Protein tyrosine sulfation, 1993--an update.
Sulfation is the most abundant post-translational modification of tyrosine residues and occurs in many soluble and membrane proteins passing through the secretory pathway of metazoan cells. The sulfation reaction is catalysed by tyrosylprotein sulfotransferase, a membrane-bound enzyme of the trans-Golgi-network. Tyrosylprotein sulfotransferase has been purified and its substrate specificity characterized. Tyrosine sulfation has been shown to be important for protein-protein interactions occurring during the intracellular transport of proteins and upon their secretion.
Institute for Neurobiology, University of Heidelberg, Germany.
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D000818:Animals; D006056:Golgi Apparatus / Q000201:enzymology; D006801:Humans; D008970:Molecular Weight; D014176:Protein Biosynthesis / Q000235:genetics; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000378:metabolism*; D013379:Substrate Specificity; D013431:Sulfates / Q000378:metabolism; D015238:Sulfotransferases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D014443:Tyrosine / Q000378:metabolism*
D011506:Proteins; D013431:Sulfates; D014443:Tyrosine; D015238:Sulfotransferases; C039079:protein-tyrosine sulfotransferase