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Protein phosphatase 2A stabilizes human securin, whose phosphorylated forms are degraded via the SCF ubiquitin ligase

Opened Access Protein phosphatase 2A stabilizes human securin, whose phosphorylated forms are degraded via the SCF ubiquitin ligase

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Autor: Gil Bernabé, Ana María
Romero Portillo, Francisco
Limón Mortés, María Cristina
Tortolero García, María Dolores
Departamento: Universidad de Sevilla. Departamento de Microbiología
Fecha: 2006
Tipo de documento: Artículo
Resumen: Sister chromatid segregation is triggered at the metaphase-to-anaphase transition by the activation of the protease separase. For most of the cell cycle, separase activity is kept in check by its association with the inhibitory chaperone securin. Activation of separase occurs at anaphase onset, when securin is targeted for destruction by the anaphase-promoting complex or cyclosome E3 ubiquitin protein ligase. This results in the release of the cohesins from chromosomes, which in turn allows the segregation of sister chromatids to opposite spindle poles. Here we show that human securin (hSecurin) forms a complex with enzymatically active protein phosphatase 2A (PP2A) and that it is a substrate of the phosphatase, both in vitro and in vivo. Treatment of cells with okadaic acid, a potent inhibitor of PP2A, results in various hyperphosphorylated forms of hSecurin which are extremely unstable, due to the action of the Skp1/Cull/F-box protein complex ubiquitin ligase. We propose that PP2A r...
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Cita: Gil Bernabé, A.M., Romero Portillo, F., Limón Mortes, M.C. y Tortolero García, M.D. (2006). Protein phosphatase 2A stabilizes human securin, whose phosphorylated forms are degraded via the SCF ubiquitin ligase. Molecular and Cellular Biology, 26 (11), 4017-4027.
Tamaño: 386.2Kb
Formato: PDF

URI: https://hdl.handle.net/11441/70528

DOI: 10.1128/MCB.01904-05

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