Kaiso regulates Znf131-mediated transcriptional activation

Donaldson, Nickett S.; Nordgaard, Curtis L.; Pierre, Christina C.; Kelly, Kevin F.; Robinson, Shaiya C.; Swystun, Laura L.; Henriquez, Roberto; Graham, Monica; Daniel, Juliet M.

doi:10.1016/j.yexcr.2010.03.011

Cited by 19 publications

(24 citation statements)

References 41 publications

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“…1B, EMSY/KDM5A components co-purified with GFP-ZNF131, as well as some subunits of the MLL H3K4me3 methyltransferase complex (MLL, DPY-30). We did not, however detect the previously reported ZNF131 interactor Kaiso (21). Nevertheless, a number of other putative DNA-binding proteins were identified as interactors, including ZMYM1, ZBTB3, and ZNF281.…”

Section: Indicated) C Effect Of Deletion Of Emsy From Hela Cells Oncontrasting

confidence: 99%

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Recruitment of the Mammalian Histone-modifying EMSY Complex to Target Genes Is Regulated by ZNF131

Varier

Pau

Groep

et al. 2016

Journal of Biological Chemistry

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Recent work from others and us revealed interactions between the Sin3/HDAC complex, the H3K4me3 demethylase KDM5A, GATAD1, and EMSY. Here, we characterize the EMSY/KDM5A/SIN3B complex in detail by quantitative interaction proteomics and ChIP-sequencing. We identify a novel substoichiometric interactor of the complex, transcription factor ZNF131, which recruits EMSY to a large number of active, H3K4me3 marked promoters. Interestingly, using an EMSY knock-out line and subsequent rescue experiments, we show that EMSY is in most cases positively correlated with transcriptional activity of its target genes and stimulates cell proliferation. Finally, by immunohistochemical staining of primary breast tissue microarrays we find that EMSY/KDM5A/SIN3B complex subunits are frequently overexpressed in primary breast cancer cases in a correlative manner. Taken together, these data open venues for exploring the possibility that sporadic breast cancer patients with EMSY amplification might benefit from epigenetic combination therapy targeting both the KDM5A demethylase and histone deacetylases.

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Section: Indicated) C Effect Of Deletion Of Emsy From Hela Cells Oncontrasting

confidence: 99%

“…Pathways with a Benjamini-Hochberg corrected p value lower than 0.1 were considered significant. Motif Enrichment Analysis-The ZNF131 DNA-binding motifs were obtained from Donaldson et al (21). We calculated the frequency of the motif in the EMSY-binding sites.…”

Section: Methodsmentioning

confidence: 99%

Recruitment of the Mammalian Histone-modifying EMSY Complex to Target Genes Is Regulated by ZNF131

Varier

Pau

Groep

et al. 2016

Journal of Biological Chemistry

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“…Because SRA domain is required for full SUMO E3 activity, as well as for SUMOylation of UHRF2 itself, we speculate that SUMO E3 ligase activity of UHRF2 somehow plays a role to regulate cell proliferation. Nevertheless, UHRF2-mediated SUMOylation might regulate other ZNF131 functions, including its putative transcriptional activator function (45). Although additional functions of ZNF131 remain unclear, it will be interesting to test whether SUMOylation may affect those activities of ZNF131.…”

Section: Discussionmentioning

confidence: 99%

UHRF2, a Ubiquitin E3 Ligase, Acts as a Small Ubiquitin-like Modifier E3 Ligase for Zinc Finger Protein 131

Chung

2013

Journal of Biological Chemistry

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“…Some members of BTB-ZF protein family function as a suppressor of transcription through forming a complex with epigenetic modifiers with repressive activities such as histone deacetylase 1/2. Binding motif of Znf131 has been reported (13). Znf131 acts as a positive transcription factor for the artificial promoter harboring several copies of this binding motif.…”

Section: Cd4mentioning

confidence: 97%

“…Znf131 was shown to suppress estrogen signaling by binding to estrogen receptor, leading to the inhibition of breast cancer cell proliferation by estrogen (12). Znf131 was identified as a partner molecule for another BTB-ZF protein Kaiso (Zbtb33) (13). Kaiso can interact with DNA through a specific binding sequence, as well as a methylated cytosine of DNA.…”

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confidence: 99%

BTB-ZF Protein Znf131 Regulates Cell Growth of Developing and Mature T Cells

Iguchi

Aoki

Ikawa

et al. 2015

The Journal of Immunology

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Many members of the BTB-ZF family have been shown to play important roles in lymphocyte development and function. The role of zinc finger Znf131 (also known as Zbtb35) in T cell lineage was elucidated through the production of mice with floxed allele to disrupt at different stages of development. In this article, we present that Znf131 is critical for T cell development during double-negative to double-positive stage, with which significant cell expansion triggered by the pre-TCR signal is coupled. In mature T cells, Znf131 is required for the activation of effector genes, as well as robust proliferation induced upon TCR signal. One of the cyclin-dependent kinase inhibitors, p21Cip1 encoded by cdkn1a gene, is one of the targets of Znf131. The regulation of T cell proliferation by Znf131 is in part attributed to its suppression on the expression of p21Cip1.

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Kaiso regulates Znf131-mediated transcriptional activation

Cited by 19 publications

References 41 publications

Recruitment of the Mammalian Histone-modifying EMSY Complex to Target Genes Is Regulated by ZNF131

Recruitment of the Mammalian Histone-modifying EMSY Complex to Target Genes Is Regulated by ZNF131

UHRF2, a Ubiquitin E3 Ligase, Acts as a Small Ubiquitin-like Modifier E3 Ligase for Zinc Finger Protein 131

BTB-ZF Protein Znf131 Regulates Cell Growth of Developing and Mature T Cells

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