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Chromodomain helicase DNA binding protein 4

Mi-2beta, CHD4, chromodomain helicase DNA-binding protein 4
The product of this gene belongs to the SNF2/RAD54 helicase family. It represents the main component of the nucleosome remodeling and deacetylase complex and plays an important role in epigenetic transcriptional repression. Patients with dermatomyositis develop antibodies against this protein. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Histone, ATPase, CAN, CHD3, fibrillin-1
Papers on Mi-2beta
The N-terminal Region of Chromodomain Helicase DNA-binding Protein 4 (CHD4) Is Essential for Activity and Contains a High Mobility Group (HMG) Box-like-domain That Can Bind Poly(ADP-ribose).
New
Mackay et al., Cambridge, United Kingdom. In J Biol Chem, Feb 2016
Chromodomain Helicase DNA-binding protein 4 (CHD4) is a chromatin-remodeling enzyme that has been reported to regulate DNA-damage responses through its N-terminal region in a poly(ADP-ribose) polymerase-dependent manner.
Selective Recognition of H3.1K36 dimethylation / H4K16 acetylation facilitates the regulation of ATRA-responsive genes by putative chromatin reader ZMYND8.
New
Das et al., India. In J Biol Chem, Jan 2016
Overall, our study identifies that ZMYND8 has CHD4-independent functions in regulating gene expression through its modified histone binding ability.
A role for repressive complexes and H3K9 di-methylation in PRDM5-associated brittle cornea syndrome.
New
Manson et al., Boston, United States. In Hum Mol Genet, Jan 2016
We identify H3K9 di-methylation (H3K9me2) at these PRDM5-target genes in fibroblasts, and demonstrate that the BCS2 mutation p.Arg83Cys diminishes interaction of PRDM5 with repressive complexes, including NuRD complex protein CHD4, and the repressive chromatin interactor HP1BP3, by co-immunoprecipitation combined with mass spectrometry.
Acetyltransferase p300 collaborates with chromodomain helicase DNA-binding protein 4 (CHD4) to facilitate DNA double-strand break repair.
New
Zeng et al., Changchun, China. In Mutagenesis, Dec 2015
Previous studies have reported that histone acetyltransferase p300 and ATP-dependent chromatin remodeler chromodomain helicase DNA-binding protein 4 (CHD4) functions, respectively, in DNA double-strand breaks (DSBs) repair.
Predicting Response to Histone Deacetylase Inhibitors Using High-Throughput Genomics.
New
Huang et al., Chicago, United States. In J Natl Cancer Inst, Nov 2015
As a proof of concept, we also discovered a novel causative role for CHD4, a helicase involved in the histone deacetylase complex that is associated with poor clinical outcome.
Depletion of the chromatin remodeler CHD4 sensitizes AML blasts to genotoxic agents and reduces tumor formation.
New
Ginder et al., Richmond, United States. In Blood, Oct 2015
Chromodomain helicase DNA-binding protein 4 (CHD4) is an ATPase that alters the phasing of nucleosomes on DNA and has recently been implicated in DNA double-stranded break (DSB) repair.
Towards elucidating the stability, dynamics and architecture of the nucleosome remodeling and deacetylase complex by using quantitative interaction proteomics.
Review
New
Vermeulen et al., Nijmegen, Netherlands. In Febs J, May 2015
STRUCTURED DIGITAL ABSTRACT: MBD3 physically interacts with ZNF512B, HDAC1, ZMYND8, GATAD2B, SALL4, GATAD2A, ZNF592, MTA3, ZNF687, CDK2AP1, CHD3, ZNF532, HDAC2, MTA2, CHD4, MTA1, KPNA2, CHD5, RBBP4 and RBBP7 by pull down (View interaction) CDK2AP1 physically interacts with MBD3, MTA3, HDAC2, GATAD2A, CHD4, CDK2AP1, MTA2, HDAC1, MTA1, CHD3, GATAD2B, MBD2, RBBP4 and RBBP7 by pull down (View interaction) MBD3 physically interacts with MTA2, MTA3, RBBP4, RBBP7, HDAC2, HDAC1, CHD4, CHD3 and MTA1 by cross-linking study (View interaction).
CHD chromatin remodelling enzymes and the DNA damage response.
Review
Goodarzi et al., Calgary, Canada. In Mutat Res, 2013
We will first touch upon all four major chromatin remodelling enzyme families and then focus chiefly on the nine members of the Chromodomain, Helicase, DNA-binding (CHD) family, particularly CHD3, CHD4, CHD5 and CHD6.
