Evidence map›Paper›PMID 17200232›Full record

ArticleGenome research2007

Serum response factor binding sites differ in three human cell types.

Sara J Cooper, Nathan D Trinklein, Loan Nguyen, Richard M Myers

Open access · hybridAbstract readComparative Study
In one paragraph

Article in Genome research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
–field-weighted citation impact
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

50 citing papers in PubMed, 75 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. The organization and regulation of mRNA-protein complexes.Wiley interdisciplinary reviews. RNA · 2017
    Review
  12. Multi-phenotypic Role of Serum Response Factor in the Gastrointestinal System.Journal of neurogastroenterology and motility · 2016
    Review
  13. Review
  14. The neuronal activity-driven transcriptome.Molecular neurobiology · 2015
    Review
  15. Article
  16. Article
  17. SRF phosphorylation by glycogen synthase kinase-3 promotes axon growth in hippocampal neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014
    Article
  18. Article
  19. Article
  20. 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

4 authors at 1 institution in 1 country.

Sara J CooperDepartment of Genetics, Stanford University School of Medicine, Stanford, California 94305-5120, USA.
Nathan D Trinklein
Loan Nguyen
Richard M Myers
Stanford University · US

Funding

INSTITUTIONAL TRAINING GRANT IN GENOME SCIENCET32HG000044 · NHGRI · STANFORD UNIVERSITY · PI MICHAEL P. SNYDER · 1995 to 2026
$32.2M
The Stanford ENCODE ProjectU01HG003162 · NHGRI · STANFORD UNIVERSITY · PI MYERS, RICHARD M · 2003 to 2006
$11.2M
NHGRI NIH HHS 1 U01 HG 03162-01NHGRI NIH HHS 5 T32 HG00044NHGRI NIH HHS T32 HG000044NHGRI NIH HHS U01 HG003162
6 · The paper itself

Abstract

The serum response factor (SRF) is essential for embryonic development and maintenance of muscle cells and neurons. The mechanism by which this factor controls these divergent pathways is unclear. Here we present a genome-wide view of occupancy of SRF at its binding sites with a focus on those that vary with cell type. We used chromatin immunoprecipitation (ChIP) in combination with human promoter microarrays to identify 216 putative SRF binding sites in the human genome. We performed independent quantitative PCR validation at over half of these sites that resulted in 146 sites we assert to be true binding sites at over 90% confidence. Nearly half of the sites are bound by SRF in only one of the three cell types we tested, providing strong evidence for the diverse roles for SRF in different cell types. We also explore possible mechanisms controlling differential binding of SRF in these cell types by assaying cofactor binding, DNA methylation, histone methylation, and histone acetylation at a subset of sites bound preferentially in smooth muscle cells. Although we did not see a strong correlation between SRF binding and epigenetics modifications, at these sites, we propose that SRF cofactors may play an important role in determining cell-dependent SRF binding sites. ELK4 (previously known as SAP-1 [SRF-associated protein-1]) is ubiquitously expressed. Therefore, we expected it to occupy sites where SRF binding is common in all cell types. Indeed, 90% of SRF sites also bound by ELK4 were common to all three cell types. Together, our data provide a more complete understanding of the regulatory network controlled by SRF.

Indexed as

Binding SitesCell LineChromatin ImmunoprecipitationEpigenesis, Geneticets-Domain Protein Elk-4Genome, HumanHumansJurkat CellsMyocytes, Smooth MuscleNeuronsOligonucleotide Array Sequence AnalysisPromoter Regions, GeneticSerum Response FactorELK4 protein, humanets-Domain Protein Elk-4Serum Response FactorSRF protein, human

Identifiers

PMID17200232
PMCPMC1781345
OpenAlexW2008509160

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.