Evidence map›Paper›PMID 35008856›Full record

ArticleInternational journal of molecular sciences2021

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

Ekaterina M Sogorina, Ekaterina R Kim, Alexey V Sorokin, Dmitry N Lyabin, Lev P Ovchinnikov, Daria A Mordovkina, Irina A Eliseeva

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.2field-weighted citation impact, top 21% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

15 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Y-box binding proteins in immunity and RNA virus infection.Microbiology and molecular biology reviews : MMBR · 2025
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. YB1 and its role in osteosarcoma: a review.Frontiers in oncology · 2024
    Review
  12. Article
  13. Article
  14. Article
  15. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 1 institution in 2 countries.

Ekaterina M SogorinaGroup of Protein Biosynthesis Regulation, Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia.
Ekaterina R KimGroup of Protein Biosynthesis Regulation, Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia.
Alexey V SorokinGroup of Protein Biosynthesis Regulation, Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia.
Dmitry N LyabinGroup of Protein Biosynthesis Regulation, Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia.
Lev P OvchinnikovGroup of Protein Biosynthesis Regulation, Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia.
Daria A MordovkinaGroup of Protein Biosynthesis Regulation, Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia.
Irina A EliseevaGroup of Protein Biosynthesis Regulation, Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia.
Institute of Protein Research · RU

Funding

Russian Science Foundation 19-74-20129
6 · The paper itself

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.

Indexed as

Amino Acid SequenceAnimalsCell NucleusHeLa CellsHumansMiceNIH 3T3 CellsPhosphorylationPhosphoserineProtein BindingProtein TransportProto-Oncogene Proteins c-aktRNASerumY-Box-Binding Protein 1PhosphoserineProto-Oncogene Proteins c-aktRNAY-Box-Binding Protein 1Aktnuclear transportphosphorylationS102S209YB-1

Identifiers

PMID35008856
PMCPMC8745666
OpenAlexW4205954141

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.