The Drosophila methyl-DNA binding protein MBD2/3 interacts with the NuRD complex via p55 and MI-2

Marhold, J.; Brehm, Alexander; Kramer, Katja

doi:10.1186/1471-2199-5-20

Cited by 35 publications

(10 citation statements)

References 34 publications

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“…Several laboratories also report the association of GATAD2A and GATAD2B (also known as p66α and p66β) to the NuRD complex 8-10 . p66α, p66β RBAp46 and RBAp48 subunits are thought to be structural components of the NuRD complex and have been shown to directly associate with histone tails 11-13 . The MBD and MTA subunits, on the other hand, are implicated in targeting the complex to different genomic locations by associating with methylated DNA 14 or with transcription factors 15 , respectively.…”

Section: Biology and Function Of The Nurd Complexmentioning

confidence: 99%

Cancer biology and NuRD: a multifaceted chromatin remodelling complex

2011

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The nucleosome remodeling and deacetylase (NuRD; also known as Mi-2) complex regulates gene expression at the level of chromatin. The NuRD complex has been identified – using both genetic and molecular analyses – as a key determinant of differentiation in mouse embryonic stem cells and during development in various model systems. Similar to other chromatin remodelers, such as SWI/SNF and polycomb complexes, NuRD has also been implicated in the regulation of transcriptional events integral to oncogenesis and cancer progression. Emerging molecular details regarding recruitment of NuRD to specific loci during development and modulation of these events in cancer are used to illustrate how inappropriate localization of the complex could contribute to tumor biology.

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Section: Biology and Function Of The Nurd Complexmentioning

confidence: 99%

Cancer biology and NuRD: a multifaceted chromatin remodelling complex

2011

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“…Although the role of GR is unclear, binding of MBD to cytosine (methylated at position 5) within a CpG dinucleotide (mCpG) is well documented 45; 46; 48; 49 . TRD of Drosophila MBD2 is involved in the interaction with p55, a Drosophila homolog of RBBP7/4 50 . The coiled-coil motif associates with p66α (see p66α below) 51; 52 .…”

Section: Mbd2/3mentioning

confidence: 99%

The NuRD architecture

Allen

Wade

Kutateladze

2013

Cell. Mol. Life Sci.

164

161

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The nucleosome remodeling and deacetylase (NuRD) complex regulates chromatin organization, gene transcription, genomic stability and developmental signaling. NuRD has a unique dual enzymatic activity, containing an ATPase and a histone deacetylase (HDAC) among its six core subunits. Recent studies indicate that NuRD composition and the interplay between subunits may dictate the diverse functions of the complex. In this review, we examine the structures and biological roles of the NuRD subunits and discuss new avenues of research to advance our understanding of the NuRD-mediated signaling network.

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“…In Drosophila , the existence of a NuRD complex has been strongly suggested by several interaction studies [6], [7], [8], [9], [10]. Recently, a new containing dMi-2 protein complex, dMec, was characterized in Drosophila .…”

Section: Introductionmentioning

confidence: 99%

Different Mi-2 Complexes for Various Developmental Functions in Caenorhabditis elegans

et al. 2010

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Biochemical purifications from mammalian cells and Xenopus oocytes revealed that vertebrate Mi-2 proteins reside in multisubunit NuRD (Nucleosome Remodeling and Deacetylase) complexes. Since all NuRD subunits are highly conserved in the genomes of C. elegans and Drosophila, it was suggested that NuRD complexes also exist in invertebrates. Recently, a novel dMec complex, composed of dMi-2 and dMEP-1 was identified in Drosophila. The genome of C. elegans encodes two highly homologous Mi-2 orthologues, LET-418 and CHD-3. Here we demonstrate that these proteins define at least three different protein complexes, two distinct NuRD complexes and one MEC complex. The two canonical NuRD complexes share the same core subunits HDA-1/HDAC, LIN-53/RbAp and LIN-40/MTA, but differ in their Mi-2 orthologues LET-418 or CHD-3. LET-418 but not CHD-3, interacts with the Krüppel-like protein MEP-1 in a distinct complex, the MEC complex. Based on microarrays analyses, we propose that MEC constitutes an important LET-418 containing regulatory complex during C. elegans embryonic and early larval development. It is required for the repression of germline potential in somatic cells and acts when blastomeres are still dividing and differentiating. The two NuRD complexes may not be important for the early development, but may act later during postembryonic development. Altogether, our data suggest a considerable complexity in the composition, the developmental function and the tissue-specificity of the different C. elegans Mi-2 complexes.

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The Drosophila methyl-DNA binding protein MBD2/3 interacts with the NuRD complex via p55 and MI-2

Cited by 35 publications

References 34 publications

Cancer biology and NuRD: a multifaceted chromatin remodelling complex

Cancer biology and NuRD: a multifaceted chromatin remodelling complex

The NuRD architecture

Different Mi-2 Complexes for Various Developmental Functions in Caenorhabditis elegans

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