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dc.contributor.author | Messina, Giovanni | |
dc.contributor.author | Atterrato, Maria Teresa | |
dc.contributor.author | Prozzillo, Yuri | |
dc.contributor.author | Piacentini, Lucia | |
dc.contributor.author | Losada, Ana | |
dc.contributor.author | Dimitri, Patrizio | |
dc.date.accessioned | 2019-03-07T11:48:14Z | |
dc.date.available | 2019-03-07T11:48:14Z | |
dc.date.issued | 2017-04-03 | |
dc.identifier.citation | Sci Rep. 2017;7:45022. | es_ES |
dc.identifier.issn | 2045-2322 | es_ES |
dc.identifier.uri | http://hdl.handle.net/20.500.12105/7299 | |
dc.description.abstract | The human Cranio Facial Development Protein 1 (Cfdp1) gene maps to chromosome 16q22.2-q22.3 and encodes the CFDP1 protein, which belongs to the evolutionarily conserved Bucentaur (BCNT) family. Craniofacial malformations are developmental disorders of particular biomedical and clinical interest, because they represent the main cause of infant mortality and disability in humans, thus it is important to understand the cellular functions and mechanism of action of the CFDP1 protein. We have carried out a multi-disciplinary study, combining cell biology, reverse genetics and biochemistry, to provide the first in vivo characterization of CFDP1 protein functions in human cells. We show that CFDP1 binds to chromatin and interacts with subunits of the SRCAP chromatin remodeling complex. An RNAi-mediated depletion of CFDP1 in HeLa cells affects chromosome organization, SMC2 condensin recruitment and cell cycle progression. Our findings provide new insight into the chromatin functions and mechanisms of the CFDP1 protein and contribute to our understanding of the link between epigenetic regulation and the onset of human complex developmental disorders. | es_ES |
dc.description.sponsorship | We are grateful to Tatsuya Hirano for gift of ISWI and H3p antibodies and to Ana Cuadrado for gift of anti-p18Hamlet antibody, pCS2-5xMyc-Arp6, pcDNA3-HA-H2A.Z and pcDNA3-HA-SRCAP plasmids. | es_ES |
dc.language.iso | eng | es_ES |
dc.publisher | Nature Publishing Group | es_ES |
dc.type.hasVersion | VoR | es_ES |
dc.rights.uri | http://creativecommons.org/licenses/by/4.0/ | * |
dc.subject.mesh | Adenosine Triphosphatases | es_ES |
dc.subject.mesh | Cell Line | es_ES |
dc.subject.mesh | Chromatin | es_ES |
dc.subject.mesh | Chromatin Assembly and Disassembly | es_ES |
dc.subject.mesh | Chromosomes | es_ES |
dc.subject.mesh | DNA-Binding Proteins | es_ES |
dc.subject.mesh | Gene Expression | es_ES |
dc.subject.mesh | HeLa Cells | es_ES |
dc.subject.mesh | Humans | es_ES |
dc.subject.mesh | Mitosis | es_ES |
dc.subject.mesh | Multiprotein Complexes | es_ES |
dc.subject.mesh | Phosphoproteins | es_ES |
dc.subject.mesh | Protein Binding | es_ES |
dc.subject.mesh | Protein Interaction Domains and Motifs | es_ES |
dc.subject.mesh | Protein Transport | es_ES |
dc.title | The human Cranio Facial Development Protein 1 (Cfdp1) gene encodes a protein required for the maintenance of higher-order chromatin organization | es_ES |
dc.type | journal article | es_ES |
dc.rights.license | Atribución 4.0 Internacional | * |
dc.identifier.pubmedID | 28367969 | es_ES |
dc.format.volume | 7 | es_ES |
dc.format.number | 1 | es_ES |
dc.format.page | 45022 | es_ES |
dc.identifier.doi | 10.1038/srep45022 | es_ES |
dc.description.peerreviewed | Sí | es_ES |
dc.identifier.e-issn | 2045-2322 | es_ES |
dc.relation.publisherversion | https://doi.org/ 10.1038/srep45022. | es_ES |
dc.identifier.journal | Scientific reports | es_ES |
dc.repisalud.institucion | CNIO | es_ES |
dc.repisalud.orgCNIO | CNIO::Grupos de investigación::Grupo de Dinámica Cromosómica | es_ES |
dc.rights.accessRights | open access | es_ES |