Tyrosine Sulfation

The O-sulfation of tyrosine residues of membrane and secretory proteins that transit through the secretory pathway of eukaryotic cells is a ubiquitous posttranslational modification conserved in all multicellular organisms. Tyrosine sulfation is catalyzed by tyrosylprotein sulfotransferase (TPST) isoenzymes, which are integral membrane proteins of the trans-Golgi network. Tyrosine sulfation has been shown to be important for protein–protein interactions occurring in diverse biological processes, ranging from the receptor binding of regulatory peptides to the interaction of viral envelope proteins with the cell surface