Cerd4, third member of the d4 gene family: expression and organization of genomic locus

Ninkina, Natalia; Мерцалов, И. Б.; Куликова, Д. А.; Alimova-Kost, Maria V.; Симонова, О. Б.; Korochkin, L. I.; Sl, Kiselev; Buchman, Vladimir L.

doi:10.1007/s00335-001-3039-1

Cited by 17 publications

(10 citation statements)

References 16 publications

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“…Three subtypes (DPF1, DPF2, and DPF3) have been identified, and they are evolutionarily conserved from nematodes to human. DPF2 is widely expressed (30), whereas DPF1 expression is restricted to neuronal systems, and DPF3 is restricted to retina and cerebellum (31,32).…”

Section: Purification and Identification Of Err␣-associated Proteins-mentioning

confidence: 99%

Double PHD Fingers Protein DPF2 Recognizes Acetylated Histones and Suppresses the Function of Estrogen-related Receptor α through Histone Deacetylase 1

Matsuyama

Takada

Yokoyama

et al. 2010

Journal of Biological Chemistry

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Estrogen-related receptor ␣ (ERR␣) is a member of the nuclear receptor superfamily and regulates many physiological functions, including mitochondrial biogenesis and lipid metabolism. ERR␣ enhances the transactivation function without endogenous ligand by associating with coactivators such as peroxisome proliferator-activated receptor ␥ coactivator 1 ␣ and ␤ (PGC-1␣ and -␤) and members of the steroid receptor coactivator family. However, the molecular mechanism by which the transactivation function of ERR␣ is converted from a repressive state to an active state is poorly understood. Here we used biochemical purification techniques to identify ERR␣-associated proteins in HeLa cells stably expressing ERR␣. Interestingly, we found that double PHD fingers protein DPF2/BAF45d suppressed PGC-1␣-dependent transactivation of ERR␣ by recognizing acetylated histone H3 and associating with HDAC1. DPF2 directly bound to ERR␣ and suppressed the transactivation function of nuclear receptors such as androgen receptor. DPF2 was recruited to ERR target gene promoters in myoblast cells, and knockdown of DPF2 derepressed the level of mRNA expressed by target genes of ERR␣. These results show that DPF2 acts as a nuclear receptor-selective co-repressor for ERR␣ by associating with both acetylated histone H3 and HDAC1.Nuclear receptors (NRs) 3 play pivotal roles during the development of vertebrates and in diverse physiological events in adults (1, 2). NRs constitute a gene superfamily and act as transcription factors. For most members of the NR superfamily, the transcriptional function is dependent on binding of lipophilic ligands such as steroid hormones and fat-soluble vitamins. The other subset of NRs is considered an orphan receptor, as physiologically relevant ligands remain to be identified. Orphan receptors are constitutively active or repressive transcription factors; however, their potency in transcriptional regulation appears to be dependent on cell types and the promoter context (3).For ligand-dependent transcriptional controls by nuclear steroid/vitamin receptors, several distinct classes of transcriptional co-regulators-co-regulator complexes are indispensable in addition to basic transcription machinery to reorganize chromatin state (4). Transcriptional co-regulators for NRs can be divided into two classes in terms of chromatin reorganization (5-7). One class consists of histone-modifying enzymes that reversibly modify the N-terminal tails of histone proteins (8, 9). For example, acetylation and methylation at histone H3K4 and H3K36 are chromatin-activating modifications and support transcriptional activation by NRs (8, 10, 11). In contrast, transcriptional repression by NRs is coupled with inactivating modifications like deacetylation and methylation at histone H3K9 and H3K27. Accordingly, cognate histone modifying enzymes serve as NR co-regulators.The other class of transcriptional co-regulators are chromatin remodeling factors that directly reorganize nucleosomal arrays through ATP hydrolysis (11). Chromatin remod...

