Evidence map›Paper›PMID 19654328›Full record

ArticleThe Journal of biological chemistry2009

Translational isoforms of FOG1 regulate GATA1-interacting complexes.

Jonathan W Snow, Stuart H Orkin

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

16 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Expression of different functional isoforms in haematopoiesis.International journal of hematology · 2014
    Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Building multifunctionality into a complex containing master regulators of hematopoiesis.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  14. GATA switches as developmental drivers.The Journal of biological chemistry · 2010
    Review
  15. Article
  16. 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

2 authors at 1 institution in 1 country.

Jonathan W SnowDivision of Hematology/Oncology, Children's Hospital, Boston, Massachusetts 02115, USA.
Stuart H Orkin
Boston Children's Hospital · US

Funding

TRANSCRIPTION FACTOR GATA-1 IN TERMINAL ERYTHROID DEVELOPMENTP01HL032262 · NHLBI · CHILDREN'S HOSPITAL BOSTON · PI ORKIN, STUART H · 1985 to 2021
$38.9M
MOLECULAR ANALYSIS OF NORMAL AND TYHALASSEMIC DNAR01HL032259 · NHLBI · CHILDREN'S HOSPITAL BOSTON · PI ORKIN, STUART H · 1985 to 2022
$8.8M
NHLBI NIH HHS HL32259NHLBI NIH HHS HL32262NHLBI NIH HHS P01 HL032262NHLBI NIH HHS R01 HL032259
6 · The paper itself

Abstract

Erythropoietic and megakaryocytic programs are directed by the transcription factor GATA1. Friend of GATA1 (FOG1), a protein interaction partner of GATA1, is critical for GATA1 function in multiple contexts. Previous work has shown that FOG1 recruits two multi-protein complexes, the nucleosome remodeling domain (NuRD) complex and a C-terminal binding protein (CTBP)-containing complex, into association with GATA1 to mediate activation and repression of target genes. To elucidate mechanisms that might differentially regulate the association of FOG1, as well as GATA1, with these two complexes, we characterized a previously unrecognized translational isoform of FOG1. We found that an N-terminally truncated version of FOG1 is produced from an internal ATG and that this isoform, designated FOG1S, lacks the nucleosome remodeling domain-binding domain, altering the complexes with which it interacts. Both isoforms interact with the C-terminal binding protein complex, which we show also contains lysine-specific demethylase 1 (LSD1). FOG1S is preferentially excluded from the nucleus by unknown mechanisms. These data reveal two novel mechanisms for the regulation of GATA1 interaction with FOG1-dependent protein complexes through the production of two translational isoforms with differential interaction profiles and independent nuclear localization controls.

Indexed as

AnimalsCell Line, TumorGATA1 Transcription FactorHistone DemethylasesHumansMi-2 Nucleosome Remodeling and Deacetylase ComplexMiceMultiprotein ComplexesNuclear ProteinsOxidoreductases, N-DemethylatingProtein BiosynthesisProtein IsoformsTranscription FactorsGATA1 protein, humanGata1 protein, mouseGATA1 Transcription FactorHistone DemethylasesKDM1A protein, humanKDM1a protein, mouseMi-2 Nucleosome Remodeling and Deacetylase ComplexMultiprotein ComplexesNuclear ProteinsOxidoreductases, N-DemethylatingProtein IsoformsTranscription FactorsZFPM1 protein, humanZfpm1 protein, mouse

Identifiers

PMID19654328
PMCPMC2785561
OpenAlexW2094152194

What OpenQuestion holds

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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.