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Una proteína de unión al ARN asociada con Src a través de sus dominios SH2 y SH3 en la mitosis
1Section of Biochemistry, Molecular and Cell Biology, Cornell University, Ithaca, New York 14853.
Nature
|April 28, 1994
Resumen
La c-Src quinasa activada durante la mitosis fosforila y se une a una proteína 68K (p68). Esto sugiere que c-Src puede regular el procesamiento, el tráfico o la traducción del ARN durante el ciclo celular.
Área de la Ciencia:
- Biología celular Biología celular.
- Biología Molecular Biología Molecular
- La bioquímica es la bioquímica.
Sus antecedentes:
- La actividad de la tirosina quinasa c-Src aumenta durante la mitosis a través de la desfosforilación.
- La activación mitótica de c-Src mejora la unión al dominio de la homología-2 (SH2) de Src.
- Los objetivos fisiológicos de c-Src mitótico siguen siendo en gran parte no identificados.
Objetivo del estudio:
- Para identificar objetivos fisiológicos de c-Src activado durante la mitosis.
- Investigar la interacción entre c-Src y sus dianas mitóticas.
Principales métodos:
- Ensayos de fosforilación de tirosina en fibroblastos de ratón durante la mitosis.
- Co-inmunoprecipitación para detectar las interacciones proteína-proteína.
- Ensayos de unión in vitro utilizando los dominios Src SH2 y SH3.
- Análisis de la homología de la proteína p68 y socios de unión.
Principales resultados:
- La proteína A 68K (p68) es fosforilada por tirosina y se asocia con Src durante la mitosis.
- p68 se une de forma independiente a los dominios Src SH2 y SH3 in vitro.
- Tanto los dominios SH2 como SH3 son esenciales para la fosforilación y unión de p68 in vivo.
- p68 comparte homología con p62, conocido por unirse a los poliribonucleótidos.
Conclusiones:
- El c-Src mitótico interactúa directamente con y fosforila el p68.8.
- La interacción involucra tanto los dominios SH2 como los SH3 de c-Src.
- c-Src puede regular los procesos relacionados con el ARN (procesamiento, tráfico, traducción) de una manera dependiente del ciclo celular.
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