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Regulación secuencial de la dinámica DOCK2 por dos fosfolípidos durante la quimiotaxis de los neutrófilos
Akihiko Nishikimi1, Hideo Fukuhara, Wenjuan Su
1Division of Immunogenetics, Department of Immunobiology and Neuroscience, Medical Institute of Bioregulation, Kyushu University, Fukuoka 812-8582, Japan.
Science (New York, N.Y.)
|March 28, 2009
Resumen
La migración de los neutrófilos se basa en la activación de Rac, guiada por la dinámica de la proteína DOCK2. Los fosfolípidos como el ácido fosfatídico son cruciales para estabilizar el DOCK2 en la célula.
Área de la Ciencia:
- Biología celular Biología celular.
- Biología molecular La biología molecular.
- Inmunología Inmunología.
Sus antecedentes:
- La quimiotaxis implica la regulación espacial de la activación de la pequeña guanosina trifosfatasa (GTPasa) Rac para la migración celular dirigida.
- En los neutrófilos, DOCK2 actúa como un factor clave de intercambio de nucleótidos de guanina que media la activación de Rac.
Objetivo del estudio:
- Para dilucidar la regulación secuencial dependiente de fosfolípidos de la dinámica intracelular de DOCK2 durante la quimiotaxis de neutrófilos.
- Comprender cómo la localización de DOCK2 en el borde de ataque influye en la polimerización de actina y la migración celular.
Principales métodos:
- Utilizamos ensayos bioquímicos e imágenes de células vivas para rastrear la translocación y localización de DOCK2.
- Investigó el papel del fosfatidilinositol 3,4,5-trisfosfato y el ácido fosfatídico en la regulación del DOCK2.
- Examinó el impacto del bloqueo de las interacciones de DOCK2-fosfolípidos en el comportamiento de los neutrófilos.
Principales resultados:
- DOCK2 se transloca rápidamente a la membrana plasmática dependiendo del fosfatidilinositol 3,4,5-trisfosfato después de la estimulación.
- La síntesis de ácido fosfatídico mediada por la fosfolipasa D fue esencial para la acumulación sostenida de DOCK2 en el borde principal.
- La estabilización de DOCK2 implicó la interacción con un grupo de aminoácidos polibásicos, promoviendo la polimerización de la actina.
- El bloqueo de esta interacción deterioró la formación del borde principal y causó defectos de quimiotaxis en los neutrófilos.
Conclusiones:
- La dinámica intracelular del DOCK2 está regulada secuencialmente por distintos fosfolípidos, fosfatidilinositol 3,4,5-trisfosfato y ácido fosfatídico.
- Esta localización precisa de DOCK2 es crítica para la activación de Rac y la quimiotaxis adecuada de los neutrófilos.
- Los hallazgos revelan un nuevo mecanismo para el control espacio-temporal de la migración celular.
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