PubMed:1833185 JSONTXT

{"project":"FSU-PRGE","denotations":[{"id":"T1","span":{"begin":0,"end":4},"obj":"protein"},{"id":"T2","span":{"begin":58,"end":64},"obj":"protein"},{"id":"T3","span":{"begin":84,"end":88},"obj":"protein"},{"id":"T4","span":{"begin":89,"end":103},"obj":"protein"},{"id":"T5","span":{"begin":213,"end":220},"obj":"protein"},{"id":"T6","span":{"begin":261,"end":265},"obj":"protein"},{"id":"T7","span":{"begin":287,"end":302},"obj":"protein"},{"id":"T8","span":{"begin":403,"end":407},"obj":"protein"},{"id":"T9","span":{"begin":432,"end":439},"obj":"protein"},{"id":"T10","span":{"begin":516,"end":531},"obj":"protein"},{"id":"T11","span":{"begin":554,"end":558},"obj":"protein"},{"id":"T12","span":{"begin":576,"end":591},"obj":"protein"},{"id":"T13","span":{"begin":641,"end":645},"obj":"protein"},{"id":"T14","span":{"begin":1061,"end":1065},"obj":"protein"}],"text":"cdc2 phosphorylation is required for its interaction with cyclin.\nActivation of the cdc2 protein kinase at different stages of the cell cycle is regulated by post-translational modifications and interactions with cyclins. We show that in vitro translated human cdc2 binds very poorly to A and B cyclins, unless it has been preincubated with a Xenopus egg extract. This results in the phosphorylation of cdc2 which allows binding to cyclins. The replacement of Thr161, a residue conserved and phosphorylated in other protein kinases, with valine inhibits cdc2 association with A and B cyclins. In addition, mutations in the amino-terminus of cdc2 and within the conserved 'PSTAIR' region strongly inhibit binding. The Thr161Val mutation causes a lethal phenotype in the fission yeast Schizosaccharomyces pombe, while replacement of Thr161 with glutamic acid, potentially mimicking phosphorylation, causes uncoordination of mitosis and multiple cytokinesis. These results suggest that a threonine phosphorylation/dephosphorylation cycle is involved in regulating cdc2 function."}

{"project":"AIMed","denotations":[{"id":"T1","span":{"begin":0,"end":4},"obj":"protein"},{"id":"T2","span":{"begin":84,"end":88},"obj":"protein"},{"id":"T3","span":{"begin":261,"end":265},"obj":"protein"},{"id":"T4","span":{"begin":403,"end":407},"obj":"protein"},{"id":"T5","span":{"begin":554,"end":558},"obj":"protein"},{"id":"T6","span":{"begin":641,"end":645},"obj":"protein"},{"id":"T7","span":{"begin":1061,"end":1065},"obj":"protein"}],"text":"cdc2 phosphorylation is required for its interaction with cyclin.\nActivation of the cdc2 protein kinase at different stages of the cell cycle is regulated by post-translational modifications and interactions with cyclins. We show that in vitro translated human cdc2 binds very poorly to A and B cyclins, unless it has been preincubated with a Xenopus egg extract. This results in the phosphorylation of cdc2 which allows binding to cyclins. The replacement of Thr161, a residue conserved and phosphorylated in other protein kinases, with valine inhibits cdc2 association with A and B cyclins. In addition, mutations in the amino-terminus of cdc2 and within the conserved 'PSTAIR' region strongly inhibit binding. The Thr161Val mutation causes a lethal phenotype in the fission yeast Schizosaccharomyces pombe, while replacement of Thr161 with glutamic acid, potentially mimicking phosphorylation, causes uncoordination of mitosis and multiple cytokinesis. These results suggest that a threonine phosphorylation/dephosphorylation cycle is involved in regulating cdc2 function."}