R. Haltiwanger

Publications187
h-index59
Citations10,828
Highly Influential Citations393
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Fringe is a glycosyltransferase that modifies Notch
TLDR
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.
Dual Roles of Cripto as a Ligand and Coreceptor in the Nodal Signaling Pathway
TLDR
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.
Mammalian Notch1 Is Modified with Two Unusual Forms ofO-Linked Glycosylation Found on Epidermal Growth Factor-like Modules*
TLDR
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.
Modulation of O-LinkedN-Acetylglucosamine Levels on Nuclear and Cytoplasmic Proteins in Vivo Using the PeptideO-GlcNAc-β-N-acetylglucosaminidase…
TLDR
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
TLDR
The authors' studies show that Rumi is an endoplasmic reticulum-retained protein with a highly conserved CAP10 domain, capable of adding glucose to serine residues in Notch EGF repeats with the consensus C1-X-S- X-P-C2 sequence, and indicates that by O-glucosylating Notch in the ER, Rumi regulates its folding and/or trafficking and allows signaling at the cell membrane.
Role of glycosylation in development.
TLDR
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.
Four-jointed Is a Golgi Kinase That Phosphorylates a Subset of Cadherin Domains
TLDR
The results indicate that Four-jointed regulates Fat signaling by phosphorylating cadherin domains of Fat and Dachsous as they transit through the Golgi.
Glycosylation of nuclear and cytoplasmic proteins. Purification and characterization of a uridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetylglucosaminyltransferase.
TLDR
The multimeric state and large size of the O-GlcNAc transferase imply that its activity may be highly regulated within the cell.
Modification of epidermal growth factor-like repeats with O-fucose. Molecular cloning and expression of a novel GDP-fucose protein O-fucosyltransferase.
TLDR
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.
Notch Ligands Are Substrates for ProteinO-Fucosyltransferase-1 and Fringe*
TLDR
It is established that both mammalian and Drosophila Notch ligands are modified with O-fucose glycans, demonstrating that the consensus site was useful for making predictions.
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