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FGF23 is endogenously phosphorylated in bone cells.

Iris Lindberg1, Hong Weng Pang, Joseph P Stains

  • 1Department of Anatomy and Neurobiology, University of Maryland School of Medicine, Baltimore, MD, USA.

Journal of Bone and Mineral Research : the Official Journal of the American Society for Bone and Mineral Research
|September 9, 2014
PubMed
Summary
This summary is machine-generated.

Fibroblast growth factor 23 (FGF23) is phosphorylated in bone osteocytes, a process potentially affecting its stability and role in phosphate regulation. This study identifies key phosphorylation sites on FGF23, revealing its natural modification in bone.

Keywords:
BONEFAM20CFGF23KINASEOSTEOCYTEPHOSPHATE HOMEOSTASIS

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Area of Science:

  • Molecular Endocrinology
  • Bone Biology
  • Biochemistry

Background:

  • Serum phosphate homeostasis is regulated by fibroblast growth factor 23 (FGF23), a bone-derived peptide hormone.
  • Dysregulation of FGF23 is implicated in hypophosphatemic disorders and chronic kidney disease.
  • FGF23 undergoes O-glycosylation, and its potential for phosphorylation in secretion pathways was unexplored.

Purpose of the Study:

  • To investigate whether FGF23 is a substrate for secretory phosphorylation.
  • To identify specific phosphorylation sites on the FGF23 protein.
  • To explore the functional implications of FGF23 phosphorylation in bone.

Main Methods:

  • Radiolabeling studies using HEK and IDG-SW3 cells to detect orthophosphate incorporation into FGF23.
  • Site-directed mutagenesis of serine residues within kinase consensus sequences.
  • Liquid chromatography-coupled mass spectrometry (LC-MS) for phosphosite identification.
  • Development of a phospho-specific antibody for detecting phosphorylated FGF23 in bone tissue.

Main Results:

  • Intact FGF23 and its carboxy-terminal fragment were phosphorylated in cellular models.
  • Phosphorylation occurred at Ser180, Ser207, and Ser212 within the carboxy-terminal fragment.
  • LC-MS confirmed phosphorylation at Ser212, and a phospho-specific antibody detected phospho-FGF23 in osteocytes.
  • Co-expression with FAM20C kinase enhanced FGF23 storage and release, suggesting phosphorylation impacts FGF23 stability.

Conclusions:

  • FGF23 is a naturally phosphorylated protein in bone osteocytes.
  • Specific serine residues, particularly Ser212, are key sites of FGF23 phosphorylation.
  • Phosphorylation by FAM20C may influence FGF23 stability and secretion, highlighting a novel regulatory mechanism.