Reactome | GALNT3 transfers GalNAc to FGF23

GALNT3 transfers GalNAc to FGF23

Stable Identifier

R-HSA-8851619

Type

Reaction [transition]

Species

Homo sapiens

Compartment

Golgi lumen, Golgi membrane

ReviewStatus

5/5

Locations in the PathwayBrowser

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Signal Transduction (Homo sapiens)

- Signaling by Receptor Tyrosine Kinases (Homo sapiens)
  - Signaling by FGFR (Homo sapiens)
    - Signaling by FGFR3 (Homo sapiens)
      - FGFR3 ligand binding and activation (Homo sapiens)
        
        FGFR3c ligand binding and activation (Homo sapiens)
        
        GALNT3 transfers GalNAc to FGF23 (Homo sapiens)

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Fibroblast growth factor 23 (FGF23, aka phosphatonin) is a regulator of phosphate homeostasis and vitamin D metabolism. Its effects are thought to be mediated via the FGFR3c receptor. Glycosylation is necessary for FGF23 secretion from the cell and that is mediated by polypeptide N-acetylgalactosaminyltransferase 3 (GALNT3), which transfers an N-acetylgalactosaminyl (GalNAc) moiety from a high energy donor to threonine 178 on FGF23 (Kato et al. 2006). Competition between proprotein convertase cleavage and O-glycosylation determines the level of secreted active FGF23.

Literature References

PubMed ID	Title	Journal	Year
16638743	Polypeptide GalNAc-transferase T3 and familial tumoral calcinosis. Secretion of fibroblast growth factor 23 requires O-glycosylation Kato, K, Jeanneau, C, Tarp, MA, Benet-Pages, A, Lorenz-Depiereux, B, Bennett, EP, Mandel, U, Strom, TM, Clausen, H	J. Biol. Chem.	2006