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La metilación de la arginina de STAT1 modula la transcripción inducida por IFNalfa/beta inducida por la arginina
1Division of Biology and UCSD Cancer Center, University of California, San Diego, Bonner Hall 3138, 9500 Gilman Drive, La Jolla, CA 92093, USA.
Cell
|March 21, 2001
Resumen
La metilación de la arginina de STAT1 por PRMT1 es crucial para la transcripción inducida por el interferón. Esta modificación impide la unión de PIAS1, lo que garantiza la unión de STAT1 al ADN y las respuestas al interferón, que a menudo se pierden en los cánceres.
Área de la Ciencia:
- Biología Molecular Biología Molecular
- Biología celular Biología celular.
- Inmunología Inmunología.
Sus antecedentes:
- La señalización del interferón se basa en la fosforilación del factor de transcripción STAT.
- Las proteínas STAT comparten un residuo de arginina N-terminal conservado.
Objetivo del estudio:
- Para investigar el papel de la metilación de la arginina en la función STAT1.
- Para explorar el impacto de la inhibición de la metilación en las respuestas al interferón.
Principales métodos:
- Se ha demostrado la metilación de la arginina de STAT1 por PRMT1.
- Utilizó metil-tioadenosina (un inhibidor de la metil-transferasa).
- Se evaluó la unión al STAT1-ADN y la asociación con PIAS1.
Principales resultados:
- La metilación de STAT1 por arginina es esencial para la transcripción inducida por IFNalfa/beta.
- La metil-tioadenosina inhibe las respuestas de interferón mediadas por STAT1.
- La inhibición es el resultado de un deterioro de la unión STAT1-ADN debido al aumento de la asociación PIAS1 en STAT1.1. no metilado.
Conclusiones:
- La metilación de la arginina es una nueva modificación post-traduccional que regula la función STAT1.
- La metilación alterada de la arginina puede explicar la falta de respuesta al interferón en las neoplasias malignas.
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