Research Topics
Genomes and Genes | Robert S HaltiwangerSummaryAffiliation: Stony Brook University Country: USA Publications
| Collaborators
|
Detail Information
Publications
Notch ligands are substrates for protein O-fucosyltransferase-1 and FringeVladislav M Panin
Howard Hughes Medical Institute, Waksman Institute and Department of Molecular Biology and Biochemistry, Rutgers, The State University, Piscataway, New Jersey 08854, USA
J Biol Chem 277:29945-52. 2002..A revised, broad consensus site, C(2)X(3-5)S/TC(3) (where X(3-5) are any 3-5 amino acid residues), is proposed...- Regulation of signal transduction pathways in development by glycosylationRobert S Haltiwanger
Department of Biochemistry and Cell Biology, Institute for Cell and Developmental Biology, State University of New York at Stony Brook, Stony Brook, NY 11794-5215, USA
Curr Opin Struct Biol 12:593-8. 2002..These and other examples provide a new paradigm for the regulation of signal transduction events by glycosylation... - Role of glycosylation in developmentRobert S Haltiwanger
Department of Biochemistry and Cell Biology, Institute for Cell and Developmental Biology, State University of New York, Stony Brook, New York 11794 5215, USA
Annu Rev Biochem 73:491-537. 2004..melanogaster, and C. elegans... - Modulation of receptor signaling by glycosylation: fringe is an O-fucose-beta1,3-N-acetylglucosaminyltransferaseRobert S Haltiwanger
Department of Biochemistry and Cell Biology, Institute for Cell and Developmental Biology, State University of New York Stony Brook, 11794 5215, USA
Biochim Biophys Acta 1573:328-35. 2002..Thus, both fringe and beta4GalT-1 are modulators of Notch function. Several models have been proposed to explain how alterations in O-fucose glycans result in changes in Notch signaling, and these models are discussed... - Two distinct pathways for O-fucosylation of epidermal growth factor-like or thrombospondin type 1 repeatsYi Luo
Department of Biochemistry and Cell Biology, Institute for Cell and Developmental Biology, Stony Brook University, Stony Brook, New York 11794 5215
J Biol Chem 281:9385-92. 2006..Taken together, these results suggest that two distinct O-fucosylation pathways exist in cells, one specific for EGF repeat and the other for TSRs... 
Fringe benefits: functional and structural impacts of O-glycosylation on the extracellular domain of Notch receptorsNadia A Rana
Department of Biochemistry and Cell Biology, Institute for Cell and Developmental Biology, Stony Brook University, Stony Brook, NY 11794 5215, USA
Curr Opin Struct Biol 21:583-9. 2011..Here we review recent advances in identification and characterization of the enzymes responsible for glycosylating Notch and molecular mechanisms for how these O-glycans affect Notch activity...- Notch signaling in normal and disease States: possible therapies related to glycosylationRaajit Rampal
Department of Biochemistry and Cell Biology, Institute for Cell and Developmental Biology, Stony Brook University, Stony Brook, New York, 11794 5215, USA
Curr Mol Med 7:427-45. 2007..As well, potential roles for glycosylation in Notch-related human diseases, and possible roles for therapeutic targeting of POFUT1 and Fringe in Notch-related human diseases, are discussed... - Rumi functions as both a protein O-glucosyltransferase and a protein O-xylosyltransferaseHideyuki Takeuchi
Department of Biochemistry and Cell Biology, Institute of Cell and Developmental Biology, Stony Brook University, Stony Brook, NY 11794, USA
Proc Natl Acad Sci U S A 108:16600-5. 2011.... - O-glucose trisaccharide is present at high but variable stoichiometry at multiple sites on mouse Notch1Nadia A Rana
Department of Biochemistry and Cell Biology, Institute of Cell and Developmental Biology, Stony Brook University, Stony Brook, New York 11794 5215, USA
J Biol Chem 286:31623-37. 2011..These results demonstrate that, like O-fucose, the O-glucose modifications of EGF repeats occur extensively on mN1, and they play important roles in Notch function... - Methods for analysis of unusual forms of O-glycosylationAleksandra Nita-Lazar
Department of Biochemistry and Cell Biology, State University of New York at Stony Brook, NY, USA
Methods Mol Biol 347:57-68. 2006..With these methods, we can determine both stoichiometry and the structure of the glycans on the expressed proteins. We have begun to utilize mass spectrometry in addition to metabolic radiolabeling methods to analyze these structures... - Site-specific O-glucosylation of the epidermal growth factor-like (EGF) repeats of notch: efficiency of glycosylation is affected by proper folding and amino acid sequence of individual EGF repeatsHideyuki Takeuchi
Department of Biochemistry and Cell Biology, Institute of Cell and Developmental Biology, Stony Brook University, Stony Brook, New York 11794, USA
