Evidence map›Paper›PMID 26198631›Full record

ArticleThe Journal of biological chemistry2015

Regulation of Yin Yang 1 by Tyrosine Phosphorylation.

Gary Z Wang, Stephen P Goff

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Yin Yang 1: Function, Mechanisms, and Glia.Neurochemical research · 2025
    Review
  6. Review
  7. Article
  8. Article
  9. Dual Role of YY1 in HPV Life Cycle and Cervical Cancer Development.International journal of molecular sciences · 2022
    Review
  10. FBXO38 Ubiquitin Ligase Controls Centromere Integrity via ZXDA/B Stability.Frontiers in cell and developmental biology · 2022
    Article
  11. Aging · 2021
    Article
  12. Review
  13. Article
  14. Yin Yang 1 is a potent activator of human T lymphotropic virus type 1 LTR-driven gene expression via RNA binding.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  15. Article
  16. MicroRNA Let-7d-3p Contributes to Cardiac Protection via Targeting HMGA2.International journal of molecular sciences · 2019
    Article
  17. Article
  18. Article
  19. Article
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

2 authors at 2 institutions in 1 country.

Gary Z WangFrom the Integrated Program in Cellular, Molecular, and Biophysical Studies, Medical Scientist Training Program, Columbia University College of Physicians and Surgeons, New York, New York 10032.
Stephen P GoffDepartment of Biochemistry and Molecular Biophysics, Department of Microbiology and Immunology, and Howard Hughes Medical Institute, Columbia University, New York, New York 10032 and spg1@columbia.edu.
Columbia University · USHoward Hughes Medical Institute · US

Funding

Mechanisms of Silencing of Retroviral DNAs in Embryonic Cell LinesR01CA030488 · NCI · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI GOFF, STEPHEN PAINE · 1985 to 2024
$4.3M
NCI NIH HHS R01 CA030488NCI NIH HHS R01 CA30488
6 · The paper itself

Abstract

Yin Yang 1 (YY1) is a member of the GLI-Krüppel class of DNA and RNA binding transcription factors that can either activate or repress gene expression during cell growth, differentiation, and embryogenesis. Although much is known about YY1 interacting proteins and the target promoters regulated by YY1, much less is known about YY1 regulation through post-translational modifications. In this study we show that YY1 is tyrosine-phosphorylated in multiple cell types. Using a combination of pharmacological inhibition, kinase overexpression, and kinase knock-out studies, we demonstrate that YY1 is a target of multiple Src family kinases in vitro and in vivo. Moreover, we have identified multiple sites of YY1 phosphorylation and analyzed the effect of phosphorylation on the activity of YY1-responsive retroviral and cellular promoters. Phosphorylation of tyrosine 383 interferes with DNA and RNA binding, leading to the down-regulation of YY1 activity. Finally, we provide the first evidence that YY1 is a downstream target of epidermal growth factor receptor signaling in vivo. Taken together, the identification of YY1 as a target of Src family kinases provide key insights into the inhibitory role of tyrosine kinases in modulating YY1 activity.

Indexed as

AnimalsBinding SitesBlotting, WesternCell LineCell Line, TumorEpidermal Growth FactorGene ExpressionHEK293 CellsHeLa CellsHumansImatinib MesylateIndolesJurkat CellsMutationPhosphorylationPromoter Regions, GeneticEpidermal Growth FactorImatinib MesylateIndolesProtein Kinase InhibitorsProto-Oncogene Proteins c-fossrc-Family KinasesSU 6656SulfonamidesTyrosineYY1 Transcription Factorgene regulationphosphotyrosineprotein phosphorylationretrovirusSrctranscription factor

Identifiers

PMID26198631
PMCPMC4571944
OpenAlexW2139644466

What OpenQuestion holds

Textmetadata
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.