Expression of the UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferase family is spatially and temporally regulated during Drosophila development
- PMID: 16251381
- DOI: 10.1093/glycob/cwj051
Expression of the UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferase family is spatially and temporally regulated during Drosophila development
Abstract
The UDP-GalNAc : polypeptide N-acetylgalactosaminyltransferase (ppGaNTase or ppGalNAcT or pgant) enzyme family is responsible for the first committed step in the synthesis of mucin-type O-glycans on protein substrates. Previous work from our group has demonstrated both sequence and functional conservation between members of this family in mammals and the fruit fly, Drosophila melanogaster. One member of this family in Drosophila has been shown to be essential for viability and development. In an effort to understand the developmental stages and processes in which O-glycosylation is involved, we have determined the expression pattern of each functional family member as well as putative isoforms during Drosophila development. Our studies indicate that isoforms are expressed in discrete spatial and temporal fashions during development, with some isoforms being found uniquely in restricted areas of the developing embryo (brain, trachea, pharynx, esophagus, proventriculus, and amnioserosa), whereas others are found in multiple regions and overlap with the expression of other isoforms (salivary glands, posterior midgut, anterior midgut, and the fore-/hindgut) during embryogenesis. Additionally, we examined expression patterns in imaginal discs from third instar larvae, which will become the adult structures. Most isoforms are also expressed in the imaginal discs, with some showing unique transcript localization and spatial regulatory control. Thus, this report provides insight into the specific regions during Drosophila development that may require O-linked glycosylation in vivo as well as which isoforms may act cooperatively in certain tissues and which may be uniquely responsible for glycosylation in others.
Similar articles
-
All in the family: the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases.Glycobiology. 2003 Jan;13(1):1R-16R. doi: 10.1093/glycob/cwg007. Epub 2002 Nov 1. Glycobiology. 2003. PMID: 12634319 Review.
-
Expression of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase isoforms in murine tissues determined by real-time PCR: a new view of a large family.Glycobiology. 2003 Jul;13(7):549-57. doi: 10.1093/glycob/cwg062. Epub 2003 Mar 19. Glycobiology. 2003. PMID: 12651884
-
Expression in human ocular surface tissues of the GalNAc-transferases that initiate mucin-type O-glycosylation.Cornea. 2006 Dec;25(10):1193-9. doi: 10.1097/01.ico.0000240099.16420.17. Cornea. 2006. PMID: 17172897
-
Functional characterization and expression analysis of members of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase family from Drosophila melanogaster.J Biol Chem. 2003 Sep 12;278(37):35039-48. doi: 10.1074/jbc.M303836200. Epub 2003 Jun 26. J Biol Chem. 2003. PMID: 12829714
-
[Determination and differentiation in the light of molecular genetics].Ontogenez. 2005 Sep-Oct;36(5):333-42. Ontogenez. 2005. PMID: 16245564 Review. Russian.
Cited by
-
N-linked glycosylation restricts the function of Short gastrulation to bind and shuttle BMPs.Development. 2018 Nov 19;145(22):dev167338. doi: 10.1242/dev.167338. Development. 2018. PMID: 30355725 Free PMC article.
-
Two protein N-acetylgalactosaminyl transferases regulate synaptic plasticity by activity-dependent regulation of integrin signaling.J Neurosci. 2014 Sep 24;34(39):13047-65. doi: 10.1523/JNEUROSCI.1484-14.2014. J Neurosci. 2014. PMID: 25253852 Free PMC article.
-
The N's and O's of Drosophila glycoprotein glycobiology.Glycoconj J. 2013 Jan;30(1):57-66. doi: 10.1007/s10719-012-9442-x. Epub 2012 Aug 31. Glycoconj J. 2013. PMID: 22936173 Free PMC article. Review.
-
Dissecting the biological role of mucin-type O-glycosylation using RNA interference in Drosophila cell culture.J Biol Chem. 2010 Nov 5;285(45):34477-84. doi: 10.1074/jbc.M110.133561. Epub 2010 Aug 31. J Biol Chem. 2010. PMID: 20807760 Free PMC article.
-
Synthesis and biological roles of O-glycans in insects.Glycoconj J. 2020 Feb;37(1):47-56. doi: 10.1007/s10719-019-09867-1. Epub 2019 Apr 1. Glycoconj J. 2020. PMID: 30937676 Review.
MeSH terms
Substances
Associated data
- Actions
- Actions
LinkOut - more resources
Full Text Sources
Molecular Biology Databases