4.6 Review

The XPA Protein-Life under Precise Control

Journal

CELLS
Volume 11, Issue 23, Pages -

Publisher

MDPI
DOI: 10.3390/cells11233723

Keywords

XPA; nucleotide excision repair (NER); DNA repair; post-translational modifications; PARP1; PARylation; ATR; phosphorylation

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This review summarizes the structure of the XPA protein and its interactions with other proteins during nucleotide excision repair, as well as the regulation of XPA protein activity and expression and the network of post-translational modifications. It also discusses data that does not align with the current hypothesis about the functioning of the XPA protein.
Nucleotide excision repair (NER) is a central DNA repair pathway responsible for removing a wide variety of DNA-distorting lesions from the genome. The highly choreographed cascade of core NER reactions requires more than 30 polypeptides. The xeroderma pigmentosum group A (XPA) protein plays an essential role in the NER process. XPA interacts with almost all NER participants and organizes the correct NER repair complex. In the absence of XPA's scaffolding function, no repair process occurs. In this review, we briefly summarize our current knowledge about the XPA protein structure and analyze the formation of contact with its protein partners during NER complex assembling. We focus on different ways of regulation of the XPA protein's activity and expression and pay special attention to the network of post-translational modifications. We also discuss the data that is not in line with the currently accepted hypothesis about the functioning of the XPA protein.

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