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

4 Citations (Scopus)

Abstract

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
Volume427
Issue number6 Part B
Early online date7 Feb 2015
DOIs
Publication statusPublished - 27 Mar 2015

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Golgi Apparatus
Transferases
Post Translational Protein Processing
Membranes
Sialyltransferases
Virus Internalization
Blood Coagulation
Enzymes
Adenosine
Sulfates
Ovum
Tyrosine
Catalytic Domain
Inflammation
Antibodies
protein-tyrosine sulfotransferase
Proteins

Keywords

  • TPST
  • SiaT
  • ST6
  • dimerization
  • BiFC

Cite this

Heterodimers of Tyrosylprotein Sulfotransferases Suggest Existence of a Higher Organization Level of Transferases in the Membrane of the trans-Golgi Apparatus. / Hartmann-Fatu, Christina; Trusch, Franziska; Moll, Carina N.; Michin, Irina; Hassinen, Antti; Kellokumpu, Sakari; Bayer, Peter.

In: Journal of Molecular Biology, Vol. 427, No. 6 Part B, 27.03.2015, p. 1404-1412.

Research output: Contribution to journalArticle

Hartmann-Fatu, Christina ; Trusch, Franziska ; Moll, Carina N. ; Michin, Irina ; Hassinen, Antti ; Kellokumpu, Sakari ; Bayer, Peter. / Heterodimers of Tyrosylprotein Sulfotransferases Suggest Existence of a Higher Organization Level of Transferases in the Membrane of the trans-Golgi Apparatus. In: Journal of Molecular Biology. 2015 ; Vol. 427, No. 6 Part B. pp. 1404-1412.
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abstract = "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.",
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AU - Kellokumpu, Sakari

AU - Bayer, Peter

N1 - Date of Acceptance: 27/01/2015 Acknowledgements We thank Tina Gerdes and Alma Rueppel for excellent technical support, Dr. Jonathan Mueller for fruitful discussions, the group of Professor Perihan Nalbant for their support with the confocal microscopy and the Deutsche Forschungsgemeinschaft for financial support (TRR-60/1, BA1624/4-1 and BA1624/4-2).

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N2 - 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.

AB - 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.

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