Fringe is a glycosyltransferase that modifies Notch
- D. J. Moloney, V. Panin, T. Vogt
- BiologyNature
- 27 July 2000
The post-translational modification of Notch by Fringe represents a striking example of modulation of a signalling event by differential receptor glycosylation and identifies a mechanism that is likely to be relevant to other signalling pathways.
Mammalian Notch1 Is Modified with Two Unusual Forms ofO-Linked Glycosylation Found on Epidermal Growth Factor-like Modules*
- D. J. Moloney, Louisa H. Shair, R. Haltiwanger
- Biology, ChemistryJournal of Biological Chemistry
- 31 March 2000
It is shown that Notch1 endogenously expressed in Chinese hamster ovary cells is modified with O-linked fucose andO-linked glucose saccharides, two unusual forms of O- linked glycosylation found on epidermal growth factor-like (EGF) modules.
Dual Roles of Cripto as a Ligand and Coreceptor in the Nodal Signaling Pathway
- Yu-Ting Yan, Jan-jan Liu, M. Shen
- BiologyMolecular and Cellular Biology
- 1 July 2002
A model in which Cripto has dual roles as a coreceptor as well as a coligand for Nodal and that this signaling interaction with NodAl is regulated by an unusual form of glycosylation is proposed.
Modulation of O-LinkedN-Acetylglucosamine Levels on Nuclear and Cytoplasmic Proteins in Vivo Using the PeptideO-GlcNAc-β-N-acetylglucosaminidase…
- R. Haltiwanger, K. Grove, G. Philipsberg
- BiologyJournal of Biological Chemistry
- 6 February 1998
Interestingly, it is demonstrated that an increase in O-GlcNAc levels on the transcription factor Sp1 resulted in a reciprocal decrease in its level of phosphorylation, supporting the hypothesis that O- GloverNAc competes with phosphate on some proteins.
Rumi Is a CAP10 Domain Glycosyltransferase that Modifies Notch and Is Required for Notch Signaling
- M. Acar, H. Jafar-Nejad, H. Bellen
- BiologyCell
- 25 January 2008
Role of glycosylation in development.
- R. Haltiwanger, J. Lowe
- Biology, ChemistryAnnual Review of Biochemistry
- 21 January 2003
A review of recent studies analyzing function of a variety of glycoconjugates, focusing on lessons learned from human disease and genetic studies in mice, Drosophila melanogaster, and Caenorhabditis elegans, suggests that O-fucose, O-mannose, N-glycans, mucin-type O-gly cans and proteoglycans are likely to play important roles in developmental processes.
Notch-Jagged complex structure implicates a catch bond in tuning ligand sensitivity
The studies help explain how low-affinity interactions of Notch with its ligands can lead to signaling and indicate that forces may differentially affect Notch-ligand interactions.
Nuclear pore complex glycoproteins contain cytoplasmically disposed O- linked N-acetylglucosamine
- G. Holt, C. Snow, A. Senior, R. Haltiwanger, L. Gerace, G. Hart
- Biology, ChemistryJournal of Cell Biology
- 1 May 1987
It is demonstrated that all members of this group of pore complex proteins bear multiple O-linked GlcNAc moieties, and it is shown that the O-links are linked via serine (and possibly threonine) side chains to these proteins.
Glycosylation of nuclear and cytoplasmic proteins. Purification and characterization of a uridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetylglucosaminyltransferase.
- R. Haltiwanger, M. Blomberg, G. Hart
- Biology, ChemistryJournal of Biological Chemistry
- 5 May 1992
Modification of epidermal growth factor-like repeats with O-fucose. Molecular cloning and expression of a novel GDP-fucose protein O-fucosyltransferase.
- Y. Wang, L. Shao, R. Haltiwanger
- BiologyJournal of Biological Chemistry
- 26 October 2001
The isolation of a cDNA that encodes human O-FucT-1 is reported, which contains an open reading frame encoding a protein of 388 amino acids with a predicted N-terminal transmembrane sequence typical of a type II membrane orientation.
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