The Human Enhancer Blocker CTC-binding Factor Interacts with the Transcription Factor Kaiso

Defossez, Pierre‐Antoine; Kelly, Kevin F.; Filion, Guillaume J.; Pérez‐Torrado, Roberto; Magdinier, Frédérique; Menoni, Hervé; Nordgaard, Curtis L.; Daniel, Juliet M.; Gilson, Éric

doi:10.1074/jbc.m510802200

Cited by 79 publications

(56 citation statements)

References 45 publications

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“…Radiolabeled ZBTB4 was produced by in vitro transcription and translation of plasmid pSG5-ZBTB4 using rabbit reticulocyte lysate (TNT, Promega, Madison, WI, USA). The pulldown was then performed as described earlier (Defossez et al, 2005).…”

Section: Two-hybrid Screeningmentioning

confidence: 99%

The human protein kinase HIPK2 phosphorylates and downregulates the methyl-binding transcription factor ZBTB4

et al. 2009

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HIPK2 is a eukaryotic Serine-Threonine kinase that controls cellular proliferation and survival in response to exogenous signals. Here, we show that the human transcription factor ZBTB4 is a new target of HIPK2. The two proteins interact in vitro, colocalize and associate in vivo, and HIPK2 phosphorylates several conserved residues of ZBTB4. Overexpressing HIPK2 causes the degradation of ZBTB4, whereas overexpressing a kinasedeficient mutant of HIPK2 has no effect. The chemical activation of HIPK2 also decreases the amount of ZBTB4 in cells. Conversely, the inhibition of HIPK2 by drugs or by RNA interference causes a large increase in ZBTB4 levels. This negative regulation of ZBTB4 by HIPK2 occurs under normal conditions of cell growth. In addition, the degradation is increased by DNA damage. These findings have two consequences. First, we have recently shown that ZBTB4 inhibits the transcription of p21. Therefore, the activation of p21 by HIPK2 is twopronged: stimulation of the activator p53, and simultaneous repression of the inhibitor ZBTB4. Second, ZBTB4 is also known to bind methylated DNA and repress methylated sequences. Consequently, our findings raise the possibility that HIPK2 might influence the epigenetic regulation of gene expression at loci that remain to be identified.

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Section: Two-hybrid Screeningmentioning

confidence: 99%

The human protein kinase HIPK2 phosphorylates and downregulates the methyl-binding transcription factor ZBTB4

et al. 2009

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“…Co-association events such as those with the histone deacetylase SIN3 [54], the thyroid hormone receptor [55], nucleophosmin [56], Kaiso [57] and the DEAD-box RNA helicase p68 with associated non-coding RNA [58] have been implicated in its insulator function. Interestingly, the p68 RNA -protein complex appears required for positioning cohesin at the CTCF sites of the H19-Igf2 ICR [58].…”

Section: Ctcf and Other Binding Partnersmentioning

confidence: 99%

CTCF: the protein, the binding partners, the binding sites and their chromatin loops

Holwerda

Laat

2013

Phil. Trans. R. Soc. B

200

170

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CTCF has it all. The transcription factor binds to tens of thousands of genomic sites, some tissue-specific, others ultra-conserved. It can act as a transcriptional activator, repressor and insulator, and it can pause transcription. CTCF binds at chromatin domain boundaries, at enhancers and gene promoters, and inside gene bodies. It can attract many other transcription factors to chromatin, including tissue-specific transcriptional activators, repressors, cohesin and RNA polymerase II, and it forms chromatin loops. Yet, or perhaps therefore, CTCF's exact function at a given genomic site is unpredictable. It appears to be determined by the associated transcription factors, by the location of the binding site relative to the transcriptional start site of a gene, and by the site's engagement in chromatin loops with other CTCF-binding sites, enhancers or gene promoters. Here, we will discuss genome-wide features of CTCF binding events, as well as locus-specific functions of this remarkable transcription factor.

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“…10 A significant amount of data indicates that BTB domains are involved in the recruitment of non-BTB-containing regulator proteins. [11][12][13] Another set of experiments have shown that BTB domains of different proteins in some cases can specifically interact with each other, but it is unknown how such interactions proceed. Rarely, heterodimerization of two different BTBs has been observed.…”

Section: Introductionmentioning

confidence: 99%

Drosophila BTB/POZ Domains of “ttk Group” Can Form Multimers and Selectively Interact with Each Other

Bonchuk

Denisov

Georgiev

et al. 2011

Journal of Molecular Biology

104

109

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Edited by M. GottesmanKeywords: GAGA; BTB domain; Mod(mdg4); CP190; chromatin insulatorThe BTB (bric-a-brac, tramtrack and broad complex)/POZ (poxvirus and zinc finger) domain is a conserved protein-protein interaction motif contained in a variety of transcription factors involved in development, chromatin remodeling, insulator activity, and carcinogenesis. All wellstudied mammalian BTB domains form obligate homodimers and, rarely, tetramers. Only the BTB domain of the Drosophila GAGA factor (GAF) has been shown to exist as higher-order multimers. The BTB domain of GAF belongs to the "ttk group" that contains several highly conserved sequences not found in other BTB domains. Here, we have shown by size-exclusion chromatography, chemical cross-linking, and nondenaturing PAGE that four additional BTB domains of the ttk group-Batman, Mod(mdg4), Pipsqueak, and Tramtrack-can form multimers, like GAF. Interestingly, the BTB domains of GAF and Batman have formed a wide range of complexes and interacted in the yeast two-hybrid assay with other BTB domains tested. In contrast, the BTB domains of Mod(mdg4), Pipsqueak, and Tramtrack have formed stable high-order multimer complexes and failed to interact with each other. The BTB domain of Drosophila CP190 protein does not belong to the ttk group. This BTB domain has formed stable dimers and has not interacted with domains of the ttk group. Previously, it was suggested that GAF oligomerization into higher-order complexes facilitates long-range activation by providing a protein bridge between an enhancer and a promoter. Unexpectedly, experiments in the Drosophila model system have not supported the role of GAF in organization of longdistance interaction between the yeast GAL4 activator and the white promoter.© 2011 Elsevier Ltd. All rights reserved. IntroductionThe BTB (bric-a-brac, tramtrack and broad complex) domain [also known as the POZ (poxvirus and zinc finger) domain] is a versatile protein-protein interaction motif that participates in a wide range of cellular functions, including transcription regulation (for review, see Ref. 1 ). Transcription factors with a BTB domain at the N-terminus comprise a large important class of molecules involved in development and carcinogenesis. As shown in crystallographic studies,

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The Human Enhancer Blocker CTC-binding Factor Interacts with the Transcription Factor Kaiso

Cited by 79 publications

References 45 publications

The human protein kinase HIPK2 phosphorylates and downregulates the methyl-binding transcription factor ZBTB4

The human protein kinase HIPK2 phosphorylates and downregulates the methyl-binding transcription factor ZBTB4

CTCF: the protein, the binding partners, the binding sites and their chromatin loops

Drosophila BTB/POZ Domains of “ttk Group” Can Form Multimers and Selectively Interact with Each Other

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