YB-1 Phosphorylation at Serine 209 Inhibits Its Nuclear Translocation
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. I...
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| Format: | Article |
| Language: | English |
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MDPI AG
2021-12-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/23/1/428 |
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| author | Ekaterina M. Sogorina Ekaterina R. Kim Alexey V. Sorokin Dmitry N. Lyabin Lev P. Ovchinnikov Daria A. Mordovkina Irina A. Eliseeva |
| author_facet | Ekaterina M. Sogorina Ekaterina R. Kim Alexey V. Sorokin Dmitry N. Lyabin Lev P. Ovchinnikov Daria A. Mordovkina Irina A. Eliseeva |
| author_sort | Ekaterina M. Sogorina |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-03-10T03:37:55Z |
| format | Article |
| id | doaj.art-b58d6b59131b4edb82b4b60caed085a2 |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-10T03:37:55Z |
| publishDate | 2021-12-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-b58d6b59131b4edb82b4b60caed085a22023-11-23T11:39:54ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672021-12-0123142810.3390/ijms23010428YB-1 Phosphorylation at Serine 209 Inhibits Its Nuclear TranslocationEkaterina M. Sogorina0Ekaterina R. Kim1Alexey V. Sorokin2Dmitry N. Lyabin3Lev P. Ovchinnikov4Daria A. Mordovkina5Irina A. Eliseeva6Group of Protein Biosynthesis Regulation, Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, RussiaGroup of Protein Biosynthesis Regulation, Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, RussiaGroup of Protein Biosynthesis Regulation, Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, RussiaGroup of Protein Biosynthesis Regulation, Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, RussiaGroup of Protein Biosynthesis Regulation, Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, RussiaGroup of Protein Biosynthesis Regulation, Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, RussiaGroup of Protein Biosynthesis Regulation, Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, RussiaYB-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.https://www.mdpi.com/1422-0067/23/1/428YB-1Aktnuclear transportS102S209phosphorylation |
| spellingShingle | Ekaterina M. Sogorina Ekaterina R. Kim Alexey V. Sorokin Dmitry N. Lyabin Lev P. Ovchinnikov Daria A. Mordovkina Irina A. Eliseeva YB-1 Phosphorylation at Serine 209 Inhibits Its Nuclear Translocation International Journal of Molecular Sciences YB-1 Akt nuclear transport S102 S209 phosphorylation |
| title | YB-1 Phosphorylation at Serine 209 Inhibits Its Nuclear Translocation |
| title_full | YB-1 Phosphorylation at Serine 209 Inhibits Its Nuclear Translocation |
| title_fullStr | YB-1 Phosphorylation at Serine 209 Inhibits Its Nuclear Translocation |
| title_full_unstemmed | YB-1 Phosphorylation at Serine 209 Inhibits Its Nuclear Translocation |
| title_short | YB-1 Phosphorylation at Serine 209 Inhibits Its Nuclear Translocation |
| title_sort | yb 1 phosphorylation at serine 209 inhibits its nuclear translocation |
| topic | YB-1 Akt nuclear transport S102 S209 phosphorylation |
| url | https://www.mdpi.com/1422-0067/23/1/428 |
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