Evidence map›Paper›PMID 11113190›Full record

ArticleMolecular and cellular biology2001

Oligomerization of ETO is obligatory for corepressor interaction.

J Zhang, B A Hug, E Y Huang, C W Chen, V Gelmetti, M Maccarana, S Minucci, P G Pelicci, M A Lazar

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
4.0field-weighted citation impact, top 5% 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

53 citing papers in PubMed, 104 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. The transcriptional corepressor CBFA2T3 inhibits all-The Journal of biological chemistry · 2020
    Article
  9. Article
  10. Review
  11. Review
  12. RUNX1-ETO: Attacking the Epigenome for Genomic Instable Leukemia.International journal of molecular sciences · 2019
    Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. INPP4B-mediated DNA repair pathway confers resistance to chemotherapy in acute myeloid leukemia.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016
    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

9 authors at 2 institutions in 2 countries.

J ZhangDivision of Endocrinology, Diabetes, and Metabolism, Departments of Medicine and Genetics, and The Penn Diabetes Center, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104, USA.
B A Hug
E Y Huang
C W Chen
V Gelmetti
M Maccarana
S Minucci
P G Pelicci
M A Lazar
University of Pennsylvania · USEuropean Institute of Oncology · IT

Funding

REV-ERB Nuclear Receptors in Circadian Rhythm and MetabolismR01DK045586 · NIDDK · UNIVERSITY OF PENNSYLVANIA · PI MITCHELL A. LAZAR · 1992 to 2026
$12.0M
THYROID HORMONE RECEPTORS-REGULATION AND FUNCTIONR37DK043806 · NIDDK · UNIVERSITY OF PENNSYLVANIA · PI LAZAR, MITCHELL A. · 1998 to 2017
$8.8M
NIDDK NIH HHS DK433806NIDDK NIH HHS DK45586NIDDK NIH HHS R01 DK045586NIDDK NIH HHS R37 DK043806
6 · The paper itself

Abstract

Nearly 40% of cases of acute myelogenous leukemia (AML) of the M2 subtype are due to a chromosomal translocation that combines a sequence-specific DNA binding protein, AML1, with a potent transcriptional repressor, ETO. ETO interacts with nuclear receptor corepressors SMRT and N-CoR, which recruit histone deacetylase to the AML1-ETO oncoprotein. SMRT-N-CoR interaction requires each of two zinc fingers contained in C-terminal Nervy homology region 4 (NHR4) of ETO. However, here we show that polypeptides containing NHR4 are insufficient for interaction with SMRT. NHR2 is also required for SMRT interaction and repression by ETO, as well as for inhibition of hematopoietic differentiation by AML1-ETO. NHR2 mediates oligomerization of ETO as well as AML1-ETO. Fusion of NHR4 polypeptide to a heterologous dimerization domain allows strong interaction with SMRT in vitro. These data support a model in which NHR2 and NHR4 have complementary functions in repression by ETO. NHR2 functions as an oligomerization domain bringing together NHR4 polypeptides that together form the surface required for high-affinity interaction with corepressors. As nuclear receptors also interact with corepressors as dimers, oligomerization may be a common mechanism regulating corepressor interactions.

Indexed as

Proto-Oncogene ProteinsBinding SitesCell DifferentiationDimerizationDNA-Binding ProteinsHematopoiesisHumansNuclear ProteinsNuclear Receptor Co-Repressor 1Nuclear Receptor Co-Repressor 2Peptide FragmentsProtein BindingProtein Structure, QuaternaryProtein Structure, TertiaryReceptors, Cytoplasmic and NuclearRepressor ProteinsDNA-Binding ProteinsNCOR1 protein, humanNCOR2 protein, humanNuclear ProteinsNuclear Receptor Co-Repressor 1Nuclear Receptor Co-Repressor 2Peptide FragmentsProto-Oncogene ProteinsReceptors, Cytoplasmic and NuclearRepressor ProteinsRUNX1T1 protein, humanRUNX1 Translocation Partner 1 ProteinTranscription Factors

Identifiers

PMID11113190
PMCPMC88789
OpenAlexW1970746316

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.