Mass spectrometry (MS)-based proteomics and the sulfome: clinical potential

Area of Science:

• Biochemistry and Molecular Biology
• Proteomics
• Post-Translational Modifications

Background:

• Protein tyrosine sulfation is a significant post-translational modification (PTM) catalyzed by TPST1 and TPST2.
• This modification plays key roles in inflammation, immunity, hemostasis, and viral entry by modulating protein interactions.
• Despite its importance, tyrosine sulfation is underrepresented in databases due to limited analytical strategies.

Purpose of the Study:

• To review the biological roles of protein sulfation by TPSTs.
• To discuss current and emerging analytical approaches for characterizing sulfated residues, including tyrosine and cysteine.
• To explore the clinical applicability of protein sulfation characterization strategies.

Main Methods:

• Review of existing literature on protein sulfation.
• Discussion of mass spectrometry (MS)-based proteomics techniques for PTM discovery.
• Exploration of analytical strategies for identifying and quantifying sulfated residues.

Main Results:

• Recent advances in MS have enhanced the sensitivity for detecting tyrosine sulfation, expanding the known 'sulfome.'
• Systematic profiling of sulfated residues is now feasible, aiding in understanding their regulatory functions.
• The field is poised for clinical translation due to improved characterization methods.

Conclusions:

• Protein tyrosine sulfation is a critical PTM with significant biological and clinical implications.
• Advanced MS-based proteomics offers powerful tools for comprehensive sulfation analysis.
• Further exploration of protein sulfation in clinical contexts holds promise for novel therapeutics.