Evidence map›Paper›PMID 17901130›Full record

ArticleMolecular endocrinology (Baltimore, Md.)2008

Phosphorylation of steroidogenic factor 1 is mediated by cyclin-dependent kinase 7.

Aurélia E Lewis, Marte Rusten, Erling A Hoivik, Elisabeth L Vikse, Magnus L Hansson, Annika E Wallberg, Marit Bakke

Open access · greenAbstract read
In one paragraph

Article in Molecular endocrinology (Baltimore, Md.), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

22 citing papers in PubMed, 41 citations in OpenAlex.

  1. Review
  2. Adrenocortical stem cells in health and disease.Nature reviews. Endocrinology · 2025
    Review
  3. Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. Coordination of Multiple Cellular Processes by NR5A1/Nr5a1.Endocrinology and metabolism (Seoul, Korea) · 2020
    Review
  9. Steroidogenic Factor 1 (NR5A1) Activates ATF3 Transcriptional Activity.International journal of molecular sciences · 2020
    Article
  10. Article
  11. Hedgehog signaling and steroidogenesis.Annual review of physiology · 2015
    Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Review
  20. Complex assembly on the human CYP17 promoter.Molecular and cellular endocrinology · 2009
    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 2 institutions in 2 countries.

Aurélia E LewisDepartment of Biomedicine, University of Bergen, 5009 Bergen, Norway.
Marte Rusten
Erling A Hoivik
Elisabeth L Vikse
Magnus L Hansson
Annika E Wallberg
Marit Bakke
University of Bergen · NOKarolinska Institutet · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The nuclear receptor steroidogenic factor-1 (SF1) is critical for development and function of steroidogenic tissues. Posttranslational modifications are known to influence the transcriptional capacity of SF1, and it was previously demonstrated that serine 203 is phosphorylated. In this paper we report that serine 203 is phosphorylated by a cyclin-dependent kinase 7 (CDK7)-mediated process. As part of the CDK-activating kinase complex, CDK7 is a component of the basal transcription factor TFIIH, and phosphorylation of SF1 as well as SF1-dependent transcription was clearly reduced in cells carrying a mutation that renders the CDK-activating kinase complex unable to interact with the TFIIH core. Coimmunoprecipitation analyses revealed that SF1 and CDK7 reside in the same complex, and kinase assays demonstrated that immunoprecipitated CDK7 and purified TFIIH phosphorylate SF1 in vitro. The CDK inhibitor roscovitine blocked phosphorylation of SF1, and an inactive form of CDK7 repressed the phosphorylation level and the transactivation capacity of SF1. Structural studies have identified phosphoinositides as potential ligands for SF1. Interestingly, we found that mutations designed to block phospholipid binding dramatically decreased the level of SF1 phosphorylation. Together our results suggest a connection between ligand occupation and phosphorylation and association with the basic transcriptional machinery, indicating an intricate regulation of SF1 transactivation.

Indexed as

Acute-Phase ProteinsAmino Acid SequenceAnimalsBlotting, WesternCarrier ProteinsCell Cycle ProteinsCell LineChlorocebus aethiopsCOS CellsCyclin-Dependent Kinase-Activating KinaseCyclin-Dependent KinasesHeLa CellsHumansImmunoprecipitationLipopolysaccharide-Binding ProteinMembrane GlycoproteinsAcute-Phase ProteinsCarrier ProteinsCell Cycle ProteinsCyclin-Dependent Kinase-Activating KinaseCyclin-Dependent KinasesLipopolysaccharide-Binding ProteinMembrane GlycoproteinsMNAT1 protein, humanNR5A1 protein, humanPhospholipidsPurinesRoscovitineSerineSteroidogenic Factor 1Transcription FactorsTranscription Factor TFIIH

Identifiers

PMID17901130
PMCPMC5419630
OpenAlexW2041816594

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.