Heterodimers of tyrosylprotein sulfotransferases suggest existence of a higher organization level of transferases in the membrane of the trans-Golgi apparatus.

@article{HartmannFatu2015HeterodimersOT,
  title={Heterodimers of tyrosylprotein sulfotransferases suggest existence of a higher organization level of transferases in the membrane of the trans-Golgi apparatus.},
  author={Cristina Hartmann-Fatu and F. Trusch and Carina N Moll and I. Michin and A. Hassinen and S. Kellokumpu and P. Bayer},
  journal={Journal of molecular biology},
  year={2015},
  volume={427 6 Pt B},
  pages={
          1404-1412
        }
}
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… Expand
Structural basis for the broad substrate specificity of the human tyrosylprotein sulfotransferase-1
TLDR
Two crystal structures of the human TPST1 complexed with two substrate peptides that are catalysed by human TP ST1 with significantly different efficiencies are reported, providing insight into the sulfation mechanism for these substrates. Expand
GOLPH3 and GOLPH3L are broad-spectrum COPI adaptors for sorting into intra-Golgi transport vesicles
TLDR
GOLPH3+3L are major COPI adaptors that impinge on most, if not all, of the glycosylation pathways of the Golgi, and interact with the cytoplasmic tails of their clients through membrane-proximal positively-charged residues. Expand
New tools for evaluating protein tyrosine sulfation: tyrosylprotein sulfotransferases (TPSTs) are novel targets for RAF protein kinase inhibitors
TLDR
A non-radioactive mobility-based enzymatic assay for TPST1 and TPST2, through which the tyrosine sulfation of synthetic fluorescent peptides can be rapidly quantified, and proposes that target-validated protein kinase inhibitors could be repurposed, or redesigned, as more-specific TPST inhibitors to help evaluate the sulfotyrosyl proteome. Expand
Glycosyltransferase complexes in eukaryotes: long-known, prevalent but still unrecognized
TLDR
Accumulated data for their prevalence and potential functional importance for glycosylation focusing mainly on their mutual interactions, the protein domains mediating these interactions, and enzymatic activity changes that occur upon complex formation are summarized. Expand
New tools for evaluating protein tyrosine sulphation: Tyrosyl Protein Sulphotransferases (TPSTs) are novel targets for RAF protein kinase inhibitors
TLDR
A non-radioactive mobility-based enzymatic assay for TPST1 and TPST2, through which the tyrosine sulphation of synthetic fluorescent peptides can be rapidly quantified, is described, suggesting new starting points to synthesise (or repurpose) small molecule compounds to evaluate biological TPST using chemical biology. Expand
Analysis of homologous and heterologous interactions between UDP-galactose transporter and beta-1,4-galactosyltransferase 1 using NanoBiT.
TLDR
The applicability of the NanoBiT system for studying homooligomerization of nucleotide sugar transporters and glycosyltransferases of the Golgi apparatus is demonstrated and a novel heterologous interaction between UDP-galactose transporter and beta-1,4-Galactosyltransferase 1 is reported. Expand
Determinants of tyrosylprotein sulfation coding and substrate specificity of tyrosylprotein sulfotransferases in metazoans.
This short review likes to give a historical view on the discovery of metazoan Tyrosylprotein Sulfotransferases (TPSTs) setting its focus on the determinants of substrate specificity of these enzymesExpand
GOLPH3 and GOLPH3L are broad-spectrum COPI adaptors for sorting into intra-Golgi transport vesicles
COPI vesicles recycle Golgi resident proteins within the Golgi stack. Welch et al. combine two orthogonal proteomic analyses to identify clients for the COPI adaptors GOLPH3 and GOLPH3L, and showExpand
Skeletal Dysplasias Caused by Sulfation Defects
TLDR
A panoramic view of skeletal dysplasias caused by mutations in genes encoding for transporters or enzymes involved in macromolecular sulfation is presented, allowing the development of targeted therapies aimed at alleviating, preventing, or modifying the disease progression. Expand

