Histone deacetylase 3 preferentially binds and collaborates with the transcription factor RUNX1 to repress AML1-ETO-dependent transcription in t(8;21) AML.
Cell Line, Tumor
Core Binding Factor Alpha 2 Subunit
/ genetics
Gene Expression Regulation, Neoplastic
Genome, Human
/ genetics
Histone Deacetylases
/ genetics
Humans
Interleukin-8
/ genetics
Leukemia, Myeloid, Acute
/ genetics
Oncogene Proteins, Fusion
/ genetics
Promoter Regions, Genetic
RUNX1 Translocation Partner 1 Protein
/ genetics
Transcriptional Activation
/ genetics
Translocation, Genetic
/ genetics
AML1–ETO
GCN5
IL8/CXCL8
Runt-related transcription factor 1 (RUNX1)
acetyltransferase
histone deacetylase 3 (HDAC3)
interleukin
leukemia
p300
transcription coactivator
transcription corepressor
transcription factor
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
27 03 2020
27 03 2020
Historique:
received:
18
08
2019
revised:
11
02
2020
pubmed:
20
2
2020
medline:
15
12
2020
entrez:
20
2
2020
Statut:
ppublish
Résumé
In up to 15% of acute myeloid leukemias (AMLs), a recurring chromosomal translocation, termed t(8;21), generates the AML1-eight-twenty-one (ETO) leukemia fusion protein, which contains the DNA-binding domain of Runt-related transcription factor 1 (RUNX1) and almost all of ETO. RUNX1 and the AML1-ETO fusion protein are coexpressed in t(8;21) AML cells and antagonize each other's gene-regulatory functions. AML1-ETO represses transcription of RUNX1 target genes by competitively displacing RUNX1 and recruiting corepressors such as histone deacetylase 3 (HDAC3). Recent studies have shown that AML1-ETO and RUNX1 co-occupy the binding sites of AML1-ETO-activated genes. How this joined binding allows RUNX1 to antagonize AML1-ETO-mediated transcriptional activation is unclear. Here we show that RUNX1 functions as a
Identifiants
pubmed: 32071087
pii: S0021-9258(17)48748-5
doi: 10.1074/jbc.RA119.010707
pmc: PMC7105303
pii:
doi:
Substances chimiques
AML1-ETO fusion protein, human
0
Core Binding Factor Alpha 2 Subunit
0
Interleukin-8
0
Oncogene Proteins, Fusion
0
RUNX1 Translocation Partner 1 Protein
0
RUNX1 protein, human
0
Histone Deacetylases
EC 3.5.1.98
histone deacetylase 3
EC 3.5.1.98
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
4212-4223Subventions
Organisme : NCI NIH HHS
ID : P30 CA033572
Pays : United States
Organisme : NHLBI NIH HHS
ID : R01 HL093195
Pays : United States
Organisme : NCI NIH HHS
ID : R21 CA178513
Pays : United States
Organisme : NIGMS NIH HHS
ID : T32 GM008306
Pays : United States
Informations de copyright
© 2020 Guo et al.
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