25] Molecular Insights into Poly(ADP-ribose) Recognition and Processing
    Zaja, Roko
    Mikoc, Andreja
    Barkauskaite, Eva
    Ahel, Ivan
    BIOMOLECULES, 2013, 3 (01): : 1 - 17
  • [26] Poly (ADP-ribose) Polymerase Inhibitors in Cancer Treatment
    Mason, Kathryn A.
    Raju, Uma
    Buchholz, Thomas A.
    Wang, Li
    Milas, Zvonimir L.
    Milas, Luka
    AMERICAN JOURNAL OF CLINICAL ONCOLOGY-CANCER CLINICAL TRIALS, 2014, 37 (01): : 90 - 100
  • [27] Poly(ADP-ribose) polymerase inhibition in pancreatic cancer
    Singh, Hans Martin
    Bailey, Peter
    Huebschmann, Daniel
    Berger, Anne Katrin
    Neoptolemos, John P.
    Jaeger, Dirk
    Siveke, Jens
    Springfeld, Christoph
    GENES CHROMOSOMES & CANCER, 2021, 60 (05) : 373 - 384
  • [28] Poly(ADP-ribose)polymerase inhibition - Where now?
    Woon, ECY
    Threadgill, MD
    CURRENT MEDICINAL CHEMISTRY, 2005, 12 (20) : 2373 - 2392
  • [29] EXPRESSION OF POLY(ADP-RIBOSE) POLYMERASE IN BONE REGENERATION
    Lo Muzio, L.
    Pannone, G.
    Santarelli, A.
    Lo Russo, L.
    De Lillo, A.
    Rubini, C.
    Bambini, F.
    Bufo, P.
    Dioguardi, M.
    Procaccini, M.
    JOURNAL OF BIOLOGICAL REGULATORS AND HOMEOSTATIC AGENTS, 2014, 28 (04) : 801 - 807
  • [30] New route for the activation of poly(ADP-ribose) polymerase-1: a passage that links poly(ADP-ribose) polymerase-1 to lipotoxicity?
    Bai, Peter
    Csoka, Balazs
    BIOCHEMICAL JOURNAL, 2015, 469 : E9 - E11