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• W1985756098 abstract "The Y-box binding protein 1 (YB-1) is a DNA/RNA-binding nucleocytoplasmic shuttling protein whose regulatory effect on many DNA and RNA-dependent events is determined by its localization in the cell. We have shown previously that YB-1 is cleaved by 20S proteasome between E219 and G220, and the truncated N-terminal YB-1 fragment accumulates in the nuclei of cells treated with DNA damaging drugs. We proposed that appearance of truncated YB-1 in the nucleus may predict multiple drug resistance. Here, we compared functional activities of the full-length and truncated YB-1 proteins and showed that the truncated form was more efficient in protecting cells against doxorubicin treatment. Both forms of YB-1 induced changes in expression of various genes without affecting those responsible for drug resistance. Interestingly, although YB-1 cleavage did not significantly affect its DNA binding properties, truncated YB-1 was detected in complexes with Mre11 and Rad50 under genotoxic stress conditions. We conclude that both full-length and truncated YB-1 are capable of protecting cells against DNA damaging agents, and the truncated form may have an additional function in DNA repair." @default.
• W1985756098 created "2016-06-24" @default.
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• W1985756098 date "2013-12-15" @default.
• W1985756098 modified "2023-10-01" @default.
• W1985756098 title "The proteolytic YB-1 fragment interacts with DNA repair machinery and enhances survival during DNA damaging stress" @default.
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• W1985756098 doi "https://doi.org/10.4161/cc.26670" @default.
• W1985756098 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3905071" @default.
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