Tyrosine sulfation as a protein post-translational modification

Yuh Shyong Yang*, Chen Chu Wang, Bo Han Chen, You Hua Hou, Kuo Sheng Hung, Yi Chih Mao

*Corresponding author for this work

Research output: Contribution to journalJournal Article peer-review

99 Scopus citations


Integration of inorganic sulfate into biological molecules plays an important role in biological systems and is directly involved in the instigation of diseases. Protein tyrosine sulfation (PTS) is a common post-translational modification that was first reported in the literature fifty years ago. However, the significance of PTS under physiological conditions and its link to diseases have just begun to be appreciated in recent years. PTS is catalyzed by tyrosylprotein sulfotransferase (TPST) through transfer of an activated sulfate from 3′-phosphoadenosine-5′-phosphosulfate to tyrosine in a variety of proteins and peptides. Currently, only a small fraction of sulfated proteins is known and the understanding of the biological sulfation mechanisms is still in progress. In this review, we give an introductory and selective brief review of PTS and then summarize the basic biochemical information including the activity and the preparation of TPST, methods for the determination of PTS, and kinetics and reaction mechanism of TPST. This information is fundamental for the further exploration of the function of PTS that induces protein-protein interactions and the subsequent biochemical and physiological reactions.

Original languageEnglish
Pages (from-to)2138-2164
Number of pages27
Issue number2
StatePublished - 01 02 2015
Externally publishedYes

Bibliographical note

Publisher Copyright:
© 2015 by the authors; licensee MDPI, Basel, Switzerland.


  • 3′-phosphoadenosine 5′-phosphosulfate (PAPS)
  • Organic sulfate
  • Post-translational modification (PTM)
  • Protein tyrosine sulfation (PTS)
  • Sulfate
  • Tyrosylprotein sulfotransferase (TPST)


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