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http://purl.uniprot.org/citations/21076410http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21076410http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21076410http://www.w3.org/2000/01/rdf-schema#comment"During interphase, centrosomes are held together by a proteinaceous linker that connects the proximal ends of the mother and daughter centriole. This linker is disassembled at the onset of mitosis in a process known as centrosome disjunction, thereby facilitating centrosome separation and bipolar spindle formation. The NIMA (never in mitosis A)-related kinase Nek2A is implicated in disconnecting the centrosomes through disjoining the linker proteins C-Nap1 and rootletin. However, the mechanisms controlling centrosome disjunction remain poorly understood. Here, we report that two Hippo pathway components, the mammalian sterile 20-like kinase 2 (Mst2) and the scaffold protein Salvador (hSav1), directly interact with Nek2A and regulate its ability to localize to centrosomes, and phosphorylate C-Nap1 and rootletin. Furthermore, we demonstrate that the hSav1-Mst2-Nek2A centrosome disjunction pathway becomes essential for bipolar spindle formation on partial inhibition of the kinesin-5 Eg5. We propose that hSav1-Mst2-Nek2A and Eg5 have distinct, but complementary functions, in centrosome disjunction."xsd:string
http://purl.uniprot.org/citations/21076410http://purl.org/dc/terms/identifier"doi:10.1038/ncb2120"xsd:string
http://purl.uniprot.org/citations/21076410http://purl.org/dc/terms/identifier"doi:10.1038/ncb2120"xsd:string
http://purl.uniprot.org/citations/21076410http://purl.uniprot.org/core/author"Lange C."xsd:string
http://purl.uniprot.org/citations/21076410http://purl.uniprot.org/core/author"Lange C."xsd:string
http://purl.uniprot.org/citations/21076410http://purl.uniprot.org/core/author"Schiebel E."xsd:string
http://purl.uniprot.org/citations/21076410http://purl.uniprot.org/core/author"Schiebel E."xsd:string
http://purl.uniprot.org/citations/21076410http://purl.uniprot.org/core/author"Mardin B.R."xsd:string
http://purl.uniprot.org/citations/21076410http://purl.uniprot.org/core/author"Mardin B.R."xsd:string
http://purl.uniprot.org/citations/21076410http://purl.uniprot.org/core/author"Fry A.M."xsd:string
http://purl.uniprot.org/citations/21076410http://purl.uniprot.org/core/author"Fry A.M."xsd:string
http://purl.uniprot.org/citations/21076410http://purl.uniprot.org/core/author"Baxter J.E."xsd:string
http://purl.uniprot.org/citations/21076410http://purl.uniprot.org/core/author"Baxter J.E."xsd:string
http://purl.uniprot.org/citations/21076410http://purl.uniprot.org/core/author"Hardy T."xsd:string
http://purl.uniprot.org/citations/21076410http://purl.uniprot.org/core/author"Hardy T."xsd:string
http://purl.uniprot.org/citations/21076410http://purl.uniprot.org/core/author"Scholz S.R."xsd:string
http://purl.uniprot.org/citations/21076410http://purl.uniprot.org/core/author"Scholz S.R."xsd:string
http://purl.uniprot.org/citations/21076410http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/21076410http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/21076410http://purl.uniprot.org/core/name"Nat. Cell Biol."xsd:string
http://purl.uniprot.org/citations/21076410http://purl.uniprot.org/core/name"Nat. Cell Biol."xsd:string
http://purl.uniprot.org/citations/21076410http://purl.uniprot.org/core/pages"1166-1176"xsd:string
http://purl.uniprot.org/citations/21076410http://purl.uniprot.org/core/pages"1166-1176"xsd:string