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Función de los dominios WW como módulos de unión a la fosfoserina o la fosfotreonina
1Cancer Biology Program, Division of Hematology/Oncology, Department of Medicine, Beth Israel Deaconess Medical Center and Harvard Medical School, Boston, MA 02215, USA.
Science (New York, N.Y.)
|February 26, 1999
Resumen
Los investigadores descubrieron que los dominios WW, específicamente el dominio Pin1 WW, actúan como módulos de unión a la fosfoserina o a la fosfotreonina. Esta unión es crucial para las interacciones de las proteínas y Pin1.
Área de la Ciencia:
- Biología Molecular Biología Molecular
- La señalización celular de las células.
- Bioquímica de las proteínas Bioquímica de las proteínas
Sus antecedentes:
- Los módulos que interactúan con las proteínas dictan la especificidad de la transducción de la señal.
- La fosforilación regula el montaje de los complejos de señalización.
- Se conocen módulos de unión a la fosfotirosina, pero los módulos de unión a la fosfoserina/treonina no están descritos.
Objetivo del estudio:
- Para caracterizar las propiedades de enlace de los dominios WW.
- Investigar el papel de los dominios WW en las interacciones y la señalización proteína-proteína.
- Para determinar si los dominios WW pueden unirse a los residuos de fosfoserina o fosfotreonina.
Principales métodos:
- Estudió los dominios WW de Pin1 y Nedd4.4.
- Se ha evaluado la unión a las fosfoproteínas de una manera dependiente de la fosforilación.
- Investigó el requisito funcional de la unión de fosfoserina/treonina para la actividad de Pin1 in vitro e in vivo.
Principales resultados:
- Los dominios WW de Pin1 y Nedd4 se unen a las fosfoproteínas, incluidos los sustratos de las enzimas.
- El dominio Pin1 WW funciona como un módulo de unión de la fosfoserina y la fosfotreonina.
- Esta actividad de unión es esencial para la interacción del sustrato de Pin1 y su función in vivo.
Conclusiones:
- Los dominios WW representan una nueva clase de módulos de unión a la fosfoserina y la treonina.
- El dominio WW de Pin1 es crítico para su papel biológico a través del reconocimiento de fosfoproteínas específicas.
- Este hallazgo amplía la comprensión de la regulación compleja de la señalización a través de interacciones dependientes de la fosforilación.
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