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La función y el mecanismo molecular de la acetilación en la regulación de la autofagia
Cong Yi1, Meisheng Ma, Leili Ran
1State Key Laboratory of Biomembrane and Membrane Biotechnology, School of Life Sciences, Tsinghua University, Beijing, China.
Science (New York, N.Y.)
|April 28, 2012
Resumen
La acetilación de proteínas regula la autofagia. El estudio identificó que Esa1 acetila Atg3 en K19 y K48, controlando la señalización de la autofagia y las interacciones de proteínas esenciales para este proceso celular.
Área de la Ciencia:
- Biología celular Biología celular.
- Biología Molecular Biología Molecular
- La bioquímica es la bioquímica.
Sus antecedentes:
- La acetilación de proteínas es un mecanismo regulador crucial en los procesos celulares.
- La autofagia, un proceso celular fundamental, está implicada en varias condiciones fisiológicas y patológicas.
- Las histonas acetiltransferasas (HAT) y las desacetilasas juegan un papel importante en la regulación de la expresión génica y la función de las proteínas.
Objetivo del estudio:
- Para investigar el papel de la acetilación de proteínas en la regulación de la autofagia.
- Para identificar proteínas específicas involucradas en la autofagia que son objetivos de la acetilación.
- Aclarar el mecanismo por el cual la acetilación controla la señalización y ejecución de la autofagia.
Principales métodos:
- El análisis genético en Saccharomyces cerevisiae.
- Identificación de residuos de lisina acetilada en las proteínas de la autofagia.
- Análisis de las interacciones proteína-proteína y la lipidación proteica.
- Investigación de la localización de enzimas y su actividad durante la inanición.
Principales resultados:
- Esa1, una histona acetiltransferasa, fue identificada como esencial para la autofagia.
- Se descubrió que Atg3, un componente de señalización de la autofagia, es un sustrato para la acetilación de Esa1 en K19 y K48.
- La acetilación de Atg3 en K19-K48 regula la autofagia mediante la modulación de la interacción Atg3-Atg8 y la lipidación de Atg8.
- El hambre induce la acetilación Atg3 transitorio a través de la regulación espacio-temporal de Esa1 y Rpd3 en las estructuras pre-autofagosómicas.
- La atenuación de la acetilación se correlacionó con la reducción de la autofagia, mientras que la deleción de Rpd3 aumentó la acetilación y la autofagia.
Conclusiones:
- La acetilación de proteínas, específicamente de Atg3 en K19-K48, es un regulador crítico de la autofagia.
- La interacción entre la acetilasa Esa1 y la desacetilasa Rpd3 controla la dinámica de la autofagia.
- Este estudio revela un nuevo mecanismo que vincula la modificación post-traducional con la regulación de la autofagia.
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