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

被引：73
|
作者：
Kosova, A. A. [1 ]
Khodyreva, S. N. [1 ,2 ]
Lavrik, O. I. [1 ,2 ]
机构：
[1] Russian Acad Sci, Inst Chem Biol & Fundamental Med, Siberian Branch, Novosibirsk 630090, Russia
[2] Novosibirsk State Univ, Novosibirsk 630090, Russia
来源：
BIOCHEMISTRY-MOSCOW | 2017年 / 82卷 / 06期
基金：
俄罗斯科学基金会;
关键词：
GAPDH; glyceraldehyde-3-phosphate dehydrogenase; protein-DNA interactions; DNA repair; AP site; NUCLEAR TRANSLOCATION; APURINIC/APYRIMIDINIC SITES; PROTEIN COMPLEX; POLYMERASE-II; BINDING; APOPTOSIS; GLYCOSYLASE; RECOGNITION; INHIBITION; INTERACTS;
D O I：
10.1134/S0006297917060013
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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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页码：643 / 654
页数：12
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