Protein kinase CK2 in DNA damage and repair

被引:31
作者
Montenarh, Mathias [1 ]
机构
[1] Univ Saarland, Med Biochem & Mol Biol, Bldg 44, D-66424 Homburg, Germany
关键词
Protein kinase; DNA repair; DNA damage; cell cycle; phosphorylation; protein-protein interactions; BASE EXCISION-REPAIR; STRAND BREAK REPAIR; CATALYZES TYROSINE PHOSPHORYLATION; TUMOR-SUPPRESSOR PROTEIN; CANCER CELL-LINES; WILD-TYPE; LIGASE-I; MRE11-RAD50-NBS1; COMPLEX; IONIZING-RADIATION; CHECKPOINT COMPLEX;
D O I
10.3978/j.issn.2218-676X.2016.01.09
中图分类号
R73 [肿瘤学];
学科分类号
100214 ;
摘要
Protein kinase CK2, formerly known as casein kinase 2, is a ubiquitously expressed serine/threonine kinase, which is absolutely required for cell viability of eukaryotic cells. The kinase occurs predominantly as a tetrameric holoenzyme composed of two regulatory a or alpha' subunits and two non-catalytic beta subunits. It is highly expressed and highly active in many tumour cells. The proliferation promoting as well as the anti-apoptotic functions have made CK2 an interesting target for cancer therapy. It phosphorylates numerous substrates in eukaryotic cells thereby regulating a variety of different cellular processes or signalling pathways. Here, I describe the role of CK2 in DNA damage recognition followed by cell cycle regulation and DNA repair. It turns out that CK2 phosphorylates a number of different proteins thereby regulating their enzymatic activity or platform proteins which are required for recruiting proteins for DNA repair. In addition, the individual subunits bind to various proteins, which may help to target the kinase to places of DNA damage and repair. Recently developed pharmacological inhibitors of the kinase activity are potent regulators of the CK2 activity in DNA repair processes. Since DNA damaging agents are used in cancer therapy the knowledge of CK2 functions in DNA repair as well as the use of specific inhibitors of CK2 may improve cancer treatment in the future.
引用
收藏
页码:49 / 63
页数:15
相关论文
共 117 条
[1]   Rad52 SUMOylation affects the efficiency of the DNA repair [J].
Altmannova, Veronika ;
Eckert-Boulet, Nadine ;
Arneric, Milica ;
Kolesar, Peter ;
Chaloupkova, Radka ;
Damborsky, Jiri ;
Sung, Patrick ;
Zhao, Xiaolan ;
Lisby, Michael ;
Krejci, Lumir .
NUCLEIC ACIDS RESEARCH, 2010, 38 (14) :4708-4721
[2]   Centrosome protein centrin 2/caltractin 1 is part of the xeroderma pigmentosum group C complex that initiates global genome nucleotide excision repair [J].
Araki, M ;
Masutani, C ;
Takemura, M ;
Uchida, A ;
Sugasawa, K ;
Kondoh, J ;
Ohkuma, Y ;
Hanaoka, F .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (22) :18665-18672
[3]   HP1-β mobilization promotes chromatin changes that initiate the DNA damage response [J].
Ayoub, Nabieh ;
Jeyasekharan, Anand D. ;
Bernal, Juan A. ;
Venkitaraman, Ashok R. .
NATURE, 2008, 453 (7195) :682-U14
[4]   JWA regulates melanoma metastasis by integrin αVβ3 signaling [J].
Bai, J. ;
Zhang, J. ;
Wu, J. ;
Shen, L. ;
Zeng, J. ;
Ding, J. ;
Wu, Y. ;
Gong, Z. ;
Li, A. ;
Xu, S. ;
Zhou, J. ;
Li, G. .
ONCOGENE, 2010, 29 (08) :1227-1237
[5]   Heat shock protein 70 enhanced deoxyribonucleic acid base excision repair in human leukemic cells after ionizing radiation [J].
Bases, Robert .
CELL STRESS & CHAPERONES, 2006, 11 (03) :240-249
[6]   Tyrosine phosphorylation of histone H2A by CK2 regulates transcriptional elongation [J].
Basnet, Harihar ;
Su, Xue B. ;
Tan, Yuliang ;
Meisenhelders, Jill ;
Merkurjev, Dana ;
Ohgi, Kenneth A. ;
Hunters, Tony ;
Pillus, Lorraine ;
Rosenfeld, Michael G. .
NATURE, 2014, 516 (7530) :267-+
[7]   Structural bases of protein kinase CK2 inhibition [J].
Battistutta, R. .
CELLULAR AND MOLECULAR LIFE SCIENCES, 2009, 66 (11-12) :1868-1889
[8]   CK2 phosphorylation-dependent interaction between aprataxin and MDC1 in the DNA damage response [J].
Becherel, Olivier J. ;
Jakob, Burkhard ;
Cherry, Amy L. ;
Gueven, Nuri ;
Fusser, Markus ;
Kijas, Amanda W. ;
Peng, Cheng ;
Katyal, Sachin ;
McKinnon, Peter J. ;
Chen, Junjie ;
Epe, Bernd ;
Smerdon, Stephen J. ;
Taucher-Scholz, Gisela ;
Lavin, Martin F. .
NUCLEIC ACIDS RESEARCH, 2010, 38 (05) :1489-1503
[9]   Loading of the human 9-1-1 checkpoint complex onto DNA by the checkpoint clamp loader hRad17-replication factor C complex in vitro [J].
Bermudez, VP ;
Lindsey-Boltz, LA ;
Cesare, AJ ;
Maniwa, Y ;
Griffith, JD ;
Hurwitz, J ;
Sancar, A .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2003, 100 (04) :1633-1638
[10]   Increased sensitivity to UV radiation in mice with a p53 point mutation at Ser389 [J].
Bruins, W ;
Zwart, E ;
Attardi, LD ;
Iwakuma, T ;
Hoogervorst, EM ;
Beems, RB ;
Miranda, B ;
van Oostrom, CTM ;
van den Berg, J ;
van den Aardweg, GJ ;
Lozano, G ;
van Steeg, H ;
Jacks, T ;
de Vries, A .
MOLECULAR AND CELLULAR BIOLOGY, 2004, 24 (20) :8884-8894