Human TPST1 transmembrane domain triggers enzyme dimerisation and localisation to the Golgi compartment

Sandra Goettsch, Rodica A Badea, Jonathan W Mueller, Christoph Wotzlaw, Beate Schoelermann, Lars Schulz, Matthias Rabiller, Peter Bayer, Cristina Hartmann-Fatu

Research output: Contribution to journalArticlepeer-review

21 Citations (Scopus)


TPST1 is a human tyrosylprotein sulfotransferase that uses 3'phosphoadenosine-5'phosphosulfate (PAPS) to transfer the sulfate moiety to proteins predominantly designated for secretion. To achieve a general understanding of the cellular role of human tyrosine-directed sulfotransferases, we investigated targeting, structure and posttranslational modification of TPST1. Golgi localisation of the enzyme in COS-7 and HeLa cells was visualised by fluorescence imaging techniques. PNGase treatment and mutational studies determined that TPST1 bears N-linked glycosyl residues exclusively at position Asn60 and Asn262. By alanine mutation of these asparagine residues, we could determine that the N-linked oligosaccharides do not have an influence on Golgi retention of TPST1. In concert with N and C-terminal flanking residues, the transmembrane domain of TPST1 was determined to act in targeting and retention of the enzyme to the trans-Golgi compartment. This domain exhibits a pronounced secondary structure in a lipid environment. Further in vivo FRET studies using the transmembrane domain suggest that the human tyrosylprotein sulfotransferase may be functional as homodimer/oligomer in the trans-Golgi compartment.

Original languageEnglish
Pages (from-to)436-49
Number of pages14
JournalJournal of Molecular Biology
Issue number3
Publication statusPublished - 18 Aug 2006


  • Amino Acid Sequence
  • Animals
  • Asparagine
  • Autoantigens
  • COS Cells
  • Cercopithecus aethiops
  • Dimerization
  • Fluorescence Resonance Energy Transfer
  • Glycosylation
  • Golgi Apparatus
  • HeLa Cells
  • Humans
  • Intracellular Membranes
  • Molecular Sequence Data
  • Mutation
  • Oligosaccharides
  • Protein Binding
  • Protein Processing, Post-Translational
  • Protein Structure, Tertiary
  • Sulfotransferases


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