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Characterization of a UDP-GalNAc:Polypeptide N-Acetylgalactosaminyltransferase That Displays Glycopeptide N-Acetylgalactosaminyltransferase Activity*
TLDR
The cloning, expression, and characterization of a novel member of the mammalian UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase (ppGaNTase) family that transfers Gal NAc to a GalNAc-containing glycopeptide is reported, suggesting thatO-glycosylation of multisite substrates may proceed in a specific hierarchical manner and underscores the potential complexity of the processes that regulate O-glyCosylation.
Cloning and Characterization of a Ninth Member of the UDP-GalNAc:Polypeptide N-Acetylgalactosaminyltransferase Family, ppGaNTase-T9*
TLDR
Northern blot analysis revealed that the gene encoding this enzyme is expressed in a broadly distributed manner across many adult tissues, lending further support to the existence of a hierarchical network of differential enzymatic activity within the diversely regulated ppGaNTase family, which may play a role in the various processes governing development.
Cloning and Expression of a Novel, Tissue Specifically Expressed Member of the UDP-GalNAc:Polypeptide N-Acetylgalactosaminyltransferase Family*
TLDR
The cloning and expression of the fifth member of the mammalian UDP-GalNAc:polypeptideN-acetylgalactosaminyltransferase (ppGaNTase) family is reported, highlighting the diversity and complexity of the family of genes controllingO-linked glycosylation.
A UDP-GalNAc:PolypeptideN-Acetylgalactosaminyltransferase Is Essential for Viability in Drosophila melanogaster *
TLDR
This study provides the first direct evidence for the involvement of a member of this conserved multigene family in eukaryotic development and viability in Drosophila melanogaster.
A Mucin-type O-Glycosyltransferase Modulates Cell Adhesion during Drosophila Development*S⃞
TLDR
This study provides the first evidence for the role of O-glycosylation in a developmentally regulated, integrin-mediated, cell adhesion event and reveals a novel player in wing blade formation during Drosophila development.
A UDP-GalNAc:Polypeptide N-Acetylgalactosaminyltransferase Is Required for Epithelial Tube Formation*
TLDR
A previously unrecognized requirement for mucin-type O-glycosylation in epithelial tube integrity is demonstrated and have obvious implications for epithelial morphogenesis in higher eukaryotes, since a unique ortholog to pgant35A exists in mammals.
cDNA Cloning and Expression of a Novel UDP-N-acetyl-d-galactosamine:PolypeptideN-Acetylgalactosaminyltransferase*
The cDNA for a fourth member of the mammalian UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase family, termed ppGaNTase-T4, has been cloned from a murine spleen cDNA library and expressed
Diverse spatial expression patterns of UDP-GalNAc:polypeptide N-acetylgalactosaminyl-transferase family member mRNAs during mouse development.
TLDR
The unique spatiotemporal expression of the different ppGaNTase family members during development suggests unique roles for each of these gene products.
Dissecting the Biological Role of Mucin-type O-Glycosylation Using RNA Interference in Drosophila Cell Culture*
TLDR
These studies demonstrate the efficient and specific knockdown of pgant gene expression in two Drosophila cell culture systems, resulting in specific morphological and functional effects.
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