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http://purl.uniprot.org/citations/12738781http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12738781http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12738781http://www.w3.org/2000/01/rdf-schema#comment"Plk1 (Polo-like kinase 1), an evolutionarily conserved serine/threonine kinase, is crucially involved in multiple events during the M phase. Here we have identified a consensus phosphorylation sequence for Plk1, by testing the ability of systematically mutated peptides derived from human Cdc25C to serve as a substrate for Plk1. The obtained results show that a hydrophobic amino acid at position +1 carboxyl-terminal of phosphorylated Ser/Thr and an acidic amino acid at position -2 are important for optimal phosphorylation by Plk1. We have then found that Myt1, an inhibitory kinase for MPF, has a number of putative phosphorylation sites for Plk1 in its COOH-terminal portion. While wild-type Myt1 (Myt1-WT) served as a good substrate for Plk1 in vitro, a mutant Myt1 (Myt1-4A), in which the four putative phosphorylation sites are replaced by alanines, did not. In nocodazole-treated cells, Myt1-WT, but not Myt1-4A, displayed its mobility shift in gel electrophoresis, due to phosphorylation. These results suggest that Plk1 phosphorylates Myt1 during M phase. Thus, this study identifies a novel substrate for Plk1 by determining a consensus phosphorylation sequence by Plk1."xsd:string
http://purl.uniprot.org/citations/12738781http://purl.org/dc/terms/identifier"doi:10.1074/jbc.c300126200"xsd:string
http://purl.uniprot.org/citations/12738781http://purl.org/dc/terms/identifier"doi:10.1074/jbc.c300126200"xsd:string
http://purl.uniprot.org/citations/12738781http://purl.uniprot.org/core/author"Nakajima H."xsd:string
http://purl.uniprot.org/citations/12738781http://purl.uniprot.org/core/author"Nakajima H."xsd:string
http://purl.uniprot.org/citations/12738781http://purl.uniprot.org/core/author"Nishida E."xsd:string
http://purl.uniprot.org/citations/12738781http://purl.uniprot.org/core/author"Nishida E."xsd:string
http://purl.uniprot.org/citations/12738781http://purl.uniprot.org/core/author"Taniguchi E."xsd:string
http://purl.uniprot.org/citations/12738781http://purl.uniprot.org/core/author"Taniguchi E."xsd:string
http://purl.uniprot.org/citations/12738781http://purl.uniprot.org/core/author"Toyoshima-Morimoto F."xsd:string
http://purl.uniprot.org/citations/12738781http://purl.uniprot.org/core/author"Toyoshima-Morimoto F."xsd:string
http://purl.uniprot.org/citations/12738781http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12738781http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12738781http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/12738781http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/12738781http://purl.uniprot.org/core/pages"25277-25280"xsd:string
http://purl.uniprot.org/citations/12738781http://purl.uniprot.org/core/pages"25277-25280"xsd:string
http://purl.uniprot.org/citations/12738781http://purl.uniprot.org/core/title"Identification of a consensus motif for Plk (Polo-like kinase) phosphorylation reveals Myt1 as a Plk1 substrate."xsd:string
http://purl.uniprot.org/citations/12738781http://purl.uniprot.org/core/title"Identification of a consensus motif for Plk (Polo-like kinase) phosphorylation reveals Myt1 as a Plk1 substrate."xsd:string
http://purl.uniprot.org/citations/12738781http://purl.uniprot.org/core/volume"278"xsd:string
http://purl.uniprot.org/citations/12738781http://purl.uniprot.org/core/volume"278"xsd:string
http://purl.uniprot.org/citations/12738781http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12738781
http://purl.uniprot.org/citations/12738781http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12738781