| http://purl.uniprot.org/citations/10775038 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10775038 | http://www.w3.org/2000/01/rdf-schema#comment | "Wee1 protein kinase plays an important regulatory role in cell cycle progression. It inhibits Cdc-2 activity by phosphorylating Tyr15 and arrests cells at G2-M phase. In an attempt to understand Wee1 regulation during cell cycle, yeast two-hybrid screening was used to identify Wee1-binding protein(s). Five of the eight positive clones identified encode 14-3-3beta. In vivo binding assay in 293 cells showed that both full-length and NH2-terminal truncated Wee1 bind with 14-3-3beta. The 14-3-3beta binding site was mapped to a COOH-terminal consensus motif, RSVSLT (codons 639 to 646). Binding with 14-3-3beta increases the protein level of full-length Wee1 but not of the truncated Wee1. Accompanying the protein level increases, the kinase activity of Wee1 also increases when coexpressed with 14-3-3beta. Increased Wee1 protein level/enzymatic activity is accountable, at least in part, to an increased Wee1 protein half-life when coexpressed with 14-3-3beta. The protein half-life of the NH2-terminal truncated Wee1 is much longer than that of the full-length protein and is not affected by 14-3-3beta cotransfection. Biologically, 14-3-3beta/Wee1 coexpression increases the cell population at G2-M phase. Thus, Wee1 binding with 14-3-3beta increases its biochemical activity as well as its biological function. The finding reveals a novel mechanism by which 14-3-3 regulates G2-M arrest and suggests that the NH2-terminal domain of Wee1 contains a negative regulatory sequence that determines Wee1 stability."xsd:string |
| http://purl.uniprot.org/citations/10775038 | http://purl.uniprot.org/core/author | "Sun Y."xsd:string |
| http://purl.uniprot.org/citations/10775038 | http://purl.uniprot.org/core/author | "Wang Y."xsd:string |
| http://purl.uniprot.org/citations/10775038 | http://purl.uniprot.org/core/author | "Duan H."xsd:string |
| http://purl.uniprot.org/citations/10775038 | http://purl.uniprot.org/core/author | "Jacobs C."xsd:string |
| http://purl.uniprot.org/citations/10775038 | http://purl.uniprot.org/core/author | "Booher R.N."xsd:string |
| http://purl.uniprot.org/citations/10775038 | http://purl.uniprot.org/core/author | "Hook K.E."xsd:string |
| http://purl.uniprot.org/citations/10775038 | http://purl.uniprot.org/core/date | "2000"xsd:gYear |
| http://purl.uniprot.org/citations/10775038 | http://purl.uniprot.org/core/name | "Cell Growth Differ"xsd:string |
| http://purl.uniprot.org/citations/10775038 | http://purl.uniprot.org/core/pages | "211-219"xsd:string |
| http://purl.uniprot.org/citations/10775038 | http://purl.uniprot.org/core/title | "Binding of 14-3-3beta to the carboxyl terminus of Wee1 increases Wee1 stability, kinase activity, and G2-M cell population."xsd:string |
| http://purl.uniprot.org/citations/10775038 | http://purl.uniprot.org/core/volume | "11"xsd:string |
| http://purl.uniprot.org/citations/10775038 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10775038 |
| http://purl.uniprot.org/citations/10775038 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/10775038 |
| http://purl.uniprot.org/uniprot/#_P30291-mappedCitation-10775038 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/10775038 |
| http://purl.uniprot.org/uniprot/#_P31946-mappedCitation-10775038 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/10775038 |
| http://purl.uniprot.org/uniprot/P30291 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/10775038 |
| http://purl.uniprot.org/uniprot/P31946 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/10775038 |