Evidence map›Paper›PMID 10673508›Full record

ArticleGenes & development2000

Phosphorylation represses Ets-1 DNA binding by reinforcing autoinhibition.

D O Cowley, B J Graves

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing 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

68 citing papers in PubMed, 146 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. ETS1 Function in Leukemia and Lymphoma.Advances in experimental medicine and biology · 2024
    Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

8 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

2 authors at 1 institution in 1 country.

D O CowleyHuntsman Cancer Institute, University of Utah, Salt Lake City, Utah 84112-5550, USA.
B J Graves
Huntsman Cancer Institute · US

Funding

UTAH REGIONAL CANCER CENTERP30CA042014 · NCI · UTAH STATE HIGHER EDUCATION SYSTEM--UNIVERSITY OF UTAH · PI Jared P Rutter · 1986 to 2026
$72.6M
DEVELOPMENTAL BIOLOGY TRAINING PROGRAMT32HD007491 · NICHD · UTAH STATE HIGHER EDUCATION SYSTEM--UNIVERSITY OF UTAH · PI James Alan Gagnon, Kristen M Kwan · 1995 to 2026
$8.0M
Transcriptional Control Mechanisms by ETS FactorsR01GM038663 · NIGMS · UNIVERSITY OF UTAH · PI GRAVES, BARBARA J · 1992 to 2015
$3.9M
RETROVIRAL TRANSCRIPTIONAL CONTROL MECHANISMSR29GM038663 · NIGMS · UNIVERSITY OF UTAH · PI GRAVES, BARBARA J · 1987 to 1991
–
NCI NIH HHS CA-24014NICHD NIH HHS HD-07491NICHD NIH HHS T32 HD007491NIGMS NIH HHS GM-38663NIGMS NIH HHS R01 GM038663
6 · The paper itself

Abstract

Phosphorylation of transcription factors is a key link between cell signaling and the control of gene expression. Here we report that phosphorylation regulates DNA binding of the Ets-1 transcription factor by reinforcing an autoinhibitory mechanism. Quantitative DNA-binding assays show that calcium-dependent phosphorylation inhibits Ets-1 DNA binding 50-fold. The four serines that mediate this inhibitory effect are distant from the DNA-binding domain but near structural elements required for autoinhibition. Mutational analyses demonstrate that an intact inhibitory module is required for phosphorylation-dependent regulation. Partial proteolysis studies indicate that phosphorylation stabilizes an inhibitory conformation. These findings provide a structural mechanism for phosphorylation-dependent inhibition of Ets-1 DNA binding and demonstrate a new function for inhibitory modules as structural mediators of negative signaling events.

Indexed as

Amino Acid SequenceCalcium-Calmodulin-Dependent Protein KinasesCalcium-Calmodulin-Dependent Protein Kinase Type 2Cell ExtractsDNADNA-Binding ProteinsHumansModels, BiologicalMolecular Sequence DataMutagenesis, Site-DirectedPhosphorylationPhosphoserineProtein Structure, TertiaryProto-Oncogene Protein c-ets-1Proto-Oncogene ProteinsProto-Oncogene Proteins c-etsCalcium-Calmodulin-Dependent Protein KinasesCalcium-Calmodulin-Dependent Protein Kinase Type 2Cell ExtractsDNADNA-Binding ProteinsETS1 protein, humanPhosphoserineProto-Oncogene Protein c-ets-1Proto-Oncogene ProteinsProto-Oncogene Proteins c-etsTranscription Factors

Identifiers

PMID10673508
PMCPMC316366
OpenAlexW2131713324

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.