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| http://purl.uniprot.org/citations/21886794 | http://www.w3.org/2000/01/rdf-schema#comment | "The function of dystrophin Dp71 in neuronal cells remains to be established. Previously, we revealed the involvement of this protein in both nerve growth factor (NGF)-induced neuronal differentiation and cell adhesion by isolation and characterization of PC12 neuronal cells with depleted levels of Dp71. In this work, a novel phenotype of Dp71-knockdown cells was characterized, which is their delayed growth rate. Cell cycle analyses revealed an altered behavior of Dp71-depleted cells, which consists of a delay in G0/G1 transition and an increase in apoptosis during nocodazole-induced mitotic arrest. Dp71 associates with lamin B1 and β-dystroglycan, proteins involved in aspects of the cell division cycle; therefore, we compared the distribution of Dp71 with that of lamin B1 and β-dystroglycan in PC12 cells at mitosis and cytokinesis by means of immunofluorescence and confocal microscopy analysis. All of these three proteins exhibited a similar immunostaining pattern, localized at mitotic spindle, cleavage furrow, and midbody. It is noteworthy that a drastic decreased staining in mitotic spindle, cleavage furrow, and midbody was observed for both lamin B1 and β-dystroglycan in Dp71-depleted cells. Furthermore, we demonstrated the interaction of Dp71 with lamin B1 in PC12 cells by immunoprecipitation and pull-down assays, and importantly, we revealed that knockdown of Dp71 expression caused a marked reduction in lamin B1 levels and altered localization of the nuclear envelope protein emerin. Our data indicate that Dp71 is a component of the mitotic spindle and cytokinesis multi-protein apparatuses that might modulate the cell division cycle by affecting lamin B1 and β-dystroglycan levels."xsd:string |
| http://purl.uniprot.org/citations/21886794 | http://purl.org/dc/terms/identifier | "doi:10.1371/journal.pone.0023504"xsd:string |
| http://purl.uniprot.org/citations/21886794 | http://purl.uniprot.org/core/author | "Centeno-Cruz F."xsd:string |
| http://purl.uniprot.org/citations/21886794 | http://purl.uniprot.org/core/author | "Garrido E."xsd:string |
| http://purl.uniprot.org/citations/21886794 | http://purl.uniprot.org/core/author | "Suarez-Sanchez R."xsd:string |
| http://purl.uniprot.org/citations/21886794 | http://purl.uniprot.org/core/author | "Cisneros B."xsd:string |
| http://purl.uniprot.org/citations/21886794 | http://purl.uniprot.org/core/author | "Villarreal-Silva M."xsd:string |
| http://purl.uniprot.org/citations/21886794 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
| http://purl.uniprot.org/citations/21886794 | http://purl.uniprot.org/core/name | "PLoS One"xsd:string |
| http://purl.uniprot.org/citations/21886794 | http://purl.uniprot.org/core/pages | "e23504"xsd:string |
| http://purl.uniprot.org/citations/21886794 | http://purl.uniprot.org/core/title | "Knockdown of dystrophin Dp71 impairs PC12 cells cycle: localization in the spindle and cytokinesis structures implies a role for Dp71 in cell division."xsd:string |
| http://purl.uniprot.org/citations/21886794 | http://purl.uniprot.org/core/volume | "6"xsd:string |
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