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

Dmitry Kretov (1, 2) , Daria Mordovkina (1) , Irina Eliseeva (1) , Dmitry Lyabin (1) , Dmitry Polyakov (1) , Vandana Joshi (2) , Bénédicte Desforges (2) , Loic Hamon (2) , Olga Lavrik (3) , David Pastre (2) , Patrick A. Curmi (2) , Lev Ovchinnikov (1)

1 Institute of Protein Research, Russian Academy of Sciences, Pushchino
2 SABNP - Structure et activité des biomolécules normales et pathologiques
3 ICBFM SB RAS - Institute of Chemical Biology and Fundamental Medicine [Novosibirsk, Russia]

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.

Keywords: YB‐1; nuclear translocation; inhibition of transcription; phosphorylation; YB-1

Domains: Life Sciences [q-bio]

Dmitry Kretov, Daria Mordovkina, Irina Eliseeva, Dmitry Lyabin, Dmitry Polyakov, et al.. Inhibition of Transcription Induces Phosphorylation of YB-1 at Ser102 and Its Accumulation in the Nucleus. Cells, 2020, 9 (1), pp.104. ⟨10.3390/cells9010104⟩. ⟨hal-02968925⟩