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La N-miristoilación posttraducional de BID como un interruptor molecular para dirigirse a las mitocondrias y la
1Howard Hughes Medical Institute, Dana-Farber Cancer Institute, Departments of Pathology and Medicine, Harvard Medical School, Boston, MA 02115, USA.
Science (New York, N.Y.)
|December 2, 2000
Resumen
La proteína pro-apoptótica BID se modifica después de la escisión, lo que le permite dirigirse a las mitocondrias. Esta modificación mejora el BID.
Área de la Ciencia:
- La bioquímica es la bioquímica.
- Biología celular Biología celular.
- Biología Molecular Biología Molecular
Sus antecedentes:
- La apoptosis implica la reubicación de moléculas dentro de las células.
- La proteína BID juega un papel en el inicio de la apoptosis.
Objetivo del estudio:
- Para investigar el mecanismo de la proteína BID dirigida a las mitocondrias durante la apoptosis.
- Para entender el papel de la N-miristoilación en la función del BID.
Principales métodos:
- Estudió la N-miristoilación post-traducional de la proteína BID.
- Investigó la orientación de los fragmentos de BID a las mitocondrias artificiales e intactas.
Principales resultados:
- La escisión por caspase 8 expuso un residuo de glicina en BID, permitiendo la N-miristoilación.
- Los fragmentos de BID N-miristoilados fueron dirigidos a las membranas mitocondriales.
- Esta modificación mejoró la liberación del citocromo c inducida por BID y la muerte celular.
Conclusiones:
- La N-miristoilación posproteolítica de BID actúa como un interruptor de activación.
- Este mecanismo es crucial para el papel de BID en el inicio de la apoptosis y la disfunción mitocondrial.
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