Evidence map›Paper›PMID 11259590›Full record

ArticleMolecular and cellular biology2001

Site-specific acetylation by p300 or CREB binding protein regulates erythroid Krüppel-like factor transcriptional activity via its interaction with the SWI-SNF complex.

W Zhang, S Kadam, B M Emerson, J J Bieker

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 93 papers.

0numbers the graph read from it
0cells of the map it votes in
93citing papers in PubMed
5.4field-weighted citation impact, top 3% 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

93 citing papers in PubMed, 180 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Erythropoiesis: insights from a genomic perspective.Experimental & molecular medicine · 2024
    Review
  5. Review
  6. Article
  7. Article
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  11. Article
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  15. Review
  16. AMolecular and cellular biology · 2020
    Article
  17. Article
  18. Article
  19. Article
  20. Article

33 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

4 authors at 2 institutions in 1 country.

W ZhangDepartment of Biochemistry and Molecular Biology, Mount Sinai School of Medicine, New York, NY 10029, USA.
S Kadam
B M Emerson
J J Bieker
Icahn School of Medicine at Mount Sinai · USSalk Institute for Biological Studies · US

Funding

Function of Putative Determinant in HematopoiesisR01DK046865 · NIDDK · MOUNT SINAI SCHOOL OF MEDICINE OF NYU · PI JAMES J BIEKER · 1993 to 2026
$11.2M
Specificity of Mammalian SWI/SNF Remodeling ComplexesR01GM038760 · NIGMS · SALK INSTITUTE FOR BIOLOGICAL STUDIES · PI EMERSON, BEVERLY MARIE · 1987 to 2007
$4.4M
NIDDK NIH HHS DK46865NIDDK NIH HHS R01 DK046865NIGMS NIH HHS GM38760NIGMS NIH HHS R01 GM038760
6 · The paper itself

Abstract

Recruitment of modifiers and remodelers to specific DNA sites within chromatin plays a critical role in controlling gene expression. The study of globin gene regulation provides a convergence point within which to address these issues in the context of tissue-specific and developmentally regulated expression. In this regard, erythroid Krüppel-like factor (EKLF) is critical. EKLF is a red cell-specific activator whose presence is crucial for establishment of the correct chromatin structure and high-level transcriptional induction of adult beta-globin. We now find, by metabolic labeling-immunoprecipitation experiments, that EKLF is acetylated in the erythroid cell. EKLF residues acetylated by CREB binding protein (CBP) in vitro map to Lys-288 in its transactivation domain and Lys-302 in its zinc finger domain. Although site-specific DNA binding by EKLF is unaffected by the acetylation status of either of these lysines, directed mutagenesis of Lys-288 (but not Lys-302) decreases the ability of EKLF to transactivate the beta-globin promoter in vivo and renders it unable to be superactivated by coexpressed p300 or CBP. In addition, the acetyltransferase function of CBP or p300 is required for superactivation of wild-type EKLF. Finally, acetylated EKLF has a higher affinity for the SWI-SNF chromatin remodeling complex and is a more potent transcriptional activator of chromatin-assembled templates in vitro. These results demonstrate that the acetylation status of EKLF is critical for its optimal activity and suggest a mechanism by which EKLF acts as an integrator of remodeling and transcriptional components to alter chromatin structure and induce adult beta-globin expression within the beta-like globin cluster.

Indexed as

Drosophila ProteinsRNA-Binding ProteinsAcetylationAdultAnimalsCOS CellsCREB-Binding ProteinDNA-Binding ProteinsErythrocytesHistone AcetyltransferasesHumansK562 CellsKruppel-Like Transcription FactorsMiceNuclear ProteinsNuclear Receptor Coactivator 3CREB-Binding ProteinCREBBP protein, humanCrebbp protein, mouseDNA-Binding ProteinsDrosophila Proteinserythroid Kruppel-like factorHistone AcetyltransferasesKruppel-Like Transcription FactorsNCOA3 protein, humanNcoa3 protein, mouseNuclear ProteinsNuclear Receptor Coactivator 3Ribonucleoprotein, U1 Small NuclearRNA-Binding Proteinssnf protein, DrosophilaTrans-ActivatorsTranscription Factors

Identifiers

PMID11259590
PMCPMC86874
OpenAlexW2140089594

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.