Isolated C-terminal tail of FGF23 alleviates hypophosphatemia by inhibiting FGF23-FGFR-Klotho complex formation.

@article{Goetz2010IsolatedCT,
  title={Isolated C-terminal tail of FGF23 alleviates hypophosphatemia by inhibiting FGF23-FGFR-Klotho complex formation.},
  author={Regina M Goetz and Yuji Nakada and Ming Chang Hu and Hiroshi Kurosu and Lei Wang and Teruyo Nakatani and Mingjun Shi and Anna V. Eliseenkova and Mohammed Shawkat Razzaque and Orson W Moe and Makoto Kuro-O and Moosa Mohammadi},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2010},
  volume={107 1},
  pages={407-12}
}
Fibroblast growth factor (FGF) 23 inhibits renal phosphate reabsorption by activating FGF receptor (FGFR) 1c in a Klotho-dependent fashion. The phosphaturic activity of FGF23 is abrogated by proteolytic cleavage at the RXXR motif that lies at the boundary between the FGF core homology domain and the 72-residue-long C-terminal tail of FGF23. Here, we show that the soluble ectodomains of FGFR1c and Klotho are sufficient to form a ternary complex with FGF23 in vitro. The C-terminal tail of FGF23… CONTINUE READING
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