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dc.contributor.authorTelkoparan P.en_US
dc.contributor.authorErkek, S.en_US
dc.contributor.authorYaman, E.en_US
dc.contributor.authorAlotaibi H.en_US
dc.contributor.authorBayik, D.en_US
dc.contributor.authorTazebay, U.H.en_US
dc.date.accessioned2016-02-08T09:37:31Z
dc.date.available2016-02-08T09:37:31Z
dc.date.issued2013en_US
dc.identifier.issn19326203
dc.identifier.urihttp://hdl.handle.net/11693/20893
dc.description.abstractCytokinetic abscission is the cellular process leading to physical separation of two postmitotic sister cells by severing the intercellular bridge. The most noticeable structural component of the intercellular bridge is a transient organelle termed as midbody, localized at a central region marking the site of abscission. Despite its major role in completion of cytokinesis, our understanding of spatiotemporal regulation of midbody assembly is limited. Here, we report the first characterization of coiled-coil domain-containing protein-124 (Ccdc124), a eukaryotic protein conserved from fungi-to-man, which we identified as a novel centrosomal and midbody protein. Knockdown of Ccdc124 in human HeLa cells leads to accumulation of enlarged and multinucleated cells; however, centrosome maturation was not affected. We found that Ccdc124 interacts with the Ras-guanine nucleotide exchange factor 1B (RasGEF1B), establishing a functional link between cytokinesis and activation of localized Rap2 signaling at the midbody. Our data indicate that Ccdc124 is a novel factor operating both for proper progression of late cytokinetic stages in eukaryotes, and for establishment of Rap2 signaling dependent cellular functions proximal to the abscission site. © 2013 Telkoparan et al.en_US
dc.language.isoEnglishen_US
dc.source.titlePLoS ONEen_US
dc.relation.isversionofhttp://dx.doi.org/10.1371/journal.pone.0069289en_US
dc.subjectcoiled coil domain containing protein 124en_US
dc.subjectguanine nucleotide binding proteinen_US
dc.subjectguanine nucleotide exchange factoren_US
dc.subjectguanine nucleotide exchange factor 1Ben_US
dc.subjectmembrane proteinen_US
dc.subjectRap2 proteinen_US
dc.subjectunclassified drugen_US
dc.subjectarticleen_US
dc.subjectcell functionen_US
dc.subjectcentrosomeen_US
dc.subjectcontrolled studyen_US
dc.subjectcytokinesisen_US
dc.subjecteukaryoteen_US
dc.subjectgene silencingen_US
dc.subjectHeLa cellen_US
dc.subjecthumanen_US
dc.subjecthuman cellen_US
dc.subjectmultinuclear cellen_US
dc.subjectnucleotide sequenceen_US
dc.subjectprotein interactionen_US
dc.subjectsignal transductionen_US
dc.subjectCarrier Proteinsen_US
dc.subjectCentrosomeen_US
dc.subjectCytokinesisen_US
dc.subjectGene Expressionen_US
dc.subjectGene Knockdown Techniquesen_US
dc.subjectHeLa Cellsen_US
dc.subjectHumansen_US
dc.subjectIntracellular Signaling Peptides and Proteinsen_US
dc.subjectOrgan Specificityen_US
dc.subjectOrganellesen_US
dc.subjectProtein Bindingen_US
dc.subjectProtein Interaction Mappingen_US
dc.subjectProtein Transporten_US
dc.subjectrap GTP-Binding Proteinsen_US
dc.subjectras Guanine Nucleotide Exchange Factorsen_US
dc.subjectRNA Interferenceen_US
dc.subjectRNA, Messengeren_US
dc.subjectTelophaseen_US
dc.titleCoiled-Coil Domain Containing Protein 124 Is a Novel Centrosome and Midbody Protein That Interacts with the Ras-Guanine Nucleotide Exchange Factor 1B and Is Involved in Cytokinesisen_US
dc.typeArticleen_US
dc.departmentDepartment of Molecular Biology and Geneticsen_US
dc.citation.volumeNumber8en_US
dc.citation.issueNumber7en_US
dc.identifier.doi10.1371/journal.pone.0069289en_US


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