CHST4 transfers SO4(2-) from PAPS to Core 2 mucins

Stable Identifier
Reaction [transition]
Homo sapiens
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Carbohydrate sulfotransferase 4 (CHST4) transfers sulfate (SO4(2-)) from the high energy donor 3'-phospho-5'-adenylyl sulfate (PAPS) to position 6 of non-reducing N-acetylglucosamine (GlcNAc) residues of mucin-associated glycans that ultimately serve as SELL ligands which are present in high endothelial cells (HEVs) and play a central role in lymphocyte homing at sites of inflammation. CHST4 preferentially sulfates Core 2 mucins (Bistrup et al. 1999). CHST4 is localised to the Golgi membrane (de Graffenried & Bertozzi 2004).

Literature References
PubMed ID Title Journal Year
12855678 Golgi localization of carbohydrate sulfotransferases is a determinant of L-selectin ligand biosynthesis

Bertozzi, CR, de Graffenried, CL

J. Biol. Chem. 2003
10330415 Sulfotransferases of two specificities function in the reconstitution of high endothelial cell ligands for L-selectin

Kannagi, R, Huang, CC, Hemmerich, S, Rosen, SD, Gunn, MD, Bistrup, A, Bhakta, S, Belov, YY, Zuo, FR, Lee, JK

J. Cell Biol. 1999
Catalyst Activity

N-acetylglucosamine 6-O-sulfotransferase activity of CHST4 [Golgi membrane]

Orthologous Events
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