YB-1 Phosphorylation at Serine 209 Inhibits Its Nuclear Translocation

International Journal of Molecular Sciences

Alexey V. Sorokin¹  Ekaterina R. Kim¹  Ekaterina M. Sogorina¹  Lev P. Ovchinnikov¹  Daria A. Mordovkina¹  Dmitry N. Lyabin¹  Irina A. Eliseeva¹ 

[1] Group of Protein Biosynthesis Regulation, Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia;

关键词: YB-1;    Akt;    nuclear transport;    S102;    S209;    phosphorylation;   

DOI  :  10.3390/ijms23010428

来源: DOAJ

【 摘 要 】

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.

【 授权许可】

Unknown