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Human XPR1 structures reveal phosphate export mechanism.

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|August 21, 2024
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This summary is machine-generated.

Researchers uncovered the structure of human XPR1, revealing how it transports phosphate (Pi) and is regulated by inositol polyphosphates (InsPPs). This provides a framework for understanding cellular phosphate homeostasis.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Cellular Biology

Background:

  • Inorganic phosphate (Pi) is essential for life, and its homeostasis is critical.
  • XPR1 is the sole known human Pi exporter, vital for cellular Pi balance.
  • XPR1 dysfunction is linked to neurodegenerative diseases, highlighting its importance.

Purpose of the Study:

  • To elucidate the structural mechanisms of XPR1-mediated Pi efflux.
  • To understand the regulation of XPR1 by intracellular inositol polyphosphates (InsPPs).
  • To provide a structural basis for XPR1 gating and InsPP sensing.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) was used to determine the structures of human XPR1.
  • Structures were obtained for Pi-bound closed and open states, and InsP6-bound forms.

Main Results:

  • The structure reveals XPR1 comprises an SPX domain, a core domain, and a Pi transport domain.
  • Three basic clusters in the transport domain are key for Pi binding and transport.
  • A conserved tryptophan (W573) acts as a gating switch, and the SPX domain regulates Pi transport via InsP6 binding.

Conclusions:

  • The study provides high-resolution structures of XPR1, detailing its gating and regulation.
  • This work offers a mechanistic understanding of Pi homeostasis mediated by XPR1 and its homologs.
  • The findings lay the groundwork for future research into XPR1 function and related diseases.