Publications by authors named "Ilya A Buldakov"

2 Publications

  • Page 1 of 1

Transportin-1-dependent YB-1 nuclear import.

Biochem Biophys Res Commun 2016 Nov 26;480(4):629-634. Epub 2016 Oct 26.

Institute of Protein Research, Russian Academy of Sciences, 4 Institutskaya St., 142290, Pushchino, Moscow Region, Russia. Electronic address:

The DNA/RNA-binding protein YB-1 (Y-box binding protein 1) performs multiple functions both in the cytoplasm and the nucleus of the cell. Generally localized to the cytoplasm, under certain conditions YB-1 is translocated to the nucleus. Here we report for the first time a transport factor that mediates YB-1 nuclear import - transportin-1. The YB-1/transportin-1 complex can be isolated from HeLa cell extract. Nuclear import of YB-1 and its truncated form YB-1 (1-219) in in vitro transport assay was diminished in the presence of a competitor substrate and ceased in the presence of transportin-1 inhibitor M9M. Inhibitors of importin β1 had no effect on YB-1 transport. Furthermore, transport of YB-1 (P201A/Y202A) and YB-1 (1-219) (P201A/Y202A) bearing inactivating mutations in the transportin-1-dependent nuclear localization signal was practically abolished. Together, these results indicate that transportin-1 mediates YB-1 nuclear translocation.
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http://dx.doi.org/10.1016/j.bbrc.2016.10.107DOI Listing
November 2016

The proteolytic YB-1 fragment interacts with DNA repair machinery and enhances survival during DNA damaging stress.

Cell Cycle 2013 Dec 7;12(24):3791-803. Epub 2013 Oct 7.

Institute of Protein Research; Russian Academy of Sciences; Pushchino, Moscow Region, Russian Federation.

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.
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http://dx.doi.org/10.4161/cc.26670DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3905071PMC
December 2013