Tyrosine Sulfation in Protein Post-Translational Modifications
Summary
Tyrosine sulfation is a widespread post-translational modification (PTM) that occurs in the secretory pathway of eukaryotic cells. Catalysed by tyrosylprotein sulfotransferases (TPST1 and TPST2) within the Golgi apparatus, it involves the transfer of a sulphate group from the universal donor 3′-phosphoadenosine 5′-phosphosulfate (PAPS) onto the phenolic hydroxyl of tyrosine residues. This negatively charged modification enhances and regulates extracellular protein–protein interactions, including hormone–receptor binding, chemokine signalling and blood-cell adhesion. The spatial clustering of sulphotyrosines within flexible acidic regions can create high-affinity binding interfaces, which are crucial in host–pathogen recognition, vascular biology and immunological responses. Recent advances in mass spectrometry, chemical biology and structural analysis have greatly expanded the known “sulfoproteome”, uncovering links between tyrosine sulfation and cardiovascular disease, chronic inflammation, and the design of next-generation therapeutics such as engineered antibodies and novel anticoagulants. The modification’s global significance lies in its capacity to fine-tune intercellular communication and its emerging utility in biotechnology and drug discovery.
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Tyrosine Sulfation in Protein Post-Translational Modifications publication trend
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Technical terms
Tyrosylprotein sulfotransferase (TPST): Golgi-resident enzymes (TPST1 and TPST2) that transfer sulphate from PAPS to tyrosine residues on proteins during maturation.
3′-Phosphoadenosine 5′-phosphosulfate (PAPS): The universal sulphate donor molecule used by sulfotransferases in sulphation reactions.
Post-translational modification (PTM): A covalent alteration of a protein after its synthesis, which can regulate its activity, localisation or interactions.
Sulfotyrosine: A tyrosine residue bearing a covalently attached sulphate group, imparting a negative charge and influencing molecular recognition.
Sulfoproteome: The subset of the proteome comprising all proteins that carry one or more sulfotyrosine modifications.
References
- Enhanced tyrosine sulfation is associated with chronic kidney disease-related atherosclerosis. BMC Biology (2023).
- Tyrosine Sulfation at Antibody Light Chain CDR-1 Increases Binding Affinity and Neutralization Potency to Interleukine-4. International Journal of Molecular Sciences (2024).
- Custom Workflow for the Confident Identification of Sulfotyrosine-Containing Peptides and Their Discrimination from Phosphopeptides. Journal of Proteome Research (2023).
- Sulfotyrosine residues: Interaction specificity determinants for extracellular protein–protein interactions. Journal of Biological Chemistry (2022).
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