The DOI matches its Crossref record; 104 of the 104 references it cites were found in a registry or an index.
All in the family: the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases
Abstract
Mucin-type linkages (GalNAcalpha1-O-Ser/Thr) are initiated by a family of glycosyltransferases known as the UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferases (ppGaNTases, EC 2.4.1.41). These enzymes transfer GalNAc from the sugar donor UDP-GalNAc to serine and threonine residues, forming an alpha anomeric linkage. Despite the seeming simplicity of ppGaNTase catalytic function, it is estimated on the basis of in silico analysis that there are 24 unique ppGaNTase human genes. ppGaNTase isoforms display tissue-specific expression in adult mammals as well as unique spatial and temporal patterns of expression during murine development. In vitro assays suggest that a subset of the ppGaNTases have overlapping substrate specificities, but at least two ppGaNTases (ppGaNTase-T7 and -T9 [now designated -T10]) appear to require the prior addition of GalNAc to a synthetic peptide before they can catalyze sugar transfer to this substrate. Site-specific O-glycosylation by several ppGaNTases is influenced by the position and structure of previously added O-glycans. Collectively, these observations argue in favor of a hierarchical addition of core GalNAc residues to the apomucin. Various forms of O-glycan pathobiology may be reexamined in light of the existence of an extensive ppGaNTase family of enzymes. Recent work has demonstrated that at least one ppGaNTase isoform is required for normal development in Drosophila melanogaster. Structural insights will no doubt lead to the development of isoform-specific inhibitors. Such tools will prove valuable to furthering our understanding of the functional roles played by O-glycans.
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Cites
On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database
Apweiler, R. (1999) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/s0304-4165(99)00165-8 · Cited by 1,855
Roseman, S. (1970) · Chemistry and Physics of Lipids · doi:10.1016/0009-3084(70)90024-1 · Cited by 1,207
CAMPBELL, J. A., DAVIES, G. J., BULONE, V., & HENRISSAT, B. (1997) · Biochemical Journal · doi:10.1042/bj3260929u · Cited by 815
Somers, W. S., Tang, J., Shaw, G. D., & Camphausen, R. T. (2000) · Cell · doi:10.1016/s0092-8674(00)00138-0 · Cited by 736
HOOPER, N. M., KARRAN, E. H., & TURNER, A. J. (1997) · Biochemical Journal · doi:10.1042/bj3210265 · Cited by 617
Hansen, J. E., Lund, O., Tolstrup, N., Gooley, A. A., Williams, K. L., & Brunak, S. (1998) · Glycoconjugate Journal · doi:10.1023/a:1006960004440 · Cited by 510
Tomana, M., Novak, J., Julian, B. A., Matousovic, K., Konecny, K., & Mestecky, J. (1999) · Journal of Clinical Investigation · doi:10.1172/jci5535 · Cited by 498
Hakomori, S.-I. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.012540899 · Cited by 492
Glycoside hydrolases and glycosyltransferases: families and functional modules
Bourne, Y., & Henrissat, B. (2001) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(00)00253-0 · Cited by 445
Dürr, G., Strayle, J., Plemper, R., Elbs, S., Klee, S. K., Catty, P., Wolf, D. H., & Rudolph, H. K. (1998) · Molecular Biology of the Cell · doi:10.1091/mbc.9.5.1149 · Cited by 388
Cited by
Precision mapping of the human O‐GalNAc glycoproteome through SimpleCell technology
Steentoft, C., Vakhrushev, S. Y., Joshi, H. J., Kong, Y., Vester‐Christensen, M. B., Schjoldager, K. T. G., Lavrsen, K., Dabelsteen, S., Pedersen, N. B., Marcos‐Silva, L., et al. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.79 · Cited by 1,408
Bennett, E. P., Mandel, U., Clausen, H., Gerken, T. A., Fritz, T. A., & Tabak, L. A. (2012) · Glycobiology · doi:10.1093/glycob/cwr182 · Cited by 876
Julenius, K., Mølgaard, A., Gupta, R., & Brunak, S. (2005) · Glycobiology · doi:10.1093/glycob/cwh151 · Cited by 872
Role of Glycosylation in Development
Haltiwanger, R. S., & Lowe, J. B. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.074043 · Cited by 757
A metabolic labeling approach toward proteomic analysis of mucin-type O-linked glycosylation
Hang, H. C., Yu, C., Kato, D. L., & Bertozzi, C. R. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2335201100 · Cited by 580
Metadata
- Authors
- Ten Hagen, K. G.
- Venue
- Glycobiology
- Publisher
- Oxford University Press (OUP)
- Published
- 2002-11-01
- Volume
- 13
- Issue
- 1
- Pages
- 1R-16
- ISSN
- 0959-6658 (ISSN-L)
- 1460-2423
- OpenAlex
- W2138605813
- Cited by
- 498
- References
- 104
- FWCI
- 5.40
- Type
- journal article
- Language
- en
- Open access
- closed
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- Ten Hagen, K. G. (2003). All in the family: the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases. Glycobiology. https://doi.org/10.1093/glycob/cwg007
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