Evidence map›Paper›PMID 19221599›Full record

ArticlePloS one2009

Post-translational regulation of Oct4 transcriptional activity.

Jonathan P Saxe, Alexey Tomilin, Hans R Schöler, Kathrin Plath, Jing Huang

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
6.3field-weighted citation impact, top 3% 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

66 citing papers in PubMed, 125 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Role of OCT4 in cancer stem-like cells and chemotherapy resistance.Biochimica et biophysica acta. Molecular basis of disease · 2020
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. Article

6 more citing papers are in PubMed but not listed here.

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

5 authors at 3 institutions in 3 countries.

Jonathan P SaxeDepartment of Molecular and Medical Pharmacology, David Geffen School of Medicine, University of California Los Angeles, Los Angeles, California, United States of America. jonathan.saxe@yale.edu
Alexey Tomilin
Hans R Schöler
Kathrin Plath
Jing Huang
University of California, Los Angeles · USInstitute of Cytology · RUMax Planck Institute for Molecular Biomedicine · DE

Funding

Exploiting TOR Signaling for Cancer Drug DiscoveryR01CA124974 · NCI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI HUANG, JING · 2007 to 2011
$1.5M
A Mixed-Bait-Strategy for Protein Interactome MappingR21HG003729 · NHGRI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI HUANG, JING · 2006 to 2007
$280k
NCI NIH HHS R01 CA124974NHGRI NIH HHS R21 HG003729
6 · The paper itself

Abstract

Oct4 is a key component of the molecular circuitry which regulates embryonic stem cell proliferation and differentiation. It is essential for maintenance of undifferentiated, pluripotent cell populations, and accomplishes these tasks by binding DNA in multiple heterodimer and homodimer configurations. Very little is known about how formation of these complexes is regulated, or the mechanisms through which Oct4 proteins respond to complex extracellular stimuli which regulate pluripotency. Here, we provide evidence for a phosphorylation-based mechanism which regulates specific Oct4 homodimer conformations. Point mutations of a putative phosphorylation site can specifically abrogate transcriptional activity of a specific homodimer assembly, with little effect on other configurations. Moreover, we performed bioinformatic predictions to identify a subset of Oct4 target genes which may be regulated by this specific assembly, and show that altering Oct4 protein levels affects transcription of Oct4 target genes which are regulated by this assembly but not others. Finally, we identified several signaling pathways which may mediate this phosphorylation and act in combination to regulate Oct4 transcriptional activity and protein stability. These results provide a mechanism for rapid and reversible alteration of Oct4 transactivation potential in response to extracellular signals.

Indexed as

Gene Expression RegulationTranscription, GeneticAnimalsCell DifferentiationCell LineCyclic AMPCyclic AMP-Dependent Protein KinasesDimerizationMiceModels, MolecularOctamer Transcription Factor-3p38 Mitogen-Activated Protein KinasesPoint MutationProtein Structure, QuaternarySignal TransductionCyclic AMPCyclic AMP-Dependent Protein KinasesOctamer Transcription Factor-3p38 Mitogen-Activated Protein KinasesPou5f1 protein, mouse

Identifiers

PMID19221599
PMCPMC2637973
OpenAlexW2095513789

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.