References

SHOWING 1-10 OF 30 REFERENCES
Existence of distinct tyrosylprotein sulfotransferase genes: molecular characterization of tyrosylprotein sulfotransferase-2.
TLDR
An approach to identify the TPST protein, referred to as MSC (modification after substrate crosslinking) labeling, which is based on the crossl linking of a substrate peptide to TPST followed by intramolecular [35S]sulfate transfer from the cosubstrate 3-phosphoadenosine 5'-phosphosulfate (PAPS). Expand
Tyrosylprotein sulfotransferase: purification and molecular cloning of an enzyme that catalyzes tyrosine O-sulfation, a common posttranslational modification of eukaryotic proteins.
TLDR
The purification of TPST from rat liver microsomes is described based on its affinity for the N-terminal 15 amino acids of PS GL-1, which defines a new class of Golgi sulfotransferases that may catalyze tyrosine O-sulfation of PSGL-1 and other protein substrates involved in diverse physiologic functions including inflammation and hemostasis. Expand
Human TPST1 transmembrane domain triggers enzyme dimerisation and localisation to the Golgi compartment.
TLDR
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. Expand
Tyrosine sulfation: an increasingly recognised post-translational modification of secreted proteins.
TLDR
The TPST enzymes are described, the detailed evidence supporting the importance of tyrosine sulfation in the cellular adhesion function of P-selectin glycoprotein ligand-1, the leukocyte trafficking and pathogen invasion functions of chemokine receptors and the ligand binding and activation of other G-protein-coupled receptors by complement proteins, phospholipdis and glycop Protein hormones are described. Expand
Crystal structure of human tyrosylprotein sulfotransferase-2 reveals the mechanism of protein tyrosine sulfation reaction
TLDR
The first crystal structure of the human TPST isoform 2 (TPST2) complexed with a substrate peptide derived from complement C4 and 3’-phosphoadenosine-5’ -phosphate (PAP) at 1.9Å resolution is presented. Expand
Golgi N-Glycosyltransferases Form Both Homo- and Heterodimeric Enzyme Complexes in Live Cells*
TLDR
This work investigates the supramolecular organization of the N-glycosylation pathway in live cells by utilizing the bimolecular fluorescence complementation approach and shows that all four N- glycosylated enzymes tested form Golgi-localized homodimers. Expand
In vivo expression and stoichiometric sulfation of the artificial protein sulfophilin, a polymer of tyrosine sulfation sites.
TLDR
The results indicate that the structural information contained in the heptapeptide motif is sufficient for stoichiometric tyrosine sulfation to occur in the living cell. Expand
Tyrosine sulfation of CCR5 N-terminal peptide by tyrosylprotein sulfotransferases 1 and 2 follows a discrete pattern and temporal sequence
TLDR
A detailed analysis of the multiple sulfation reaction of a peptide substrate by TPSTs is provided and provide a structural basis for understanding the role of tyrosine sulfation of CCR5 in HIV-1 coreceptor and chemokine receptor function. Expand
Intracellular trafficking and activation of the furin proprotein convertase: localization to the TGN and recycling from the cell surface.
TLDR
Pulse‐chase and immunofluorescence analyses demonstrated that proregion removal occurs in the endoplasmic reticulum and that cleavage may be required for exist from this compartment, and it is shown that pro region removal is necessary but not sufficient for enzyme activation. Expand
Two independent targeting signals in the cytoplasmic domain determine trans‐Golgi network localization and endosomal trafficking of the proprotein convertase furin.
TLDR
Results obtained on furin mutants with substitutions and deletions of amino acids in the cytoplasmic tail indicate that wild‐type furin is concentrated in the TGN by a mechanism involving two independent targeting signals, which consist of the acidic peptide CPSDSEEDEG783 and the tetrapeptide YKGL765. Expand
...
1
2
3
...