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YB-1 Phosphorylation at Serine 209 Inhibits Its Nuclear Translocation.

ABSTRACT: YB-1 is a multifunctional DNA- and RNA-binding protein involved in cell proliferation, differentiation, and migration. YB-1 is a predominantly cytoplasmic protein that is transported to the nucleus in certain conditions, including DNA-damaging stress, transcription inhibition, and viral infection. In tumors, YB-1 nuclear localization correlates with high aggressiveness, multidrug resistance, and a poor prognosis. It is known that posttranslational modifications can regulate the nuclear translocation of YB-1. In particular, well-studied phosphorylation at serine 102 (S102) activates YB-1 nuclear import. Here, we report that Akt kinase phosphorylates YB-1 in vitro at serine 209 (S209), which is located in the vicinity of the YB-1 nuclear localization signal. Using phosphomimetic substitutions, we showed that S209 phosphorylation inhibits YB-1 nuclear translocation and prevents p-S102-mediated YB-1 nuclear import.

SUBMITTER: Sogorina EM

PROVIDER: S-EPMC8745666 | biostudies-literature | 2021 Dec

REPOSITORIES: biostudies-literature

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YB-1 Phosphorylation at Serine 209 Inhibits Its Nuclear Translocation.

Sogorina Ekaterina M EM Kim Ekaterina R ER Sorokin Alexey V AV Lyabin Dmitry N DN Ovchinnikov Lev P LP Mordovkina Daria A DA Eliseeva Irina A IA

International journal of molecular sciences 20211231 1

YB-1 is a multifunctional DNA- and RNA-binding protein involved in cell proliferation, differentiation, and migration. YB-1 is a predominantly cytoplasmic protein that is transported to the nucleus in certain conditions, including DNA-damaging stress, transcription inhibition, and viral infection. In tumors, YB-1 nuclear localization correlates with high aggressiveness, multidrug resistance, and a poor prognosis. It is known that posttranslational modifications can regulate the nuclear transloca ...[more]

PMID: 35008856

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