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Inhibition of Transcription Induces Phosphorylation of YB-1 at Ser102 and Its Accumulation in the Nucleus

The Y-box binding protein 1 (YB-1) is an RNA/DNA-binding protein regulating gene expression in the cytoplasm and the nucleus. Although mostly cytoplasmic, YB-1 accumulates in the nucleus under stress conditions. Its nuclear localization is associated with aggressiveness and multidrug resistance of c...

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Published in:Cells (Basel, Switzerland) Switzerland), 2019-12, Vol.9 (1), p.104
Main Authors: Kretov, Dmitry A, Mordovkina, Daria A, Eliseeva, Irina A, Lyabin, Dmitry N, Polyakov, Dmitry N, Joshi, Vandana, Desforges, Bénédicte, Hamon, Loic, Lavrik, Olga I, Pastré, David, Curmi, Patrick A, Ovchinnikov, Lev P
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Language:English
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Summary:The Y-box binding protein 1 (YB-1) is an RNA/DNA-binding protein regulating gene expression in the cytoplasm and the nucleus. Although mostly cytoplasmic, YB-1 accumulates in the nucleus under stress conditions. Its nuclear localization is associated with aggressiveness and multidrug resistance of cancer cells, which makes the understanding of the regulatory mechanisms of YB-1 subcellular distribution essential. Here, we report that inhibition of RNA polymerase II (RNAPII) activity results in the nuclear accumulation of YB-1 accompanied by its phosphorylation at Ser102. The inhibition of kinase activity reduces YB-1 phosphorylation and its accumulation in the nucleus. The presence of RNA in the nucleus is shown to be required for the nuclear retention of YB-1. Thus, the subcellular localization of YB-1 depends on its post-translational modifications (PTMs) and intracellular RNA distribution.
ISSN:2073-4409
2073-4409
DOI:10.3390/cells9010104