CHD4 in the DNA-damage response and cell cycle progression: not so NuRDy now.
Review
Hendrich et al., Cambridge, United Kingdom. In Biochem Soc Trans, 2013
The CHD4 (chromodomain-helicase-DNA-binding 4) (or Mi-2β) protein is a founding component of the NuRD (nucleosome remodelling and deacetylation) complex.
Exome sequencing of serous endometrial tumors identifies recurrent somatic mutations in chromatin-remodeling and ubiquitin ligase complex genes.
Impact
Bell et al., Bethesda, United States. In Nat Genet, 2012
We identified high frequencies of somatic mutations in CHD4 (17%), EP300 (8%), ARID1A (6%), TSPYL2 (6%), FBXW7 (29%), SPOP (8%), MAP3K4 (6%) and ABCC9 (6%).
The PHD and chromo domains regulate the ATPase activity of the human chromatin remodeler CHD4.
GeneRIF
Laue et al., Cambridge, United Kingdom. In J Mol Biol, 2012
a three-dimensional structural model describing the overall shape and domain interactions of CHD4 and discuss the relevance of these for regulating the remodeling of chromatin by the NuRD complex.
Concerted action of the PHD, chromo and motor domains regulates the human chromatin remodelling ATPase CHD4.
GeneRIF
Mancini et al., Oxford, United Kingdom. In Febs Lett, 2012
Concerted action of the PHD, chromo and motor domains regulates the human chromatin remodelling ATPase CHD4
The chromatin-remodeling enzymes BRG1 and CHD4 antagonistically regulate vascular Wnt signaling.
GeneRIF
Griffin et al., Oklahoma City, United States. In Mol Cell Biol, 2012
Concomitant deletion of Chd4 and Brg1 rescued vascular abnormalities seen in Brg1 mutant yolk sacs to the same extent as LiCl treatment.
The nucleosome remodeling and deacetylase chromatin remodeling (NuRD) complex is required for peripheral nerve myelination.
GeneRIF
Svaren et al., Madison, United States. In J Neurosci, 2012
Chd4 is necessary to guide proper terminal differentiation of Schwann cells; the nucleosome remodeling and deacetylase (NURD) complex is a requisite factor in timely and stable peripheral chromatin remodeling.
Harnessing of the nucleosome-remodeling-deacetylase complex controls lymphocyte development and prevents leukemogenesis.
Impact
GeneRIF
Georgopoulos et al., Cambridge, United States. In Nat Immunol, 2012
activity of the Mi-2beta nucleosome-remodeling and histone-deacetylase (NuRD) complex was controlled by the Ikaros family of lymphoid lineage-determining proteins.
The Mi-2/NuRD complex: a critical epigenetic regulator of hematopoietic development, differentiation and cancer.
Review
Hagman et al., Denver, United States. In Epigenetics, 2009
Alternatively, the Mi-2beta ATPase subunit of Mi-2/NuRD can promote transcription.
Antagonistic interactions between Ikaros and the chromatin remodeler Mi-2beta determine silencer activity and Cd4 gene expression.
Impact
Georgopoulos et al., United States. In Immunity, 2007
Here, we revealed the antagonistic interplay between Ikaros and its associate the chromatin remodeler Mi-2beta during T cell development, as exemplified by the regulation of Cd4 expression.
The chromatin remodeler Mi-2beta is required for CD4 expression and T cell development.
Impact
Georgopoulos et al., United States. In Immunity, 2004
The chromatin remodeler Mi-2beta is highly expressed in thymocytes and is presumed to be a transcriptional repressor because of its presence in the nucleosome remodeling deacetylase (NuRD) complex.
Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex.
Impact
Schreiber et al., Cambridge, United States. In Nature, 1998
This activity is derived from the CHD3 and CHD4 proteins which contain helicase/ATPase domains found in SWI2-related chromatin remodelling factors, and facilitates the deacetylation of oligonucleosomal histones in vitro.
The dermatomyositis-specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities.
Impact
Reinberg et al., United States. In Cell, 1998
The complex contains the histone deacetylases HDAC1/2, histone-binding proteins, the dermatomyositis-specific autoantigen Mi2beta, a polypeptide related to the metastasis-associated protein 1, and a novel polypeptide of 32 kDa.
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