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Expression and Purification of the Human Lipid-sensitive Cation Channel TRPC3 for Structural Determination by Single-particle Cryo-electron Microscopy
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Estructuras del canal TRPML1 humano en conformaciones abiertas y cerradas

Philip Schmiege1,2, Michael Fine3, Günter Blobel1

  • 1Laboratory of Cell Biology, Howard Hughes Medical Institute, The Rockefeller University, New York, New York 10065, USA.

Nature
|October 12, 2017
PubMed
Resumen

Los investigadores revelaron la estructura del canal de mucolipina potencial del receptor transitorio 1 (TRPML1) en estados cerrados y abiertos. Esto proporciona información sobre la señalización del calcio, la función lisosómica y la mucolipidosis tipo IV.

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Área de la Ciencia:

  • Biología estructural
  • Biología molecular
  • Biología celular

Sus antecedentes:

  • La mucolipina potencial del receptor transitorio 1 (TRPML1) es un canal de liberación de calcio crucial para la señalización de calcio lisosomal y la homeostasis.
  • La disfunción de TRPML1 causa mucolipidosis tipo IV, un trastorno de almacenamiento lisosomal severo.

Objetivo del estudio:

  • Determinar las estructuras de alta resolución de TRPML1 humano de cuerpo entero tanto en estado cerrado como abierto.
  • Aclarar los mecanismos moleculares subyacentes a la regulación y activación del canal TRPML1.
  • Proporcionar información sobre las bases estructurales de la mucolipidosis tipo IV.

Principales métodos:

  • Se utilizó la crio-microscopia electrónica (cryo-EM) para obtener estructuras de TRPML1 humano.
  • Se determinaron las estructuras para el estado apo (cerrado) a pH 7.0 y el estado ligado al agonista (abierto) a pH 6.0.

Principales resultados:

  • Se resolvieron dos estructuras cryo-EM distintas de TRPML1 humano a alta resolución (3,72 Å y 3,49 Å).
  • Se identificó una cavidad hidrofóbica única formada por residuos específicos en las hélices S5, S6 y la hélice del poro 1 como el sitio de unión del agonista.
  • La apertura del canal implica la dilatación de la puerta inferior y los desplazamientos estructurales en la hélice del poro 1.

Conclusiones:

  • El estudio revela el mecanismo regulador de los canales TRPML y su proceso de activación.
  • Los hallazgos ofrecen una comprensión molecular de la patogénesis de la mucolipidosis tipo IV.
  • Este trabajo avanza en la comprensión de la función y la regulación del canal TRP.