title: Heterodimers of tyrosylprotein sulfotransferases suggest existence of a higher organization level of transferases in the membrane of the trans-Golgi apparatus.
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.
authors: Department of Structural and Medicinal Biochemistry, University of Duisburg-Essen, Universitaetsstrasse 2, 45141 Essen, Germany. Electronic address: Cristina.hartmann_fatu@uni-due.de.
authors: Cristina
authors: C
authors: Hartmann-Fatu
authors: Department of Structural and Medicinal Biochemistry, University of Duisburg-Essen, Universitaetsstrasse 2, 45141 Essen, Germany. Electronic address: franziska.trusch@abdn.ac.uk.
authors: Franziska
authors: F
authors: Trusch
authors: Department of Developmental Biology, University of Duisburg-Essen, Universitaetsstrasse 2, 45141 Essen, Germany. Electronic address: carina.moll@uni-due.de.
authors: Carina N
authors: CN
authors: Moll
authors: Department of Structural and Medicinal Biochemistry, University of Duisburg-Essen, Universitaetsstrasse 2, 45141 Essen, Germany. Electronic address: Irina.michin@uni-due.de.
authors: Irina
authors: I
authors: Michin
authors: Faculty of Biochemistry and Molecular Medicine, University of Oulu, Aapistie 7A, FI-90220 Oulu, Finland. Electronic address: antti.hassinen@oulu.fi.
authors: Antti
authors: A
authors: Hassinen
authors: Faculty of Biochemistry and Molecular Medicine, University of Oulu, Aapistie 7A, FI-90220 Oulu, Finland. Electronic address: sakari.kellokumpu@oulu.fi.
authors: Sakari
authors: S
authors: Kellokumpu
authors: Department of Structural and Medicinal Biochemistry, University of Duisburg-Essen, Universitaetsstrasse 2, 45141 Essen, Germany. Electronic address: peter.bayer@uni-due.de.
authors: Peter
authors: P
authors: Bayer
mesh_terms: D015153:Blotting, Western; D002462:Cell Membrane / Q000378:metabolism*; D019084:Fluorescent Antibody Technique, Indirect; D006056:Golgi Apparatus / Q000378:metabolism*; D006367:HeLa Cells; D006801:Humans; D047468:Immunoprecipitation; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism*; D055503:Protein Multimerization; D011499:Protein Processing, Post-Translational; D012799:Sialyltransferases / Q000737:chemistry* / Q000378:metabolism*; D015238:Sulfotransferases / Q000737:chemistry* / Q000378:metabolism*; D014443:Tyrosine / Q000031:analogs & derivatives / Q000378:metabolism; D000094802:beta-D-Galactoside alpha 2-6-Sialyltransferase
chemical_list: D008565:Membrane Proteins; C005662:tyrosine O-sulfate; D014443:Tyrosine; D012799:Sialyltransferases; D015238:Sulfotransferases; C114740:TPST2 protein, human; C039079:protein-tyrosine sulfotransferase; D000094802:beta-D-Galactoside alpha 2-6-Sialyltransferase
keywords: BiFC; ST6; SiaT; TPST; dimerization