Knockdown of RBBP7 unveils a requirement of histone deacetylation for CPC function in mouse oocytes

Balboula, Ahmed Z.; Stein, Paula; Schultz, Richard M.; Schindler, Karen

doi:10.4161/cc.27410

Cited by 29 publications

(37 citation statements)

References 48 publications

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“…Perturbing RBBP7 function phenocopies oocytes treated with trichostatin A (TSA), a global inhibitor of HDACs. These phenotypes include chromosome misalignment, cytokinesis defects, and aneuploidy at metaphase (Met) II [7]. Furthermore, we found that the changes in histone acetylation caused delocalization of the chromosomal passenger complex (CPC), which is consistent with the observed phenotypes.…”

Section: Introductionsupporting

confidence: 73%

“…The DNA linearization and purification were carried out as described previously [7,15]. In vitro transcription to generate Aurka-Gfp, Aurkc-Gfp, and H2b-mCherry was carried out using the mMessage mMachine T7 Ultra Kit (Ambion).…”

Section: In Vitro Crna Synthesismentioning

confidence: 99%

“…Recently, we identified retinoblastoma binding protein P46 (RBBP7) as a regulator of HDAC activity in mouse oocytes [7]. Perturbing RBBP7 function phenocopies oocytes treated with trichostatin A (TSA), a global inhibitor of HDACs.…”

Section: Introductionmentioning

confidence: 99%

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RBBP4 Regulates Histone Deacetylation and Bipolar Spindle Assembly During Oocyte Maturation in the Mouse1

Balboula¹,

Stein²,

Schultz³

et al. 2015

Biology of Reproduction

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During meiosis I (MI) in oocytes, the maturation-associated decrease of histone acetylation is critical for normal meiotic progression and accurate chromosome segregation. RBBP4 is a component of several different histone deacetylase containing chromatin-remodeling complexes, but RBBP4's role in regulating MI is not known. Depleting RBBP4 in mouse oocytes resulted in multipolar spindles at metaphase (Met) I with subsequent perturbed meiotic progression and increased incidence of abnormal spindles, chromosome misalignment, and aneuploidy at Met II. We attribute these defects to improper deacetylation of histones because histones H3K4, H4K8, H4K12, and H4K16 were hyperacetylated in RBBP4-depleted oocytes. Importantly, we show that RBBP4-mediated histone deacetylation is essential for regulating bipolar spindle assembly, at least partially, through promoting Aurora kinase (AURK) C function. To our knowledge, these results are the first to identify RBBP4 as a regulator of histone deacetylation during oocyte maturation, and they provide evidence that deacetylation is required for bipolar spindle assembly through AURKC.

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Section: Introductionsupporting

confidence: 73%

Section: In Vitro Crna Synthesismentioning

confidence: 99%

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RBBP4 Regulates Histone Deacetylation and Bipolar Spindle Assembly During Oocyte Maturation in the Mouse1

Balboula¹,

Stein²,

Schultz³

et al. 2015

Biology of Reproduction

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“…Knockdown of retinoblastoma binding protein P46 (RBAP46, also called RBBP7), an integral subunit in HDAC1/2-containing complexes, results in similar phenotypes including H4K16 hyperacetylation and missegregation of chromosomes to that observed in Hdac2 mutant eggs. 76 Immunoblot analysis revealed that RBBP7 protein level increases significantly from GV to MII eggs; 76 this maturation-associated increase in RBBP7 protein is well correlated with activation of HDAC2. In addition, RBBP7 colocalizes with chromosomes during meiosis division, 76 suggesting that it may promote HDAC2 association with chromatin and thereby facilitate deacetylation of H4K16.…”

Section: Hdac2 Regulates Chromosome Segregation and Kinetochore Functmentioning

confidence: 88%

“…76 Immunoblot analysis revealed that RBBP7 protein level increases significantly from GV to MII eggs; 76 this maturation-associated increase in RBBP7 protein is well correlated with activation of HDAC2. In addition, RBBP7 colocalizes with chromosomes during meiosis division, 76 suggesting that it may promote HDAC2 association with chromatin and thereby facilitate deacetylation of H4K16.…”

Section: Hdac2 Regulates Chromosome Segregation and Kinetochore Functmentioning

confidence: 88%

HDAC1 and HDAC2 in mouse oocytes and preimplantation embryos: Specificity versus compensation