J Biol Chem 287:33934-44. 2012..These results indicate that protein folding and amino acid sequences of individual EGF repeats fundamentally affect both attachment and elongation of O-glucose glycans... - Lunatic fringe, manic fringe, and radical fringe recognize similar specificity determinants in O-fucosylated epidermal growth factor-like repeatsRaajit Rampal
Department of Biochemistry and Cell Biology, Institute for Cell and Developmental Biology, Stony Brook University, Stony Brook, New York 11794 5215, USA
J Biol Chem 280:42454-63. 2005..These amino acids provide an initial step toward defining sequences that will allow us to predict which O-fucosylated EGF repeats are modified by the Fringes... - Highly conserved O-fucose sites have distinct effects on Notch1 functionRaajit Rampal
Department of Biochemistry and Cell Biology, Institute for Cell and Developmental Biology, Stony Brook University, New York 11794 5215, USA
J Biol Chem 280:32133-40. 2005..These results indicate that the most highly conserved O-fucose sites in Notch1 are important for both processing and ligand-mediated signaling in the context of a cell-based signaling assay... - O-fucosylation of thrombospondin type 1 repeats restricts epithelial to mesenchymal transition (EMT) and maintains epiblast pluripotency during mouse gastrulationJianguang Du
Department of Biochemistry and Cell Biology, Institute for Cell and Developmental Biology, Center for Developmental Genetics, Stony Brook University, Stony Brook, NY 11794 5215, USA
Dev Biol 346:25-38. 2010.... - Protein O-fucosyltransferase 2 adds O-fucose to thrombospondin type 1 repeatsYi Luo
Department of Biochemistry and Cell Biology, Institute for Cell and Developmental Biology, Stony Brook University, Stony Brook, New York 11794 5215, USA
J Biol Chem 281:9393-9. 2006..These results demonstrate that O-fucosyltransferase 2 is in fact a TSR-specific O-fucosyltransferase... - Role of unusual O-glycans in intercellular signalingKelvin B Luther
Department of Biochemistry and Cell Biology, Institute for Cell and Developmental Biology, Stony Brook University, Stony Brook, NY 11794 5215, USA
Int J Biochem Cell Biol 41:1011-24. 2009..We will review each of these areas focusing on the glycan structures produced, the consequence of their presence, and the enzymes responsible... - Methods for analysis of O-linked modifications on epidermal growth factor-like and thrombospondin type 1 repeatsAleksandra Nita-Lazar
Department of Biochemistry and Cell Biology, SUNY at Stony Brook, Stony Brook, New York, USA
Methods Enzymol 417:93-111. 2006..These methods use both traditional biochemical methods of carbohydrate composition analysis and electrospray ionization-mass spectrometry of glycopeptides... 
O-fucosylation of thrombospondin type 1 repeatsChristina Leonhard-Melief
Department of Biochemistry and Cell Biology, Institute for Cell and Developmental Biology, Stony Brook University, Stony Brook, New York, USA
Methods Enzymol 480:401-16. 2010..These methods include techniques to identify glycosylated peptides and the relative amounts of elongated products by electrospray ionization mass spectrometry of glycopeptides...- Role of glycosylation of Notch in developmentHideyuki Takeuchi
Department of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, NY 11794 5215, USA
Semin Cell Dev Biol 21:638-45. 2010..In this review we summarize the significance of the Notch pathway in development and the players responsible for its glycosylation, and then discuss the molecular mechanisms by which protein glycosylation may regulate Notch function... - Structural and mechanistic insights into lunatic fringe from a kinetic analysis of enzyme mutantsKelvin B Luther
Department of Biochemistry and Cell Biology, Institute for Cell and Developmental Biology, Stony Brook University, Stony Brook, NY 11794 5215, USA
J Biol Chem 284:3294-305. 2009..Finally, we identify several residues near the UDP-GlcNAc-binding site, which are specifically permissive toward UDP-GlcNAc utilization... - O-fucosylation of notch occurs in the endoplasmic reticulumYi Luo
Department of Biochemistry and Cell Biology, Institute for Cell and Developmental Biology, State University of New York at Stony Brook, Stony Brook, New York 11794 5215, USA
J Biol Chem 280:11289-94. 2005..The fact that O-FucT-1 recognizes properly folded epidermal growth factor-like repeats, together with this unique localization, suggests that it may play a role in quality control... - Studies on the N-glycosylation of the subunits of oligosaccharyl transferase in Saccharomyces cerevisiaeGuangtao Li
Department of Biochemistry and Cell Biology and Institute for Cell and Developmental Biology, State University of New York, Stony Brook, New York 11794-5215, USA
