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Role of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) in DNA repair

Authors
  • Kosova, A. A.1
  • Khodyreva, S. N.1, 2
  • Lavrik, O. I.1, 2
  • 1 Siberian Branch of the Russian Academy of Sciences, Institute of Chemical Biology and Fundamental Medicine, Novosibirsk, 630090, Russia , Novosibirsk (Russia)
  • 2 Novosibirsk State University, Novosibirsk, 630090, Russia , Novosibirsk (Russia)
Type
Published Article
Journal
Biochemistry (Moscow)
Publisher
Pleiades Publishing
Publication Date
Jun 15, 2017
Volume
82
Issue
6
Pages
643–654
Identifiers
DOI: 10.1134/S0006297917060013
Source
Springer Nature
Keywords
License
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Abstract

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is widely known as a glycolytic enzyme. Nevertheless, various functions of GAPDH have been found that are unrelated to glycolysis. Some of these functions presume interaction of GAPDH with DNA, but the mechanism of its translocation to the nucleus is not fully understood. When in the nucleus, GAPDH participates in the initiation of apoptosis and transcription of genes involved in antiapoptotic pathways and cell proliferation and plays a role in the regulation of telomere length. Several authors have shown that GAPDH displays the uracil-DNA glycosylase activity and interacts with some types of DNA damages, such as apurinic/apyrimidinic sites, nucleotide analogs, and covalent DNA adducts with alkylating agents. Moreover, GAPDH can interact with proteins participating in DNA repair, such as APE1, PARP1, HMGB1, and HMGB2. In this review, the functions of GAPDH associated with DNA repair are discussed in detail.

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