YB-1 Phosphorylation at Serine 209 Inhibits Its Nuclear Translocation
| Autor: | Ekaterina M. Sogorina, Ekaterina R. Kim, Alexey V. Sorokin, Dmitry N. Lyabin, Lev P. Ovchinnikov, Daria A. Mordovkina, Irina A. Eliseeva |
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| Rok vydání: | 2021 |
| Předmět: |
Serum
QH301-705.5 YB-1 Akt nuclear transport S102 S209 phosphorylation Catalysis Article Inorganic Chemistry Mice Phosphoserine Animals Humans Amino Acid Sequence Biology (General) Physical and Theoretical Chemistry QD1-999 Molecular Biology Spectroscopy Cell Nucleus Organic Chemistry General Medicine Computer Science Applications Chemistry Protein Transport NIH 3T3 Cells RNA Y-Box-Binding Protein 1 Proto-Oncogene Proteins c-akt HeLa Cells Protein Binding |
| Zdroj: | International Journal of Molecular Sciences International Journal of Molecular Sciences; Volume 23; Issue 1; Pages: 428 International Journal of Molecular Sciences, Vol 23, Iss 428, p 428 (2022) |
| ISSN: | 1422-0067 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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