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Proteasome‐mediated cleavage of the Y‐box‐binding protein 1 is linked to DNA‐damage stress response
Author(s) -
Sorokin Alexey V,
Selyutina Anastasia A,
Skabkin Maxim A,
Guryanov Sergey G,
Nazimov Igor V,
Richard Christina,
Th'ng John,
Yau Jonathan,
Sorensen Poul HB,
Ovchinnikov Lev P,
Evdokimova Valentina
Publication year - 2005
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1038/sj.emboj.7600830
Subject(s) - thunder , russian federation , bay , biological sciences , library science , geography , biology , archaeology , microbiology and biotechnology , regional science , meteorology , computer science
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. Distribution of YB‐1 between the nucleus and the cytoplasm is known to be dependent on nuclear targeting and cytoplasmic retention signals located within the C‐terminal portion of YB‐1. Here, we report that YB‐1 undergoes a specific proteolytic cleavage by the 20S proteasome, which splits off the C‐terminal 105‐amino‐acid‐long YB‐1 fragment containing a cytoplasmic retention signal. Cleavage of YB‐1 by the 20S proteasome in vitro appears to be ubiquitin‐ and ATP‐independent, and is abolished by the association of YB‐1 with messenger RNA. We also found that genotoxic stress triggers a proteasome‐mediated cleavage of YB‐1 in vivo and leads to accumulation of the truncated protein in nuclei of stressed cells. Endoproteolytic activity of the proteasome may therefore play an important role in regulating YB‐1 functioning, especially under certain stress conditions.