The study presents cryo-electron microscopy structures of human XPR1 in various forms, revealing critical insights into its role in phosphate efflux and InsPP regulation.
XPR1's structural composition includes an N-terminal SPX domain, a core domain for dimer formation, and a transport domain essential for phosphate binding and transport.
The SPX domain's interaction with InsP6 is crucial, as it aids phosphate efflux by displacing a C-terminal loop that otherwise restricts phosphate entry into the transport domain.
Understanding XPR1's mechanisms provides a conceptual framework for phosphate homeostasis regulation across different organisms, including fungi, plants, and animals.
#phosphate-homeostasis #xpr1 #cryo-electron-microscopy #cellular-biology #neurodegenerative-diseases
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