ZBTB2 protein is a new partner of the Nucleosome Remodeling and Deacetylase (NuRD) complex

Russo, Rosita; Russo, Veronica; Cecere, Francesco; Valletta, Mariangela; Gentile, Maria Teresa; Colucci-D’Amato, Luca; Angelini, Claudia; Riccio, Andrea; Pedone, Paolo V.; Baglivo, Ilaria

doi:10.1016/j.ijbiomac.2020.12.029

Cited by 4 publications

(1 citation statement)

References 46 publications

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“…This raises the question whether PATZ1 can also bind to the NuRD complex. In fact the BTB domains of PATZ1 and numerous other family members were shown to interact with the Gatad2 component of the NuRD complex in a yeast two hybrid screen [28,78]. The predicted ThPOK-NuRD interaction site also has residues in the extreme C-terminus of the BTB domain.…”

Section: The Choice Between Ncor Vs Nurdmentioning

confidence: 99%

Dimerization choice and alternative functions of ZBTB transcription factors

Barakat,

Ezen,

Devecioğlu

et al. 2023

The FEBS Journal

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Zinc Finger DNA‐binding domain‐containing proteins are the most populous family among eukaryotic transcription factors. Among these, members of the BTB domain‐containing ZBTB sub‐family are mostly known for their transcriptional repressive functions. In this Viewpoint article, we explore molecular mechanisms that potentially diversify the function of ZBTB proteins based on their homo and heterodimerization, alternative splicing and post‐translational modifications. We describe how the BTB domain is as much a scaffold for the assembly of co‐repressors, as a domain that regulates protein stability. We highlight another mechanism that regulates ZBTB protein stability: phosphorylation in the zinc finger domain. We explore the non‐transcriptional, structural roles of ZBTB proteins and highlight novel findings that describe the ability of ZBTB proteins to associate with poly adenosine ribose in the nucleus during the DNA damage response. Herein, we discuss the contribution of BTB domain scaffolds to the formation of transcriptional repressive complexes, to chromosome compartmentalization and their non‐transcriptional, purely structural functions in the nucleus.

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Section: The Choice Between Ncor Vs Nurdmentioning

confidence: 99%

Dimerization choice and alternative functions of ZBTB transcription factors

Barakat,

Ezen,

Devecioğlu

et al. 2023

The FEBS Journal

View full text Add to dashboard Cite

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Histone deacetylase complexes: Structure, regulation and function

Asmamaw,

He,

Zhang

et al. 2024

Biochimica et Biophysica Acta (BBA) - Reviews on Cancer

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BTBD10 inhibits glioma tumorigenesis by downregulating cyclin D1 and p-Akt

Liu

Chen

et al. 2022

Open Life Sciences

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The aim of this study was to investigate the role of BTBD10 in glioma tumorigenesis. The mRNA and protein levels of BTBD10 in 52 glioma tissues and eight normal brain tissues were determined using reverse transcription polymerase chain reaction (RT-PCR) and western blot analysis, respectively. U251 human glioblastoma cells were infected with BTBD10-expressing or control lentiviruses. Cell growth was evaluated using the methyl thiazolyl tetrazolium (MTT) assay. Cell apoptosis and cell cycle distribution were analyzed using flow cytometry. Cyclin D1 and p-Akt levels were determined using western blot analysis. The results showed that BTBD10 mRNA and protein levels were significantly lower in glioma tissues than in normal brain tissues. Additionally, BTBD10 levels were significantly lower in high-grade gliomas than in low-grade tumors. Compared with control cells, U251 cells overexpressing BTBD10 exhibited decreased cell proliferation, increased cell accumulation at the G0/G1 phase, increased cell apoptosis, and decreased levels of cyclin D1 and p-Akt. These findings show that BTBD10 is downregulated in human glioma tissue and that BTBD10 expression negatively correlates with the pathological grade of the tumor. Furthermore, BTBD10 overexpression inhibits proliferation, induces G0/G1 arrest, and promotes apoptosis in human glioblastoma cells by downregulating cyclin D1- and Akt-dependent signaling pathways.

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ZBTB2 protein is a new partner of the Nucleosome Remodeling and Deacetylase (NuRD) complex

Cited by 4 publications

References 46 publications

Dimerization choice and alternative functions of ZBTB transcription factors

Dimerization choice and alternative functions of ZBTB transcription factors

Histone deacetylase complexes: Structure, regulation and function

BTBD10 inhibits glioma tumorigenesis by downregulating cyclin D1 and p-Akt

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