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http://purl.uniprot.org/citations/16076287http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16076287http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16076287http://www.w3.org/2000/01/rdf-schema#comment"Tankyrase 1 is a PARP [poly(ADP-ribose) polymerase] that localizes to multiple subcellular sites, including telomeres and mitotic centrosomes. Previous studies demonstrated that cells deficient in tankyrase 1 suffered a block in resolution of sister telomeres and arrested in early anaphase [Dynek and Smith (2004) Science 304, 97-100]. This phenotype was dependent on the catalytic PARP activity of tankyrase 1. To identify critical acceptors of PARsylation [poly(ADP-ribosyl)ation] by tankyrase 1 in mitosis, tankyrase 1 immunoprecipitates were analysed for associated PARsylated proteins. We identified NuMA (nuclear mitotic apparatus protein) as a major acceptor of poly(ADP-ribose) from tankyrase 1 in mitosis. We showed by immunofluorescence and immunoprecipitation that association between tankyrase 1 and NuMA increases dramatically at the onset of mitosis, concomitant with PARsylation of NuMA. Knockdown of tankyrase 1 by siRNA (small interfering RNA) eliminates PARsylation of NuMA in mitosis, confirming tankyrase 1 as the PARP responsible for this modification. However, even in the absence of tankyrase 1 and PARsylation, NuMA localizes to spindle poles. By contrast, siRNA knockdown of NuMA results in complete loss of tankyrase 1 from spindle poles. We discuss our result in terms of a model where PARsylation of NuMA by tankyrase 1 in mitosis could play a role in sister telomere separation and/or mitotic progression."xsd:string
http://purl.uniprot.org/citations/16076287http://purl.org/dc/terms/identifier"doi:10.1042/bj20050885"xsd:string
http://purl.uniprot.org/citations/16076287http://purl.org/dc/terms/identifier"doi:10.1042/bj20050885"xsd:string
http://purl.uniprot.org/citations/16076287http://purl.uniprot.org/core/author"Chang W."xsd:string
http://purl.uniprot.org/citations/16076287http://purl.uniprot.org/core/author"Chang W."xsd:string
http://purl.uniprot.org/citations/16076287http://purl.uniprot.org/core/author"Smith S."xsd:string
http://purl.uniprot.org/citations/16076287http://purl.uniprot.org/core/author"Smith S."xsd:string
http://purl.uniprot.org/citations/16076287http://purl.uniprot.org/core/author"Dynek J.N."xsd:string
http://purl.uniprot.org/citations/16076287http://purl.uniprot.org/core/author"Dynek J.N."xsd:string
http://purl.uniprot.org/citations/16076287http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16076287http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16076287http://purl.uniprot.org/core/name"Biochem. J."xsd:string
http://purl.uniprot.org/citations/16076287http://purl.uniprot.org/core/name"Biochem. J."xsd:string
http://purl.uniprot.org/citations/16076287http://purl.uniprot.org/core/pages"177-184"xsd:string
http://purl.uniprot.org/citations/16076287http://purl.uniprot.org/core/pages"177-184"xsd:string
http://purl.uniprot.org/citations/16076287http://purl.uniprot.org/core/title"NuMA is a major acceptor of poly(ADP-ribosyl)ation by tankyrase 1 in mitosis."xsd:string
http://purl.uniprot.org/citations/16076287http://purl.uniprot.org/core/title"NuMA is a major acceptor of poly(ADP-ribosyl)ation by tankyrase 1 in mitosis."xsd:string
http://purl.uniprot.org/citations/16076287http://purl.uniprot.org/core/volume"391"xsd:string
http://purl.uniprot.org/citations/16076287http://purl.uniprot.org/core/volume"391"xsd:string
http://purl.uniprot.org/citations/16076287http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16076287
http://purl.uniprot.org/citations/16076287http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16076287
http://purl.uniprot.org/citations/16076287http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/16076287
http://purl.uniprot.org/citations/16076287http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/16076287