Gene Symbol: Galnt2
Description: polypeptide N-acetylgalactosaminyltransferase 2
Alias: polypeptide N-acetylgalactosaminyltransferase 2, UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 2 (GalNAc-T2)
Species: rat
Products:     Galnt2

Top Publications

  1. Storrie B, White J, Rottger S, Stelzer E, Suganuma T, Nilsson T. Recycling of golgi-resident glycosyltransferases through the ER reveals a novel pathway and provides an explanation for nocodazole-induced Golgi scattering. J Cell Biol. 1998;143:1505-21 pubmed
    ..In conclusion, we have shown that Golgi-resident glycosylation enzymes recycle through the ER and that this novel pathway is the likely explanation for the nocodazole-induced Golgi scattering observed in interphase cells. ..
  2. Fritz T, Raman J, Tabak L. Dynamic association between the catalytic and lectin domains of human UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase-2. J Biol Chem. 2006;281:8613-9 pubmed
    ..The structure of the hT2-UDP-EA2 complex also resolves long standing questions regarding ppGalNAcT acceptor substrate specificity. ..
  3. Perrine C, Ganguli A, Wu P, Bertozzi C, Fritz T, Raman J, et al. Glycopeptide-preferring polypeptide GalNAc transferase 10 (ppGalNAc T10), involved in mucin-type O-glycosylation, has a unique GalNAc-O-Ser/Thr-binding site in its catalytic domain not found in ppGalNAc T1 or T2. J Biol Chem. 2009;284:20387-97 pubmed publisher
    ..Our results reveal that these transferases have unique peptide and glycopeptide preferences demonstrating their substrate diversity and their likely roles ranging from initiating transferases to filling-in transferases. ..
  4. Wandall H, Hassan H, Mirgorodskaya E, Kristensen A, Roepstorff P, Bennett E, et al. Substrate specificities of three members of the human UDP-N-acetyl-alpha-D-galactosamine:Polypeptide N-acetylgalactosaminyltransferase family, GalNAc-T1, -T2, and -T3. J Biol Chem. 1997;272:23503-14 pubmed
    ..The results demonstrate that individual GalNAc-transferases have distinct activities and the initiation of O-glycosylation in a cell is regulated by a repertoire of GalNAc-transferases. ..
  5. ARGUESO P, Tisdale A, Mandel U, Letko E, Foster C, Gipson I. The cell-layer- and cell-type-specific distribution of GalNAc-transferases in the ocular surface epithelia is altered during keratinization. Invest Ophthalmol Vis Sci. 2003;44:86-92 pubmed
    ..This early increase in isoenzymes in nonkeratinized OCP epithelia is reduced as keratinization proceeds in the disease. ..
  6. Khetarpal S, Schjoldager K, Christoffersen C, Raghavan A, Edmondson A, Reutter H, et al. Loss of Function of GALNT2 Lowers High-Density Lipoproteins in Humans, Nonhuman Primates, and Rodents. Cell Metab. 2016;24:234-45 pubmed publisher
    Human genetics studies have implicated GALNT2, encoding GalNAc-T2, as a regulator of high-density lipoprotein cholesterol (HDL-C) metabolism, but the mechanisms relating GALNT2 to HDL-C remain unclear...
  7. Iwasaki H, Zhang Y, Tachibana K, Gotoh M, Kikuchi N, Kwon Y, et al. Initiation of O-glycan synthesis in IgA1 hinge region is determined by a single enzyme, UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 2. J Biol Chem. 2003;278:5613-21 pubmed
    ..We found that pp-GalNAc-T2 selectively transferred GalNAc residues to the same five positions. These results strongly suggested that pp-GalNAc-T2 is an essential enzyme for initiation of O-linked glycosylation of the IgA1 hinge region. ..
  8. Raman J, Fritz T, Gerken T, Jamison O, Live D, Liu M, et al. The catalytic and lectin domains of UDP-GalNAc:polypeptide alpha-N-Acetylgalactosaminyltransferase function in concert to direct glycosylation site selection. J Biol Chem. 2008;283:22942-51 pubmed publisher
    ..Local sequence recognition by the catalytic domain differs between hT2 and hT10 in that hT10 requires a pre-existing GalNAc residue while hT2 does not. ..
  9. Goth C, Tuhkanen H, Khan H, Lackman J, Wang S, Narimatsu Y, et al. Site-specific O-Glycosylation by Polypeptide N-Acetylgalactosaminyltransferase 2 (GalNAc-transferase T2) Co-regulates β1-Adrenergic Receptor N-terminal Cleavage. J Biol Chem. 2017;292:4714-4726 pubmed publisher
    ..The results provide a new level of β1AR regulation that may open up possibilities for new therapeutic strategies for cardiovascular diseases. ..