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Protein tyrosine sulfation, 1993--an update
C Niehrs1, R Beisswanger, W B Huttner
1Institute for Neurobiology, University of Heidelberg, Germany.
Chemico-Biological Interactions
|June 1, 1994
Summary
Tyrosine sulfation, a common protein modification, is crucial for protein interactions during cellular transport and secretion. This process is catalyzed by the enzyme tyrosylprotein sulfotransferase.
Area of Science:
- Biochemistry
- Cell Biology
- Molecular Biology
Background:
- Sulfation is the most abundant post-translational modification of tyrosine residues.
- This modification occurs in soluble and membrane proteins within the secretory pathway of metazoan cells.
Purpose of the Study:
- To investigate the role of tyrosine sulfation in protein function.
- To characterize the enzyme responsible for tyrosine sulfation.
Main Methods:
- Purification of tyrosylprotein sulfotransferase.
- Characterization of enzyme substrate specificity.
Main Results:
- Tyrosylprotein sulfotransferase, a trans-Golgi-network enzyme, catalyzes tyrosine sulfation.
- The enzyme's substrate specificity was determined.
- Tyrosine sulfation is vital for protein-protein interactions in intracellular transport and secretion.
Conclusions:
- Tyrosine sulfation is a key post-translational modification regulating protein interactions.
- Tyrosylprotein sulfotransferase plays a critical role in this essential cellular process.