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A High-throughput Calcium-flux Assay to Study NMDA-receptors with Sensitivity to Glycine/D-serine and Glutamate
Published on: July 10, 2018
Regulación de la fosforilación del receptor NMDA mediante el empalme alternativo del dominio C-terminal
W G Tingley1, K W Roche, A K Thompson
1Department of Neuroscience, Howard Hughes Medical Institute, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.
Nature
|July 1, 1993
Resumen
El empalme alternativo de la subunidad NR1 del receptor NMDA regula la fosforilación de la proteína kinasa C (PKC). Este mecanismo de empalme de ARNm influye en la sensibilidad del receptor de glutamato y sugiere NR1.
Área de la Ciencia:
- La neurociencia es la neurociencia.
- Biología Molecular Biología Molecular
- Biología celular Biología celular.
Sus antecedentes:
- Los receptores NMDA son cruciales para las funciones cerebrales como la plasticidad sináptica.
- Se sugiere la fosforilación proteica de los receptores NMDA para modular su actividad.
- La subunidad NR1 del receptor NMDA está compuesta de subunidades homólogas.
Objetivo del estudio:
- Para investigar la fosforilación de la subunidad NR1 del receptor NMDA por la proteína quinasa C (PKC).
- Para determinar el papel del empalme alternativo en la fosforilación NR1.
- Para explorar la localización intracelular del dominio terminal C de NR1.
Principales métodos:
- Examinó la fosforilación NR1 por PKC en células que expresan el NR1 recombinante.
- Estudió la fosforilación NR1 en cultivos de neuronas corticales primarias.
- Se analizó el impacto del empalme alternativo en los sitios de fosforilación NR1.
Principales resultados:
- PKC fosforila el NR1 en varios sitios distintos.
- Muchos sitios de fosforilación se encuentran dentro de un exón empalmado alternativamente en el dominio terminal C de NR1.
- El empalme alternativo del ARNm NR1 regula su fosforilación por PKC.
Conclusiones:
- El empalme de ARNm es un nuevo mecanismo que controla la sensibilidad del receptor de glutamato a la fosforilación.
- El dominio C-terminal de NR1 está localizado de forma intracelular.
- El modelo de topología transmembrana propuesto para los receptores de glutamato puede necesitar revisión.
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