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Los complejos SNARE neuronales reconstituidos individuales se cierran en tres etapas distintas
Ying Gao1, Sylvain Zorman, Gregory Gundersen
1Department of Cell Biology, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06520, USA.
Science (New York, N.Y.)
|August 21, 2012
Resumen
Las proteínas del receptor de la proteína de adhesión sensible al factor soluble N-etilmaleimida (SNARE) median la fusión de la membrana. Este estudio revela un intermedio clave en el ensamblaje de SNARE, lo que sugiere un proceso gradual, no continuo, de cremallera que impulsa la fusión.
Área de la Ciencia:
- La bioquímica es la bioquímica.
- Biología celular Biología celular.
- La biofísica es la biofísica.
Sus antecedentes:
- Las proteínas solubles del receptor de la proteína de unión sensible al factor N-etilmaleimida (SNARE) son esenciales para la fusión de la membrana.
- Las SNARE se ensamblan en un haz de cuatro hélices a través de un mecanismo de cremallera.
Objetivo del estudio:
- Para observar y caracterizar un ensamblaje SNARE intermedio en tiempo real.
- Para aclarar el mecanismo paso a paso de la fusión de membranas mediada por SNARE.
Principales métodos:
- Utilizó pinzas ópticas en un experimento de reconstitución libre de células.
- Se aplica fuerza externa para imitar la repulsión de la membrana y estabilizar los intermedios.
Principales resultados:
- Se observó un intermedio de haz de SNARE de cuatro hélices estable, medio ensamblado.
- Se demostró que la cremallera SNARE se produce a través de tres interruptores binarios secuenciales.
- Cuantificó la energía libre liberada durante la fusión (36 kB).
Conclusiones:
- La hipótesis de la cremallera se apoya, pero procede en pasos discretos.
- Un intermediario con media cremallera juega un papel crucial en la fusión de la membrana.
- La fuerza aplicada externamente puede estabilizar e influir en el conjunto complejo SNARE.
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01:25Rab Cascades
Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.