Heterodimers of Tyrosylprotein Sulfotransferases Suggest Existence of a Higher Organization Level of Transferases in the Membrane of the trans-Golgi Apparatus

Christina Hartmann-Fatu, Franziska Trusch, Carina N. Moll, Irina Michin, Antti Hassinen, Sakari Kellokumpu, Peter Bayer

Research output: Contribution to journalArticle

6 Citations (Scopus)


Tyrosine sulfation of proteins is an important post-translational modification shown to play a role in many membrane-associated or extracellular processes such as virus entry, blood clotting, antibody-mediated immune response, inflammation and egg fecundation. The sole two human enzymes that transfer sulfate moieties from 3'-phospho-adenosine-5'-phospho-sulfate onto tyrosine residues, TPST1 and TPST2, are anchored to the membranes of the trans-Golgi compartment with the catalytic domain oriented to the lumen. In contrast to the relatively well studied organization of medial Golgi enzymes, the organization of trans-Golgi transferases remains elusive. Although tyrosylprotein sulfotransferases are known to exist as homodimers in the Golgi membranes, this organization level may represent only a small piece of a puzzle that is linked to the entire picture. Here we report the formation of TPST1/TPST2 heterodimers and a novel interaction between either TPST1 or TPST2 and the α-2,6-sialyltransferase, indicating a higher organization level of tyrosylprotein sulfotransferases that may serve for substrate selectivity and/or effective organization of multiple post-translational modification of proteins.
Original languageEnglish
Pages (from-to)1404-1412
Number of pages9
JournalJournal of Molecular Biology
Issue number6 Part B
Early online date7 Feb 2015
Publication statusPublished - 27 Mar 2015



  • TPST
  • SiaT
  • ST6
  • dimerization
  • BiFC

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