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Interacción dinámica de los TARP similares a la estargazina con los receptores AMPA en ciclo en las sinapsis
Susumu Tomita1, Masaki Fukata, Roger A Nicoll
1Department of Physiology, University of California, San Francisco, San Francisco, CA 94143-2140, USA.
Science (New York, N.Y.)
|March 6, 2004
Resumen
Las proteínas reguladoras del receptor AMPA transmembrana (TARP) controlan la plasticidad cerebral mediante la estabilización de los receptores AMPA. La unión al glutamato hace que los receptores AMPA se desprendan de los TARP, lo que facilita su internalización.
Área de la Ciencia:
- La neurociencia es la neurociencia.
- Biología Molecular Biología Molecular
- Biología celular Biología celular.
Sus antecedentes:
- La plasticidad dependiente de la actividad, crucial para el aprendizaje y la memoria, implica regular el número de receptores sinápticos de AMPA.
- Las proteínas reguladoras del receptor AMPA transmembrana (TARP), incluida la stargazina, son reguladores clave del tráfico de receptores AMPA en las sinapsis.
Objetivo del estudio:
- Investigar el mecanismo molecular por el cual el glutamato regula el tráfico de receptores AMPA a través de TARPs.
- Para determinar el papel de las interacciones del receptor TARP-AMPA en la plasticidad sináptica.
Principales métodos:
- Se utilizaron ensayos celulares y bioquímicos para examinar la estabilidad e interacciones de las TARP y los receptores AMPA.
- Investigó el efecto de la unión del glutamato en el complejo del receptor TARP-AMPA.
- Evaluó el requisito de flujo iónico y segundos mensajeros en la disociación del receptor.
Principales resultados:
- Los TARP permanecen estables en la membrana plasmática, mientras que los receptores AMPA se internalizan.
- La internalización del receptor AMPA está regulada por el glutamato.
- La unión al glutamato induce la disociación de los receptores AMPA de los TARP, involucrando tanto los dominios extracelulares como los intracelulares de los TARP.
- Esta disociación ocurre independientemente del flujo iónico o de las vías de señalización intracelular.
Conclusiones:
- Un nuevo mecanismo alostérico explica la disociación del receptor AMPA mediado por glutamato de los TARP.
- Este mecanismo probablemente contribuye a la internalización dependiente de la actividad de los receptores AMPA durante la plasticidad sináptica.
- Comprender este proceso ofrece información sobre las bases moleculares del aprendizaje y la memoria.
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