Btg2 Enhances Retinoic Acid-Induced Differentiation by Modulating Histone H4 Methylation and Acetylation

Passeri, Daniela; Marcucci, Antonella; Rizzo, Giovanni; Billi, Monia; Panigada, Maddalena; Leonardi, Luca; Tirone, Felice; Grignani, Francesco

doi:10.1128/mcb.01360-05

Cited by 58 publications

(56 citation statements)

References 56 publications

(64 reference statements)

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“…In addition, these proteins interact via leucine-rich motifs with yeast Caf1 (Pop2) or its human orthologues CNOT7 (hCaf1/Caf1a) and CNOT8 (hPop2/Caf1b/Calif), which contain RNA nuclease activities attributed to DEDD domains (Daugeron et al, 2001;Dupressoir et al, 2001;Clark et al, 2004;Viswanathan et al, 2004;Bianchin et al, 2005). The CNOT7 and CNOT8 proteins interact with members of the BTG/Tob family of antiproliferative proteins, which are implicated in mRNA turnover (Ezzeddine et al, 2007;Funakoshi et al, 2007;Mauxion et al, 2008) and transcription (Prevot et al, 2000;Yoshida et al, 2000;Tzachanis et al, 2001;Passeri et al, 2006;Ou et al, 2007). Consistent with their role in mRNA decay, combined depletion of CNOT7 and CNOT8 in human cells results in decreased deadenylation of bulk mRNA and stabilizes an unstable reporter mRNA (Schwede et al, 2008).…”

Section: Introductionmentioning

confidence: 76%

The Ccr4–Not Deadenylase Subunits CNOT7 and CNOT8 Have Overlapping Roles and Modulate Cell Proliferation

Aslam

Mittal

Koch

et al. 2009

MBoC

101

115

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Accurate gene expression requires the precise control of mRNA levels, which are determined by the relative rates of nuclear (pre-)mRNA synthesis and processing, and cytoplasmic mRNA turnover. A key step in mRNA degradation is the removal of the poly(A) tail, which involves several deadenylases including components of the Ccr4 -Not complex. Here, we focused on the role of the human paralogues CNOT7 (hCaf1/Caf1a) and CNOT8 (hPop2/Caf1b/Calif), which possess deadenylase activity mediated by DEDD nuclease domains. We show that efficient proliferation requires both subunits, although combined knockdown of CNOT7 and CNOT8 further reduces cell proliferation indicating partial redundancy between these proteins. Interestingly, the function of CNOT7 in cell proliferation partly depends on its catalytic activity. On the other hand, the interaction between CNOT7 and BTG2, a member of the antiproliferative BTG/Tob family involved in transcription and mRNA decay appears less important for proliferation of MCF7 cells, suggesting that CNOT7 does not function solely in conjunction with BTG2. Further analysis of gene expression profiles of CNOT7 and/or CNOT8 knockdown cells underscores the partial redundancy between these subunits and suggests that regulation of several genes, including repression of the antiproliferative genes MSMB and PMP22, by the Ccr4 -Not complex contributes to cell proliferation. INTRODUCTIONAccurate gene expression requires the precise control of mRNA levels that are determined by the relative rates of (pre-)mRNA synthesis and processing, and by mRNA turnover. Degradation of eukaryotic mRNA is initiated by the shortening and removal of the poly(A) tail by at least two different complexes containing distinct deadenylase subunits (Parker and Song, 2004;Garneau et al., 2007;Goldstrohm and Wickens, 2008). In both yeast and human cells, initial shortening of the poly(A) tail is carried out by Pan2, which forms a heterodimer with Pan3 (Brown et al., 1996;Boeck et al., 1998;Brown and Sachs, 1998;Uchida et al., 2004). Subsequent removal of poly(A) residues is achieved by Ccr4 -Not, a conserved complex, which contains about 10 subunits, including several deadenylase components (Tucker et al., 2001;Temme et al., 2004;Yamashita et al., 2005). The yeast Ccr4 protein and its human orthologues CNOT6 (hCcr4/Ccr4a) and CNOT6L (hCcr4-like/Ccr4b) contain an exonuclease/endonuclease/ phosphatase (EEP) domain that is responsible for the RNA nuclease activity (Dupressoir et al., 2001;Chen et al., 2002;Tucker et al., 2002;Morita et al., 2007). In addition, these proteins interact via leucine-rich motifs with yeast Caf1 (Pop2) or its human orthologues CNOT7 (hCaf1/Caf1a) and CNOT8 (hPop2/Caf1b/Calif), which contain RNA nuclease activities attributed to DEDD domains (Daugeron et al., 2001;Dupressoir et al., 2001;Clark et al., 2004;Viswanathan et al., 2004;Bianchin et al., 2005). The CNOT7 and CNOT8 proteins interact with members of the BTG/Tob family of antiproliferative proteins, which are implicated in mRNA turnover (Ezzeddine ...