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Section: Purification and Identification Of Err␣-associated Proteins-mentioning

confidence: 99%

Double PHD Fingers Protein DPF2 Recognizes Acetylated Histones and Suppresses the Function of Estrogen-related Receptor α through Histone Deacetylase 1

Matsuyama

Takada

Yokoyama

et al. 2010

Journal of Biological Chemistry

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“…Importantly, transactivation mediated through RelA/p50 (Fig. 1C, lanes 14 -18 compared with lane 13), RelB/p52 (lanes 20 -24 compared with lane 19), and c-Rel/p50 (lanes 8 -12 compared with lane 7) was enhanced by the endogenous expression of any of the five candidate proteins (lanes [7][8][9][10][11][12][13][14][15][16][17][18][19][20][21][22][23][24]. No significant differences were found among these five proteins in terms of the enhancement of any of the three NF-B dimers, suggesting that all potentially function as co-activators of NF-B in any context, at least when expressed at high levels.…”

Section: High Expression Of Each Member Of the D4 Family And Phf10mentioning

confidence: 99%

Double Plant Homeodomain (PHD) Finger Proteins DPF3a and -3b Are Required as Transcriptional Co-activators in SWI/SNF Complex-dependent Activation of NF-κB RelA/p50 Heterodimer

Ishizaka

Mizutani

Kobayashi

et al. 2012

Journal of Biological Chemistry

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Background:The NF-B dimer, RelA/p50, often requires the SWI/SNF complex for its transactivation function, but its molecular mechanisms remain elusive. Results: The NF-B canonical pathway induced by TNF-␣ is DPF3a/b-and SWI/SNF-dependent for some promoters. Conclusion: DPF3a and DPF3b are effective linkers for the SWI/SNF complex and RelA/p50. Significance: The NF-B⅐DPF3a/b⅐SWI/SNF complex would be an effective platform for promoter-specific transactivation.

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“…We also found that semen progressive motility (Grade a + b) was greatly reduced in CT heterozygotes ( P = 0.0003) and the concentration of semen in CT heterozygotes was also low ( P = 0.0319). DPF3 encodes a member of the D4 protein family of zinc finger proteins which is implicated as an epigenetic factor specifically binding acetylated and methylated lysine residues of histone 3 and histone 4 to provide easy access of transcription factors to DNA 1516…”

Section: Discussionmentioning

confidence: 99%

Strong association of SLC1A1 and DPF3 gene variants with idiopathic male infertility in Han Chinese

et al. 2017

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Male infertility is a multifactorial syndrome encompassing a wide variety of disorders. In recent years, several genome-wide single-nucleotide polymorphism (SNP) association studies (GWAS) have been performed on azoospermia and/or oligozoospermia in different populations including two GWAS on nonobstructive azoospermia in China; however, the association of SNPs with idiopathic male infertility, especially asthenozoospermia and oligozoospermia, and their correlation with semen parameters are still not clear. To investigate genetic variants associated with idiopathic male infertility (asthenozoospermia, oligozoospermia, and oligoasthenozoospermia) in Chinese Han people, 20 candidate SNPs were selected from GWAS results and genotyped using the Sequenom MassARRAY assay. A total of 136 subfertile men and 456 healthy fertile men were recruited. rs6476866 in SLC1A1 (P = 1.919E-4, OR = 0.5905, 95% CI: 0.447–0.78) and rs10129954 in DPF3 (P = 0.0023, OR = 2.199, 95% CI: 1.311–3.689) were strongly associated with idiopathic male infertility. In addition, positive associations were observed between asthenozoospermia and rs215702 in LSM5 (P = 0.0016, OR = 1.479, 95% CI: 1.075–2.033) and between oligoasthenozoospermia and rs2477686 in PEX10 (P = 0.0011, OR = 2.935, 95% CI: 1.492–5.775). In addition, six SNPs (rs215702 in LSM5, rs6476866 in SLC1A1, rs10129954 in DPF3, rs1801133 in MTHFR, rs2477686 in PEX10, and rs10841496 in PED3A) were significantly correlated with semen quality alterations. Our results suggest that idiopathic male infertility in different ethnic groups may share the same mechanism or pathway. Cohort expansion and further mechanistic studies on the role of genetic factors that influence spermatogenesis and sperm progressive motility are suggested.

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Cerd4, third member of the d4 gene family: expression and organization of genomic locus

Cited by 17 publications

References 16 publications

Double PHD Fingers Protein DPF2 Recognizes Acetylated Histones and Suppresses the Function of Estrogen-related Receptor α through Histone Deacetylase 1

Double PHD Fingers Protein DPF2 Recognizes Acetylated Histones and Suppresses the Function of Estrogen-related Receptor α through Histone Deacetylase 1

Double Plant Homeodomain (PHD) Finger Proteins DPF3a and -3b Are Required as Transcriptional Co-activators in SWI/SNF Complex-dependent Activation of NF-κB RelA/p50 Heterodimer

Strong association of SLC1A1 and DPF3 gene variants with idiopathic male infertility in Han Chinese

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