Molecular mechanisms of TWIST1-regulated transcription in EMT and cancer metastasis.


Journal

EMBO reports
ISSN: 1469-3178
Titre abrégé: EMBO Rep
Pays: England
ID NLM: 100963049

Informations de publication

Date de publication:
06 11 2023
Historique:
revised: 23 08 2023
received: 28 01 2023
accepted: 25 08 2023
pmc-release: 08 09 2024
medline: 7 11 2023
pubmed: 8 9 2023
entrez: 8 9 2023
Statut: ppublish

Résumé

TWIST1 induces epithelial-to-mesenchymal transition (EMT) to drive cancer metastasis. It is yet unclear what determines TWIST1 functions to activate or repress transcription. We found that the TWIST1 N-terminus antagonizes TWIST1-regulated gene expression, cancer growth and metastasis. TWIST1 interacts with both the NuRD complex and the NuA4/TIP60 complex (TIP60-Com) via its N-terminus. Non-acetylated TWIST1-K73/76 selectively interacts with and recruits NuRD to repress epithelial target gene transcription. Diacetylated TWIST1-acK73/76 binds BRD8, a component of TIP60-Com that also binds histone H4-acK5/8, to recruit TIP60-Com to activate mesenchymal target genes and MYC. Knockdown of BRD8 abolishes TWIST1 and TIP60-Com interaction and TIP60-Com recruitment to TWIST1-activated genes, resulting in decreasing TWIST1-activated target gene expression and cancer metastasis. Both TWIST1/NuRD and TWIST1/TIP60-Com complexes are required for TWIST1 to promote EMT, proliferation, and metastasis at full capacity. Therefore, the diacetylation status of TWIST1-K73/76 dictates whether TWIST1 interacts either with NuRD to repress epithelial genes, or with TIP60-Com to activate mesenchymal genes and MYC. Since BRD8 is essential for TWIST1-acK73/76 and TIP60-Com interaction, targeting BRD8 could be a means to inhibit TWIST1-activated gene expression.

Identifiants

pubmed: 37680145
doi: 10.15252/embr.202356902
pmc: PMC10626429
doi:

Substances chimiques

TWIST1 protein, human 0
Nuclear Proteins 0
Twist-Related Protein 1 0

Banques de données

GEO
['GSE189828']

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

e56902

Subventions

Organisme : NCI NIH HHS
ID : R01 CA193455
Pays : United States
Organisme : NCI NIH HHS
ID : R21 CA267006
Pays : United States
Organisme : NCI NIH HHS
ID : P30 CA125123
Pays : United States
Organisme : NIDCR NIH HHS
ID : R21 DE033147
Pays : United States
Organisme : NIH HHS
ID : S10 OD028648
Pays : United States

Informations de copyright

© 2023 The Authors.

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Auteurs

Xiaobin Yu (X)

Department of Molecular and Cellular Biology, Baylor College of Medicine, Houston, TX, USA.

Tao He (T)

Department of Molecular and Cellular Biology, Baylor College of Medicine, Houston, TX, USA.

Zhangwei Tong (Z)

Department of Molecular and Cellular Biology, Baylor College of Medicine, Houston, TX, USA.

Lan Liao (L)

Department of Molecular and Cellular Biology, Baylor College of Medicine, Houston, TX, USA.
Dan L. Duncan Comprehensive Cancer Center, Baylor College of Medicine, Houston, TX, USA.

Shixia Huang (S)

Department of Molecular and Cellular Biology, Baylor College of Medicine, Houston, TX, USA.
Dan L. Duncan Comprehensive Cancer Center, Baylor College of Medicine, Houston, TX, USA.

Walid D Fakhouri (WD)

Department of Diagnostic and Biomedical Sciences, Center for Craniofacial Research, School of Dentistry, University of Texas Health Science Center at Houston, Houston, TX, USA.

Dean P Edwards (DP)

Department of Molecular and Cellular Biology, Baylor College of Medicine, Houston, TX, USA.
Dan L. Duncan Comprehensive Cancer Center, Baylor College of Medicine, Houston, TX, USA.

Jianming Xu (J)

Department of Molecular and Cellular Biology, Baylor College of Medicine, Houston, TX, USA.
Dan L. Duncan Comprehensive Cancer Center, Baylor College of Medicine, Houston, TX, USA.

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