Evidence map›Paper›PMID 20587419›Full record

ArticleThe Journal of biological chemistry2010

Sumoylation regulates interaction of FOG1 with C-terminal-binding protein (CTBP).

Jonathan W Snow, Jonghwan Kim, Caroline R Currie, Jian Xu, Stuart H Orkin

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

17 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Review
  6. Review
  7. Review
  8. Article
  9. Epigenetic and genetic mechanisms in red cell biology.Current opinion in hematology · 2014
    Review
  10. Transcriptional mechanisms underlying hemoglobin synthesis.Cold Spring Harbor perspectives in medicine · 2013
    Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Networking erythropoiesis.The Journal of experimental medicine · 2010
    Review
  17. 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

5 authors at 4 institutions in 1 country.

Jonathan W SnowDivision of Hematology/Oncology, Children's Hospital, Boston, Massachusetts 02115, USA.
Jonghwan Kim
Caroline R Currie
Jian Xu
Stuart H Orkin
Howard Hughes Medical Institute · USBoston Children's Hospital · USDana-Farber Cancer Institute · USHarvard University · US

Funding

MOLECULAR ANALYSIS OF NORMAL AND TYHALASSEMIC DNAR01HL032259 · NHLBI · CHILDREN'S HOSPITAL BOSTON · PI ORKIN, STUART H · 1985 to 2022
$8.8M
Howard Hughes Medical InstituteNHLBI NIH HHS HL32259NHLBI NIH HHS R01 HL032259
6 · The paper itself

Abstract

Erythropoietic and megakaryocytic programs are specified from multipotential progenitors by the transcription factor GATA1. FOG1, a GATA1-interaction partner, is critical for GATA1 function in several contexts by bringing multiple complexes into association with GATA1 to facilitate activation or repression of target genes. To further elucidate regulation of these associations by cellular and extracellular cues, we examined FOG1 for post-translational modifications. We found that FOG1 is SUMOylated and phosphorylated in erythroid cells in a differentiation-dependent manner. Removal of the SUMOylation sites in FOG1 does not impair nuclear localization, protein stability, or chromatin occupancy. However, SUMOylation of FOG1 modulates interactions with C-terminal binding protein family members, specifically promoting CTBP1 binding. Phosphorylation of FOG1 modulates SUMOylation and, therefore, indirectly regulates the CTBP interaction. Post-translational modification of FOG1 may contribute to control of co-occupancy by CTBP family members, the NuRD complex, and GATA1 at differentially regulated genes.

Indexed as

Alcohol OxidoreductasesCell LineDNA-Binding ProteinsErythroid CellsHumansLysineMegakaryocytesMutagenesis, Site-DirectedMutationPeptide HydrolasesPhosphorylationProtein BindingProtein Processing, Post-TranslationalProtein TransportSmall Ubiquitin-Related Modifier ProteinsSubstrate SpecificityAlcohol OxidoreductasesC-terminal binding proteinDNA-Binding ProteinsLysinePeptide HydrolasesSmall Ubiquitin-Related Modifier ProteinsSUMO-1 ProteinSUMO1 protein, humanTranscription Factors

Identifiers

PMID20587419
PMCPMC2934671
OpenAlexW2093276293

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.