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Tyrosine sulfation and the secretory pathway
1Cell Biology Program, European Molecular Biology Laboratory, Heidelberg, Federal Republic of Germany.
Annual Review of Physiology
|January 1, 1988
Summary
Tyrosine sulfation, a key protein modification, impacts secretory proteins like neuropeptides. This irreversible process, occurring late in the Golgi, affects protein transport and activity, with chlorate offering a new research tool.
Area of Science:
- Biochemistry
- Molecular Biology
- Cell Biology
Background:
- Tyrosine sulfation is a prevalent posttranslational modification.
- Primarily observed in secretory proteins, including neuropeptides.
- Occurs in the trans-Golgi network as a late protein processing step.
Purpose of the Study:
- To summarize the current understanding of tyrosine sulfation.
- To highlight its impact on protein function and transport.
- To introduce chlorate as a tool for future research.
Main Methods:
- Review of existing literature on tyrosine sulfation.
- Identification of key enzymes and substrates.
- Discussion of the implications of tyrosine sulfation.
Main Results:
- Tyrosine sulfation is catalyzed by tyrosylprotein sulfotransferase.
- The modification is generally irreversible, altering protein phenotype.
- It influences intracellular transport kinetics and neuropeptide activity.
Conclusions:
- Tyrosine sulfation plays a significant role in the function of secretory proteins.
- Understanding this modification is crucial for various biological processes.
- Chlorate presents a promising, non-toxic inhibitor for studying sulfation in cellular systems.
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