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http://purl.uniprot.org/citations/16024801http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16024801http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16024801http://www.w3.org/2000/01/rdf-schema#comment"SIL is an immediate-early gene that is essential for embryonic development and is implicated in T-cell leukemia-associated translocations. We now show that the Sil protein is hyperphosphorylated during mitosis or in cells blocked at prometaphase by microtubule inhibitors. Cell cycle-dependent phosphorylation of Sil is required for its interaction with Pin1, a regulator of mitosis. Point mutation of the seven (S/T)P sites between amino acids 567 and 760 reduces mitotic phosphorylation of Sil, Pin1 binding, and spindle checkpoint duration. When a phosphorylation site mutant Sil is stably expressed, the duration of the spindle checkpoint is shortened in cells challenged with taxol or nocodazole, and the cells revert to a G2-like state. This event is associated with the downregulation of the kinase activity of the Cdc2/cyclin B1 complex and the dephosphorylation of the threonine 161 on the Cdc2 subunit. Sil downregulation by plasmid-mediated RNA interference limited the ability of cells to activate the spindle checkpoint and correlated with a reduction of Cdc2/cyclin B1 activity and phosphorylation on T161 on the Cdc2 subunit. These data suggest that a critical region of Sil is required to mediate the presentation of Cdc2 activity during spindle checkpoint arrest."xsd:string
http://purl.uniprot.org/citations/16024801http://purl.org/dc/terms/identifier"doi:10.1128/mcb.25.15.6660-6672.2005"xsd:string
http://purl.uniprot.org/citations/16024801http://purl.org/dc/terms/identifier"doi:10.1128/mcb.25.15.6660-6672.2005"xsd:string
http://purl.uniprot.org/citations/16024801http://purl.uniprot.org/core/author"Kaldis P."xsd:string
http://purl.uniprot.org/citations/16024801http://purl.uniprot.org/core/author"Kaldis P."xsd:string
http://purl.uniprot.org/citations/16024801http://purl.uniprot.org/core/author"Kirsch I.R."xsd:string
http://purl.uniprot.org/citations/16024801http://purl.uniprot.org/core/author"Kirsch I.R."xsd:string
http://purl.uniprot.org/citations/16024801http://purl.uniprot.org/core/author"Campaner S."xsd:string
http://purl.uniprot.org/citations/16024801http://purl.uniprot.org/core/author"Campaner S."xsd:string
http://purl.uniprot.org/citations/16024801http://purl.uniprot.org/core/author"Izraeli S."xsd:string
http://purl.uniprot.org/citations/16024801http://purl.uniprot.org/core/author"Izraeli S."xsd:string
http://purl.uniprot.org/citations/16024801http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16024801http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16024801http://purl.uniprot.org/core/name"Mol. Cell. Biol."xsd:string
http://purl.uniprot.org/citations/16024801http://purl.uniprot.org/core/name"Mol. Cell. Biol."xsd:string
http://purl.uniprot.org/citations/16024801http://purl.uniprot.org/core/pages"6660-6672"xsd:string
http://purl.uniprot.org/citations/16024801http://purl.uniprot.org/core/pages"6660-6672"xsd:string
http://purl.uniprot.org/citations/16024801http://purl.uniprot.org/core/title"Sil phosphorylation in a Pin1 binding domain affects the duration of the spindle checkpoint."xsd:string
http://purl.uniprot.org/citations/16024801http://purl.uniprot.org/core/title"Sil phosphorylation in a Pin1 binding domain affects the duration of the spindle checkpoint."xsd:string
http://purl.uniprot.org/citations/16024801http://purl.uniprot.org/core/volume"25"xsd:string
http://purl.uniprot.org/citations/16024801http://purl.uniprot.org/core/volume"25"xsd:string
http://purl.uniprot.org/citations/16024801http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16024801
http://purl.uniprot.org/citations/16024801http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16024801