J Biol Chem 280:1864-71. 2005..Based on these studies, we conclude that N-glycosylation of Stt3p at Asn(539) is essential for its function in the OT complex... - 6-Alkynyl fucose is a bioorthogonal analog for O-fucosylation of epidermal growth factor-like repeats and thrombospondin Type-1 repeats by protein O-fucosyltransferases 1 and 2Esam Al-Shareffi
Department of Biochemistry and Cell Biology, Stony Brook University, NY 11794 5215, USA
Glycobiology 23:188-98. 2013..These results show that 6AF is efficiently utilized in a truly bioorthogonal manner by Pofut1, Pofut2 and the enzymes that elongate O-fucose, providing evidence that 6AF is a significant new tool in the study of protein O-fucosylation... - Four-jointed is a Golgi kinase that phosphorylates a subset of cadherin domainsHiroyuki O Ishikawa
Howard Hughes Medical Institute, Waksman Institute and Department of Molecular Biology and Biochemistry, Rutgers University, Piscataway, NJ 08854, USA
Science 321:401-4. 2008..Our results indicate that Four-jointed regulates Fat signaling by phosphorylating cadherin domains of Fat and Dachsous as they transit through the Golgi... - In vitro reconstitution of the modulation of Drosophila Notch-ligand binding by FringeAiguo Xu
Howard Hughes Medical Institute, Waksman Institute and Department of Molecular Biology and Biochemistry, Rutgers University, Piscataway, New Jersey 08854, USA
J Biol Chem 282:35153-62. 2007.... - Differential terminal fucosylation of N-linked glycans versus protein O-fucosylation in leukocyte adhesion deficiency type II (CDG IIc)Laura Sturla
Giannina Gaslini Institute, 16147 Genova, Italy
J Biol Chem 278:26727-33. 2003.... - CADASIL mutations impair Notch3 glycosylation by FringeJoseph F Arboleda-Velasquez
Neurology Department, Brigham and Women s Hospital and Harvard Medical School, Boston, MA 02115, USA
Hum Mol Genet 14:1631-9. 2005..CADASIL changes also induced aberrant homodimerization of mutant Notch3 fragments and heterodimerization of mutant Notch3 with Lunatic Fringe itself. Together, these data suggest that Fringe plays a role in CADASIL pathophysiology... - Rumi is a CAP10 domain glycosyltransferase that modifies Notch and is required for Notch signalingMelih Acar
Program in Developmental Biology, Baylor College of Medicine, Houston, TX 77030, USA
Cell 132:247-58. 2008..These data indicate that by O-glucosylating Notch in the ER, Rumi regulates its folding and/or trafficking and allows signaling at the cell membrane... - Dual roles of Cripto as a ligand and coreceptor in the nodal signaling pathwayYu Ting Yan
Center for Advanced Biotechnology and Medicine and Department of Pediatric, University of Medicine and Dentistry of New Jersey Robert Wood Johnson Medical School, Piscataway, New Jersey 08854, USA
Mol Cell Biol 22:4439-49. 2002..Our findings highlight the significance of extracellular modulation of ligand activity as an important means of regulating TGF beta signaling pathways during vertebrate development... - Identification and characterization of abeta1,3-glucosyltransferase that synthesizes the Glc-beta1,3-Fuc disaccharide on thrombospondin type 1 repeatsKrisztina Kozma
Friedrich Miescher Institute, Maulbeerstrasse 66, CH 4058 Basel, Switzerland
J Biol Chem 281:36742-51. 2006..The identification of the beta1,3-glucosyltransferase gene allows us to manipulate the formation of the rare Glcbeta1,3Fucalpha1 structure to investigate its biological function... - O-fucosylation is required for ADAMTS13 secretionLindsay M Ricketts
Department of Internal Medicine, Division of Hematology, Washington University School of Medicine, St Louis, Missouri, 63110, USA
J Biol Chem 282:17014-23. 2007..Together these findings indicate that O-fucosylation is functionally significant for secretion of ADAMTS13... - The threonine that carries fucose, but not fucose, is required for Cripto to facilitate Nodal signalingShaolin Shi
Department of Cell Biology, Albert Einstein College of Medicine, 1300 Morris Park Avenue, New York, NY 10461, USA
J Biol Chem 282:20133-41. 2007..By contrast, we show that O-fucose, and not the Thr to which it is attached, is required in the ligand-binding domain of Notch1 for Notch1 signaling... - O-fucosylation of thrombospondin type 1 repeats in ADAMTS-like-1/punctin-1 regulates secretion: implications for the ADAMTS superfamilyLauren W Wang
Department of Biomedical Engineering, Lerner Research Institute, Cleveland Clinic Foundation, Cleveland, Ohio 44195, USA
J Biol Chem 282:17024-31. 2007..From a broad perspective, these data suggest that O-fucosylation may be a widespread post-translational modification in members of the ADAMTS superfamily with possible regulatory consequences...