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Published on: November 8, 2006
Regulación coordinada del flujo de azúcar y la traducción por PAS quinasa
Jared Rutter1, Brandon L Probst, Steven L McKnight
1Department of Biochemistry, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390, USA.
Cell
|October 10, 2002
Resumen
La PAS quinasa regula el metabolismo del azúcar y la síntesis de proteínas en la levadura. Esta enzima fosforila las proteínas clave, inhibiendo el almacenamiento de carbohidratos y vinculando el balance de combustible a la traducción.
Área de la Ciencia:
- La bioquímica es la bioquímica.
- Biología Molecular Biología Molecular
- Genética de la levadura Genética de la levadura
Sus antecedentes:
- La PAS quinasa es una serina/treonina quinasa regulada por su dominio PAS.
- Estudios genéticos anteriores implicaron a la PAS quinasa en el metabolismo del azúcar de la levadura en ciernes y el control de la traducción.
Objetivo del estudio:
- Para identificar los sustratos de la PAS quinasa y dilucidar su papel en el metabolismo celular.
- Investigar los mecanismos reguladores que conectan el almacenamiento de carbohidratos y la síntesis de proteínas.
Principales métodos:
- Cribado bioquímico para identificar objetivos de fosforilación de la PAS quinasa.
- Análisis genéticos, bioquímicos y fisiológicos en levaduras en ciernes.
Principales resultados:
- Se identificaron tres factores de traducción como sustratos directos de la PAS quinasa.
- Se ha demostrado que la PAS quinasa fosforila y inhibe la UDP-glucosa pirofosforilasa y la síntesis de glucógeno, enzimas clave en la síntesis de glucógeno.
- Se ha demostrado que la fosforilación dependiente de la PAS quinasa regula a la baja el almacenamiento de carbohidratos.
Conclusiones:
- La quinasa PAS actúa como un regulador central que vincula el metabolismo de los carbohidratos y la síntesis de proteínas.
- Un sistema de señalización celular autónomo controlado por la PAS quinasa equilibra el consumo y el almacenamiento de combustible con la síntesis de proteínas.
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