Schultz

2016

Cell Death Differ

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Oocyte and preimplantation embryo development entail dynamic changes in chromatin structure and gene expression, which are regulated by a number of maternal and zygotic epigenetic factors. Histone deacetylases (HDACs), which tighten chromatin structure, repress transcription and gene expression by removing acetyl groups from histone or non-histone proteins. HDAC1 and HDAC2 are two highly homologous Class I HDACs and display compensatory or specific roles in different cell types or in response to different stimuli and signaling pathways. We summarize here the current knowledge about the functions of HDAC1 and HDAC2 in regulating histone modifications, transcription, DNA methylation, chromosome segregation, and cell cycle during oocyte and preimplantation embryo development. What emerges from these studies is that although HDAC1 and HDAC2 are highly homologous, HDAC2 is more critical than HDAC1 for oocyte development and reciprocally, HDAC1 is more critical than HDAC2 for preimplantation development. In eukaryotes, DNA is organized into a highly ordered nucleoprotein assembly called chromatin, whose fundamental unit is the nucleosome. The nucleosome consists of 146 bp of DNA wrapped around a histone core comprised of two molecules each of histones H2A, H2B, H3 and H4. Histone H1 is bound to linker DNA between nucleosomes. 1,2 Histones are subject to multiple post-translational modifications (PTMs), including acetylation, methylation, ubiquitylation, phosphorylation, and sumoylation. These PTMs determine open and closed chromatin conformations, which, in turn, regulate the differential access and recruitment of transcription factors and other regulatory chromatin-binding proteins to DNA. 3-5 Among these histone modifications, histone acetylation is the most well-studied modification, which occurs at the ε-amino groups of evolutionarily conserved lysine residues located at the N termini. Although all core histones are acetylated in vivo, modifications of histones H3 and H4 are more extensively characterized than those of H2A and H2B. Abbreviations: HDAC, histone deacetylase; HAT, histone acetyl transferase; PTM, post-translational modification; KDAC, lysine deacetylase; TSA, trichostatin A; NAD + , nicotinamide adenine dinucleotide; HAD, HDAC association domain ; GVBD, germinal vesicle breakdown; ChIP-seq, chromatin immunoprecipitation sequencing; TFIID, transcription factor II D; YY1, yin yang 1; Pol II CTD S2, serine 2 within the RNApolymerase II C-terminal domain; H3K4, lysine 4 of histone 3; H3K9, lysine 9 of histone 3; H4K16, lysine 16 of histone 4; SIRT, NAD-dependent deacetylase sirtuin; TBP2, TATA-binding protein 2; DNMT, DNA methyltransferases; RBAP46, retinoblastoma binding protein P46; RNAi, RNA interference; aa, amino acidic; BrUTP, 5-Bromouridine 5′-triphosphate; qRT-PCR, quantitative reverse transcription polymerase chain reaction;

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RNF20 Regulates Oocyte Meiotic Spindle Assembly by Recruiting TPM3 to Centromeres and Spindle Poles

Wang,

Liu,

et al. 2024

Advanced Science

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Previously a ring finger protein 20 (RNF20) is found to be essential for meiotic recombination and mediates H2B ubiquitination during spermatogenesis. However, its role in meiotic division is still unknown. Here, it is shown that RNF20 is localized at both centromeres and spindle poles, and it is required for oocyte acentrosomal spindle organization and female fertility. RNF20‐depleted oocytes exhibit severely abnormal spindle and chromosome misalignment caused by defective bipolar organization. Notably, it is found that the function of RNF20 in spindle assembly is not dependent on its E3 ligase activity. Instead, RNF20 regulates spindle assembly by recruiting tropomyosin3 (TPM3) to both centromeres and spindle poles with its coiled‐coil motif. The RNF20‐TPM3 interaction is essential for acentrosomal meiotic spindle assembly. Together, the studies uncover a novel function for RNF20 in mediating TPM3 recruitment to both centromeres and spindle poles during oocyte spindle assembly.

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Knockdown of RBBP7 unveils a requirement of histone deacetylation for CPC function in mouse oocytes

Cited by 29 publications

References 48 publications

RBBP4 Regulates Histone Deacetylation and Bipolar Spindle Assembly During Oocyte Maturation in the Mouse1

RBBP4 Regulates Histone Deacetylation and Bipolar Spindle Assembly During Oocyte Maturation in the Mouse1

HDAC1 and HDAC2 in mouse oocytes and preimplantation embryos: Specificity versus compensation

RNF20 Regulates Oocyte Meiotic Spindle Assembly by Recruiting TPM3 to Centromeres and Spindle Poles

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