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ATP-binding cassette or ABC transporter is the largest superfamily of integral membrane proteins. The transporters have transmembrane-binding domains (TMDs) and nucleotide-binding domains (NBDs). The TMDs are specific to their substrates, whereas the NBDs are similar to engines that complete ATP hydrolysis to complete the substrate transport. They can be full transporters consisting of two TMDs and NBDs, half transporters with one TMD and NBD, while some encoded with a single TMD or NBD are...
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The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
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Las estructuras humanas de XPR1 revelan el mecanismo de exportación de fosfato

Rui Yan1,2, Huiwen Chen1,3, Chuanyu Liu1,4

  • 1Laboratory of Soft Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing, China.

Nature
|August 21, 2024
PubMed
Resumen

Los investigadores descubrieron la estructura del XPR1 humano, revelando cómo transporta fosfato (Pi) y está regulado por los polifosfatos de inositol (InsPP). Esto proporciona un marco para comprender la homeostasis de fosfato celular.

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Área de la Ciencia:

  • La bioquímica
  • Biología estructural
  • Biología celular

Sus antecedentes:

  • El fosfato inorgánico (Pi) es esencial para la vida, y su homeostasis es crítica.
  • XPR1 es el único exportador humano conocido de Pi, vital para el equilibrio celular de Pi.
  • La disfunción de XPR1 está relacionada con enfermedades neurodegenerativas, lo que pone de relieve su importancia.

Objetivo del estudio:

  • Para aclarar los mecanismos estructurales del flujo de Pi mediado por XPR1.
  • Para comprender la regulación de XPR1 por los polifosfatos de inositol intracelulares (InsPP).
  • Proporcionar una base estructural para la detección de puertas XPR1 y InsPP.

Principales métodos:

  • Se utilizó la criomicroscopia electrónica (Cryo-EM) para determinar las estructuras de la XPR1 humana.
  • Se obtuvieron estructuras para estados cerrados y abiertos ligados a Pi y formas ligadas a InsP6.

Principales resultados:

  • La estructura revela que XPR1 comprende un dominio SPX, un dominio central y un dominio de transporte Pi.
  • Tres grupos básicos en el dominio del transporte son clave para la unión y el transporte de Pi.
  • Un triptófano conservado (W573) actúa como un interruptor de entrada, y el dominio SPX regula el transporte de Pi a través de la unión InsP6.

Conclusiones:

  • El estudio proporciona estructuras de alta resolución de XPR1, detallando su entrada y regulación.
  • Este trabajo ofrece una comprensión mecanicista de la homeostasis Pi mediada por XPR1 y sus homólogos.
  • Los hallazgos sientan las bases para futuras investigaciones sobre la función de XPR1 y enfermedades relacionadas.