Heat shock factor 1 (HSF1) specifically potentiates c-MYC-mediated transcription independently of the canonical heat shock response.
CP: Molecular biology
CUT&RUN-seq
GCN5
HSF1
c-MYC
transcription factor complex
Journal
Cell reports
ISSN: 2211-1247
Titre abrégé: Cell Rep
Pays: United States
ID NLM: 101573691
Informations de publication
Date de publication:
27 06 2023
27 06 2023
Historique:
received:
19
09
2022
revised:
27
03
2023
accepted:
08
05
2023
medline:
4
10
2023
pubmed:
24
5
2023
entrez:
24
5
2023
Statut:
ppublish
Résumé
Despite its pivotal roles in biology, how the transcriptional activity of c-MYC is tuned quantitatively remains poorly defined. Here, we show that heat shock factor 1 (HSF1), the master transcriptional regulator of the heat shock response, acts as a prime modifier of the c-MYC-mediated transcription. HSF1 deficiency diminishes c-MYC DNA binding and dampens its transcriptional activity genome wide. Mechanistically, c-MYC, MAX, and HSF1 assemble into a transcription factor complex on genomic DNAs, and surprisingly, the DNA binding of HSF1 is dispensable. Instead, HSF1 physically recruits the histone acetyltransferase general control nonderepressible 5 (GCN5), promoting histone acetylation and augmenting c-MYC transcriptional activity. Thus, we find that HSF1 specifically potentiates the c-MYC-mediated transcription, discrete from its canonical role in countering proteotoxic stress. Importantly, this mechanism of action engenders two distinct c-MYC activation states, primary and advanced, which may be important to accommodate diverse physiological and pathological conditions.
Identifiants
pubmed: 37224019
pii: S2211-1247(23)00568-5
doi: 10.1016/j.celrep.2023.112557
pmc: PMC10592515
mid: NIHMS1912767
pii:
doi:
Substances chimiques
DNA
9007-49-2
DNA-Binding Proteins
0
Heat Shock Transcription Factors
0
Proto-Oncogene Proteins c-myc
0
Transcription Factors
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, N.I.H., Intramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
112557Subventions
Organisme : NIH HHS
ID : DP2 OD007070
Pays : United States
Organisme : Intramural NIH HHS
ID : ZIA BC011767
Pays : United States
Informations de copyright
Copyright © 2023 The Author(s). Published by Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of interests The authors declare no competing interests.
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