Abstract
The genome stability of higher eukaryotes depends largely on the functioning of the DNA repair systems. In turn, the precise regulation of each step of repair processes is necessary for the efficient DNA repair. Although most pathways of DNA repair have already been established, their regulation mechanisms require further investigation. Poly(ADP-ribose) polymerases (PARPs) are widely considered to be potential regulators of DNA repair. The role of the most prominent member of this protein family, i.e., PARP1, in DNA repair has been being intensively studied, while the literature data on participation in the repair processes of PARP2, the closest PARP1 homolog, are poorly summarized, although a great body of information concerning its participation in DNA repair has been accumulated. Using the PARP2-deficient model organisms and cell lines, their increased sensitivity to several DNA damaging agents was elucidated. The accumulation of PARP2 at the DNA damage sites in cells was shown. There are data that demonstrate the proteinprotein interaction of PARP2 with several proteins of the base excision repair/single-strand break repair and nonhomologous end joining. Most of the data on the PARP2 role were obtained in experiments with model organisms and cell lines; thus, it is difficult to elucidate the influence of PARP2 on specific processes in vivo. In this review, we tried to summarize data on the participation of PARP2 in the DNA repair processes, including our recent results.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.