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Section: Introductionmentioning

confidence: 76%

The Ccr4–Not Deadenylase Subunits CNOT7 and CNOT8 Have Overlapping Roles and Modulate Cell Proliferation

Aslam

Mittal

Koch

et al. 2009

MBoC

101

115

View full text Add to dashboard Cite

show abstract

“…Btg2 is also a putative direct target of RAR [174] and is induced by RA in neurula-stage embryos [175,176] and in various cell lines [174,177]. Btg2 decreases arginine methylation and lysine acetylation of histone H4 at RAR target genes, thus increasing the transcriptional activity of RAR [177]. Btg2 is expressed in differentiating neuroblasts [178] and promotes neuronal differentiation in PC12 cells [179].…”

Section: Downstream Effectors Of Retinoic Acid Signaling Related To Nmentioning

confidence: 99%

“…HoxA1-null ES cells are refractory to treatment with RA as measured by reduced expression of post-mitotic neuron markers (e.g., b-tubulin III, Nestin); RA sensitivity can be restored by rescue with HoxA1 cDNA [173]. Btg2 is also a putative direct target of RAR [174] and is induced by RA in neurula-stage embryos [175,176] and in various cell lines [174,177]. Btg2 decreases arginine methylation and lysine acetylation of histone H4 at RAR target genes, thus increasing the transcriptional activity of RAR [177].…”

Section: Downstream Effectors Of Retinoic Acid Signaling Related To Nmentioning

confidence: 99%

Retinoic acid signaling and neuronal differentiation

Janesick

Blumberg

2015

Cell. Mol. Life Sci.

235

173

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“…It is notable that whereas other SET1-like complexes have not been found to contain any H3K27 demethylases as integral subunits, with the identity of the H3K27 demethylases required for their functions being unknown, ASCOM does contain the H3K27 demethylase UTX as an integral subunit (7,8). Thus, we examined the role of UTX in transactivation of five direct RAR target genes that included p21, RAR-␤2, PDCD4 (for programmed cell death 4), IGFBP2 (for insulin-like growth factor binding protein 2), and BTG2 (for B-cell translocation gene 2) (5,(34)(35)(36). Notably, the knockdown of UTX by si-UTX RNA (24) profoundly compromised RA-mediated upregulation of expression of all five genes ( Fig.…”

Section: Identification Of a Novel Set1-like Complex Binding Site In H3mentioning

confidence: 99%

Histone H3K27 Trimethylation Inhibits H3 Binding and Function of SET1-Like H3K4 Methyltransferase Complexes

Kim

Tang

Shimada

et al. 2013

Molecular and Cellular Biology

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g Trimethylated histone H3 lysine 4 (H3K4) and H3K27 generally mark transcriptionally active and repressive chromatins, respectively. In most cell types, these two modifications are mutually exclusive, and this segregation is crucial for the regulation of gene expression. However, how this anticorrelation is achieved has not been fully understood. Here, we show that removal of the H3K27 trimethyl mark facilitates recruitment of SET1-like H3K4 methyltransferase complexes to their target genes by eliciting a novel interaction between histone H3 and two common subunits, WDR5 and RBBP5, of SET1-like complexes. Consistent with this result, H3K27 trimethylation destabilizes interactions of H3 with SET1-like complexes and antagonizes their ability to carry out H3K4 trimethylation of peptide (H3 residues 1 to 36), histone octamer, and mononucleosome substrates. Altogether, our studies reveal that H3K27 trimethylation of histone H3 represses a previously unrecognized interaction between H3 and SET1-like complexes. This provides an important mechanism that directs the anticorrelation between H3K4 and H3K27 trimethylation.T rimethylation of histone H3 at lysine 4 (H3K4me3) is a mark for active chromatin that counters the repressive chromatin milieu imposed by H3K9 and H3K27 methylation in higher eukaryotes (1). H3K4 trimethylation is primarily carried out by the vertebrate H3K4 methyltransferases SET1A/SET1B (SET1A/B) and MLL1 to MLL4, which form a family of related SET1-like complexes (2, 3). Each complex contains a unique H3K4 methyltransferase enzyme, complex-specific subunits, and a common subcomplex, consisting of RBBP5, ASH2L, WDR5, and DPY-30, that facilitates the H3K4 methyltransferase activity of SET1-like complexes (2, 3). We previously identified the first mammalian SET1-like complexes containing MLL3 and MLL4 (MLL3/4), which play essential roles in transactivation by retinoic acid receptor (RAR) and multiple other transcription factors (3)(4)(5). Unique subunits in these two complexes include PA1, PTIP, the H3K27 demethylase UTX, and the transcriptional coactivator ASC-2 (3, 4, 6-9). These complexes were originally named ASCOM (for ASC-2 complex)-MLL3 and ASCOM-MLL4 (4, 5).WDR5 was earlier reported to bind to K4-dimethylated H3 (10) and, in subsequent structural studies, to interact not only with dimethylated H3K4, by virtue of both water-mediated hydrogen bonding and the altered hydrophilicity of the modified K4, but also with the second arginine residue (H3R2) of H3 (11-14). The arginine methyltransferase PRMT6 catalyzes H3R2 dimethylation in vitro and controls global levels of H3R2 dimethylation in vivo (15,16). Of note, and as a paradigm for the present study, H3R2 methylation by PRMT6 is blocked by the presence of the H3K4 trimethyl mark, whereas the H3R2 methyl mark interferes with binding of WDR5 to the H3 tail and thus prevents H3K4 trimethylation by 16).It is well established that, in general, H3K4 trimethylation is inversely correlated with H3K27 trimethylation throughout the genome in most vertebrate...

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Btg2 Enhances Retinoic Acid-Induced Differentiation by Modulating Histone H4 Methylation and Acetylation

Cited by 58 publications

References 56 publications

The Ccr4–Not Deadenylase Subunits CNOT7 and CNOT8 Have Overlapping Roles and Modulate Cell Proliferation

The Ccr4–Not Deadenylase Subunits CNOT7 and CNOT8 Have Overlapping Roles and Modulate Cell Proliferation

Retinoic acid signaling and neuronal differentiation

Histone H3K27 Trimethylation Inhibits H3 Binding and Function of SET1-Like H3K4 Methyltransferase Complexes

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