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cPLA2 es fosforilado y activado por la kinasa MAP.

L L Lin1, M Wartmann, A Y Lin

  • 1Genetics Institute, Small Molecule Drug Discovery Group, Cambridge, Massachusetts 02140.

Cell
|January 29, 1993
PubMed
Resumen

La proteína kinasa activada por mitógeno (MAP) fosforila y activa la fosfolipasa citosólica A2 (cPLA2) en el Ser-505.5. Esta activación mediada por MAP quinasa es crucial para la liberación de ácido araquidónico inducida por agonistas en las células.

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Área de la Ciencia:

  • Las vías de señalización celular.
  • Enzimología Enzimología.
  • Biología molecular La biología molecular.

Sus antecedentes:

  • La estimulación agonista desencadena la liberación de ácido araquidónico, que incluye la activación de la fosfolipasa citosólica A2 (cPLA2) y la fosforilación de la serina.
  • Los mecanismos precisos que regulan la activación del cPLA2 aún no se comprenden por completo.

Objetivo del estudio:

  • Para investigar el papel de la proteína kinasa activada por mitógeno (MAP) en la activación de cPLA2.2.
  • Para identificar el sitio específico de fosforilación en cPLA2 dirigido por la MAP quinasa.

Principales métodos:

  • Pruebas in vitro de la quinasa para determinar si el cPLA2 es un sustrato para la MAP quinasa.
  • Mutagenesis dirigida al sitio para reemplazar el sitio de fosforilación identificado (Ser-505) con alanina.
  • Evaluación de la actividad enzimática del cPLA2 y la liberación de ácido araquidónico en células que expresan el tipo silvestre y el cPLA2 mutante.

Principales resultados:

  • cPLA2 fue identificado como un sustrato directo para la MAP quinasa.
  • La fosforilación de cPLA2 por MAP quinasa aumentó significativamente su actividad enzimática.
  • La serina-505 fue identificada como el sitio primario de la fosforilación mediada por la cinasa MAP en el cPLA2.2.
  • Un cPLA2 mutante con Ser-505 reemplazado por alanina no fue fosforilado por la MAP quinasa y mostró una liberación de ácido araquidónico estimulada por agonistas significativamente reducida.

Conclusiones:

  • La MAP quinasa juega un papel importante en la mediación de la activación inducida por agonistas de cPLA2.
  • La fosforilación de cPLA2 en Ser-505 por MAP quinasa es un paso clave en la regulación de la liberación de ácido araquidónico.