Результаты исследований: Научные публикации в периодических изданиях › обзорная статья › Рецензирование
Role of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) in DNA repair. / Kosova, A. A.; Khodyreva, S. N.; Lavrik, O. I.
в: Biochemistry (Moscow), Том 82, № 6, 01.06.2017, стр. 643-654.Результаты исследований: Научные публикации в периодических изданиях › обзорная статья › Рецензирование
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TY - JOUR
T1 - Role of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) in DNA repair
AU - Kosova, A. A.
AU - Khodyreva, S. N.
AU - Lavrik, O. I.
PY - 2017/6/1
Y1 - 2017/6/1
N2 - 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.
AB - 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.
KW - AP site
KW - DNA repair
KW - GAPDH
KW - glyceraldehyde-3-phosphate dehydrogenase
KW - protein–DNA interactions
UR - http://www.scopus.com/inward/record.url?scp=85020699564&partnerID=8YFLogxK
U2 - 10.1134/S0006297917060013
DO - 10.1134/S0006297917060013
M3 - Review article
C2 - 28601074
AN - SCOPUS:85020699564
VL - 82
SP - 643
EP - 654
JO - Biochemistry (Moscow)
JF - Biochemistry (Moscow)
SN - 0006-2979
IS - 6
ER -
ID: 8680969