Search

Your search keyword '"C. Voelker"' showing total 2 results
Start Over Author "C. Voelker" Journal cell reports
2 results on '"C. Voelker"'

1. ZMYND8 Co-localizes with NuRD on Target Genes and Regulates Poly(ADP-Ribose)-Dependent Recruitment of GATAD2A/NuRD to Sites of DNA Damage

Author

Cornelia G. Spruijt, Martijn S. Luijsterburg, Roberta Menafra, Rik G.H. Lindeboom, Pascal W.T.C. Jansen, Raghu Ram Edupuganti, Marijke P. Baltissen, Wouter W. Wiegant, Moritz C. Voelker-Albert, Filomena Matarese, Anneloes Mensinga, Ina Poser, Harmjan R. Vos, Hendrik G. Stunnenberg, Haico van Attikum, and Michiel Vermeulen

Subjects
NuRD, ZMYND8, interaction proteomics, next-generation sequencing, gene expression, DNA damage, chromatin, GATAD2A, Biology (General), QH301-705.5
Abstract

NuRD (nucleosome remodeling and histone deacetylase) is a versatile multi-protein complex with roles in transcription regulation and the DNA damage response. Here, we show that ZMYND8 bridges NuRD to a number of putative DNA-binding zinc finger proteins. The MYND domain of ZMYND8 directly interacts with PPPLΦ motifs in the NuRD subunit GATAD2A. Both GATAD2A and GATAD2B exclusively form homodimers and define mutually exclusive NuRD subcomplexes. ZMYND8 and NuRD share a large number of genome-wide binding sites, mostly active promoters and enhancers. Depletion of ZMYND8 does not affect NuRD occupancy genome-wide and only slightly affects expression of NuRD/ZMYND8 target genes. In contrast, the MYND domain in ZMYND8 facilitates the rapid, poly(ADP-ribose)-dependent recruitment of GATAD2A/NuRD to sites of DNA damage to promote repair by homologous recombination. Thus, these results show that a specific substoichiometric interaction with a NuRD subunit paralogue provides unique functionality to distinct NuRD subcomplexes.

Published
2016
Full Text
View/download PDF

2. ZMYND8 Co-localizes with NuRD on Target Genes and Regulates Poly(ADP-Ribose)-Dependent Recruitment of GATAD2A/NuRD to Sites of DNA Damage

Author

Marijke P. Baltissen, Raghu Ram Edupuganti, Michiel Vermeulen, Rik G.H. Lindeboom, Martijn S. Luijsterburg, Cornelia G. Spruijt, Roberta Menafra, Filomena Matarese, Hendrik G. Stunnenberg, Harmjan R. Vos, Anneloes Mensinga, Moritz C. Voelker-Albert, Haico van Attikum, Wouter W. Wiegant, Pascal W.T.C. Jansen, and Ina Poser

Subjects
0301 basic medicine, Poly Adenosine Diphosphate Ribose, DNA Repair, DNA damage, Protein subunit, Biology, GATA Transcription Factors, General Biochemistry, Genetics and Molecular Biology, 03 medical and health sciences, Protein Domains, NuRD, GATAD2A, ZMYND8, Nucleosome, Humans, Protein Interaction Domains and Motifs, Amino Acid Sequence, Enhancer, Promoter Regions, Genetic, Molecular Biology, GeneralLiterature_REFERENCE(e.g.,dictionaries,encyclopedias,glossaries), lcsh:QH301-705.5, Zinc finger, Genetics, Genome, Human, Proteomics and Chromatin Biology, Tumor Suppressor Proteins, Mi-2/NuRD complex, Cell biology, Chromatin, Repressor Proteins, Protein Subunits, 030104 developmental biology, Enhancer Elements, Genetic, HEK293 Cells, lcsh:Biology (General), gene expression, chromatin, next-generation sequencing, Histone deacetylase, HeLa Cells, Mi-2 Nucleosome Remodeling and Deacetylase Complex, Protein Binding, interaction proteomics
Abstract

SummaryNuRD (nucleosome remodeling and histone deacetylase) is a versatile multi-protein complex with roles in transcription regulation and the DNA damage response. Here, we show that ZMYND8 bridges NuRD to a number of putative DNA-binding zinc finger proteins. The MYND domain of ZMYND8 directly interacts with PPPLΦ motifs in the NuRD subunit GATAD2A. Both GATAD2A and GATAD2B exclusively form homodimers and define mutually exclusive NuRD subcomplexes. ZMYND8 and NuRD share a large number of genome-wide binding sites, mostly active promoters and enhancers. Depletion of ZMYND8 does not affect NuRD occupancy genome-wide and only slightly affects expression of NuRD/ZMYND8 target genes. In contrast, the MYND domain in ZMYND8 facilitates the rapid, poly(ADP-ribose)-dependent recruitment of GATAD2A/NuRD to sites of DNA damage to promote repair by homologous recombination. Thus, these results show that a specific substoichiometric interaction with a NuRD subunit paralogue provides unique functionality to distinct NuRD subcomplexes.

Published
2016

Catalog

Books, media, physical & digital resources
See catalog results