Polypeptide <i>N</i>-acetylgalactosaminyltransferase-Associated Phenotypes in Mammals
Mucin-type <i>O</i>-glycosylation involves the attachment of glycans to an initial <i>O</i>-linked <i>N</i>-acetylgalactosamine (GalNAc) on serine and threonine residues on proteins. This process in mammals is initiated and regulated by a large family of 20 UDP-Ga...
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MDPI AG
2021-09-01
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| Series: | Molecules |
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| Online Access: | https://www.mdpi.com/1420-3049/26/18/5504 |
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| author | Kentaro Kato Lars Hansen Henrik Clausen |
| author_facet | Kentaro Kato Lars Hansen Henrik Clausen |
| author_sort | Kentaro Kato |
| collection | DOAJ |
| description | Mucin-type <i>O</i>-glycosylation involves the attachment of glycans to an initial <i>O</i>-linked <i>N</i>-acetylgalactosamine (GalNAc) on serine and threonine residues on proteins. This process in mammals is initiated and regulated by a large family of 20 UDP-GalNAc: polypeptide <i>N</i>-acetylgalactosaminyltransferases (GalNAc-Ts) (EC 2.4.1.41). The enzymes are encoded by a large gene family (<i>GALNT</i>s). Two of these genes, <i>GALNT2</i> and <i>GALNT3</i>, are known as monogenic autosomal recessive inherited disease genes with well characterized phenotypes, whereas a broad spectrum of phenotypes is associated with the remaining 18 genes. Until recently, the overlapping functionality of the 20 members of the enzyme family has hindered characterizing the specific biological roles of individual enzymes. However, recent evidence suggests that these enzymes do not have full functional redundancy and may serve specific purposes that are found in the different phenotypes described. Here, we summarize the current knowledge of <i>GALNT</i> and associated phenotypes. |
| first_indexed | 2024-03-10T07:24:00Z |
| format | Article |
| id | doaj.art-4002194119fc4628bdfab5b95149e51e |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-03-10T07:24:00Z |
| publishDate | 2021-09-01 |
| publisher | MDPI AG |
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| series | Molecules |
| spelling | doaj.art-4002194119fc4628bdfab5b95149e51e2023-11-22T14:24:08ZengMDPI AGMolecules1420-30492021-09-012618550410.3390/molecules26185504Polypeptide <i>N</i>-acetylgalactosaminyltransferase-Associated Phenotypes in MammalsKentaro Kato0Lars Hansen1Henrik Clausen2Department of Eco-Epidemiology, Institute of Tropical Medicine, Nagasaki University, 1-12-4 Sakamoto, Nagasaki 852-8523, JapanCopenhagen Center for Glycomics, Department of Cellular and Molecular Medicine, Mærsk Building, University of Copenhagen, Blegdamsvej 3B, 2200 Copenhagen N, DenmarkCopenhagen Center for Glycomics, Department of Cellular and Molecular Medicine, Mærsk Building, University of Copenhagen, Blegdamsvej 3B, 2200 Copenhagen N, DenmarkMucin-type <i>O</i>-glycosylation involves the attachment of glycans to an initial <i>O</i>-linked <i>N</i>-acetylgalactosamine (GalNAc) on serine and threonine residues on proteins. This process in mammals is initiated and regulated by a large family of 20 UDP-GalNAc: polypeptide <i>N</i>-acetylgalactosaminyltransferases (GalNAc-Ts) (EC 2.4.1.41). The enzymes are encoded by a large gene family (<i>GALNT</i>s). Two of these genes, <i>GALNT2</i> and <i>GALNT3</i>, are known as monogenic autosomal recessive inherited disease genes with well characterized phenotypes, whereas a broad spectrum of phenotypes is associated with the remaining 18 genes. Until recently, the overlapping functionality of the 20 members of the enzyme family has hindered characterizing the specific biological roles of individual enzymes. However, recent evidence suggests that these enzymes do not have full functional redundancy and may serve specific purposes that are found in the different phenotypes described. Here, we summarize the current knowledge of <i>GALNT</i> and associated phenotypes.https://www.mdpi.com/1420-3049/26/18/5504polypeptide <i>N</i>-acetylgalactosaminyltransferaseUDP-GalNAc: polypeptide <i>N</i>-acetylgalactosaminyltransferaseGalNAc-T<i>GALNT</i><i>O</i>-glycosylation |
| spellingShingle | Kentaro Kato Lars Hansen Henrik Clausen Polypeptide <i>N</i>-acetylgalactosaminyltransferase-Associated Phenotypes in Mammals Molecules polypeptide <i>N</i>-acetylgalactosaminyltransferase UDP-GalNAc: polypeptide <i>N</i>-acetylgalactosaminyltransferase GalNAc-T <i>GALNT</i> <i>O</i>-glycosylation |
| title | Polypeptide <i>N</i>-acetylgalactosaminyltransferase-Associated Phenotypes in Mammals |
| title_full | Polypeptide <i>N</i>-acetylgalactosaminyltransferase-Associated Phenotypes in Mammals |
| title_fullStr | Polypeptide <i>N</i>-acetylgalactosaminyltransferase-Associated Phenotypes in Mammals |
| title_full_unstemmed | Polypeptide <i>N</i>-acetylgalactosaminyltransferase-Associated Phenotypes in Mammals |
| title_short | Polypeptide <i>N</i>-acetylgalactosaminyltransferase-Associated Phenotypes in Mammals |
| title_sort | polypeptide i n i acetylgalactosaminyltransferase associated phenotypes in mammals |
| topic | polypeptide <i>N</i>-acetylgalactosaminyltransferase UDP-GalNAc: polypeptide <i>N</i>-acetylgalactosaminyltransferase GalNAc-T <i>GALNT</i> <i>O</i>-glycosylation |
| url | https://www.mdpi.com/1420-3049/26/18/5504 |
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