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Review
. 2021 Sep 10;26(18):5504.
doi: 10.3390/molecules26185504.

Polypeptide N-acetylgalactosaminyltransferase-Associated Phenotypes in Mammals

Kentaro Kato  1   2 , Lars Hansen  3 , Henrik Clausen  3
Affiliations
Review

Polypeptide N-acetylgalactosaminyltransferase-Associated Phenotypes in Mammals

Kentaro Kato et al. Molecules. .

Abstract

Mucin-type O-glycosylation involves the attachment of glycans to an initial O-linked N-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 N-acetylgalactosaminyltransferases (GalNAc-Ts) (EC 2.4.1.41). The enzymes are encoded by a large gene family (GALNTs). Two of these genes, GALNT2 and GALNT3, 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 GALNT and associated phenotypes.

Keywords: GALNT; GalNAc-T; O-glycosylation; UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferase; polypeptide N-acetylgalactosaminyltransferase.

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
GALNT3 and GalNAc-T3 mutations reported in HFTC patients. (A) Structure for the GALNT3 transcript (NM_004482.4) with positions of exons in the transcript. Note that exon1 is non-coding. Splice site variants are shown with the position in the corresponding introns. (B) The protein domain structure of GalNAc-T3 with the exon positions and LOF and missense mutations is shown. ex; exon.
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