Robert S Haltiwanger

Summary

Affiliation: Stony Brook University
Country: USA

Publications

  1. ncbi request reprint Notch ligands are substrates for protein O-fucosyltransferase-1 and Fringe
    Vladislav 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
  2. ncbi request reprint Regulation of signal transduction pathways in development by glycosylation
    Robert 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
  3. ncbi request reprint Modulation of receptor signaling by glycosylation: fringe is an O-fucose-beta1,3-N-acetylglucosaminyltransferase
    Robert 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
  4. ncbi request reprint Role of glycosylation in development
    Robert 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
  5. ncbi request reprint Two distinct pathways for O-fucosylation of epidermal growth factor-like or thrombospondin type 1 repeats
    Yi 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
  6. pmc Fringe benefits: functional and structural impacts of O-glycosylation on the extracellular domain of Notch receptors
    Nadia 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
  7. ncbi request reprint Notch signaling in normal and disease States: possible therapies related to glycosylation
    Raajit 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
  8. pmc Rumi functions as both a protein O-glucosyltransferase and a protein O-xylosyltransferase
    Hideyuki 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
  9. pmc O-glucose trisaccharide is present at high but variable stoichiometry at multiple sites on mouse Notch1
    Nadia 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
  10. doi request reprint Enzymatic analysis of the protein O-glycosyltransferase, Rumi, acting toward epidermal growth factor-like (EGF) repeats
    Hideyuki Takeuchi
    Department of Biochemistry and Cell Biology, Institute of Cell and Developmental Biology, Stony Brook University, Stony Brook, NY, USA
    Methods Mol Biol 1022:119-28. 2013

Collaborators

  • Kenneth Irvine
  • Chi Huey Wong
  • Kenneth S Kosik
  • William J Lennarz
  • Hamed Jafar-Nejad
  • Qi Yan
  • PAMELA M STANLEY
  • Yi Luo
  • J B Lowe
  • Nicola Haines
  • Kate Koles
  • Hideyuki Takeuchi
  • Kelvin B Luther
  • Nadia A Rana
  • Aleksandra Nita-Lazar
  • Raajit Rampal
  • Christina Leonhard-Melief
  • Malgosia Dlugosz
  • Esam Al-Shareffi
  • Joseph F Arboleda-Velasquez
  • Jianguang Du
  • Hiroyuki O Ishikawa
  • Melih Acar
  • Shaolin Shi
  • Lindsay M Ricketts
  • Lauren W Wang
  • Aiguo Xu
  • Krisztina Kozma
  • Guangtao Li
  • Daniel J Moloney
  • Laura Sturla
  • Vladislav M Panin
  • Yu Ting Yan
  • Jean Luc Chaubard
  • Sheng Kai Wang
  • Joshua Kantharia
  • Maya K Sethi
  • Hans Bakker
  • Devin S Caswell
  • Rodrigo C Fernández-Valdivia
  • Thomas P Garner
  • Thomas K Weldeghiorghis
  • Shinako Kakuda
  • Megan A Macnaughtan
  • Bernadette C Holdener
  • Kenneth R Shroyer
  • Hermann Schindelin
  • Akhila Rajan
  • Dafina Ibrani
  • Hongling Pan
  • Hugo J Bellen
  • Elaine M Majerus
  • Xinghua Hou
  • Changhui Ge
  • Suneel S Apte
  • Robert P T Somerville
  • Mona Raed
  • Dominique Klein
  • Björn Hegemann
  • Jan Hofsteenge
  • Jeremy J Keusch
  • Daniel Hess
  • Min Liu
  • Manuel F Navarro-Gonzalez
  • Maria C Martinez
  • Annie S Y Li
  • Christine P Donahue
  • Peter Libby
  • Alexandra Nita-Lazar
  • Stephanie A Georgiou
  • PATRICIA A D'AMORE
  • Diane C Darland
  • Masanori Aikawa
  • Erik Fung
  • Amos Etzioni
  • Michela Tonetti
  • Floriana Fruscione
  • Chaosu E
  • Li Shao
  • Cory Abate-Shen
  • Michael M Shen
  • Jan Jan Liu
  • Liang Lei

Detail Information

Publications34

  1. ncbi request reprint Notch ligands are substrates for protein O-fucosyltransferase-1 and Fringe
    Vladislav 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...
  2. ncbi request reprint Regulation of signal transduction pathways in development by glycosylation
    Robert 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...
  3. ncbi request reprint Modulation of receptor signaling by glycosylation: fringe is an O-fucose-beta1,3-N-acetylglucosaminyltransferase
    Robert 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...
  4. ncbi request reprint Role of glycosylation in development
    Robert 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...
  5. ncbi request reprint Two distinct pathways for O-fucosylation of epidermal growth factor-like or thrombospondin type 1 repeats
    Yi 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...
  6. pmc Fringe benefits: functional and structural impacts of O-glycosylation on the extracellular domain of Notch receptors
    Nadia 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...
  7. ncbi request reprint Notch signaling in normal and disease States: possible therapies related to glycosylation
    Raajit 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...
  8. pmc Rumi functions as both a protein O-glucosyltransferase and a protein O-xylosyltransferase
    Hideyuki 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
    ....
  9. pmc O-glucose trisaccharide is present at high but variable stoichiometry at multiple sites on mouse Notch1
    Nadia 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...
  10. doi request reprint Enzymatic analysis of the protein O-glycosyltransferase, Rumi, acting toward epidermal growth factor-like (EGF) repeats
    Hideyuki Takeuchi
    Department of Biochemistry and Cell Biology, Institute of Cell and Developmental Biology, Stony Brook University, Stony Brook, NY, USA
    Methods Mol Biol 1022:119-28. 2013
    ..Here, we describe how we characterize the enzymatic activity of these enzymes, including preparation of the acceptor substrates, using bacterially expressed EGF repeats...
  11. pmc 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 2
    Esam Al-Shareffi
    Department of Biochemistry and Cell Biology, Stony Brook University, New York, 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...
  12. ncbi request reprint Methods for analysis of unusual forms of O-glycosylation
    Aleksandra 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...
  13. pmc 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 repeats
    Hideyuki 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...
  14. pmc O-fucosylation of thrombospondin type 1 repeats restricts epithelial to mesenchymal transition (EMT) and maintains epiblast pluripotency during mouse gastrulation
    Jianguang 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
    ....
  15. ncbi request reprint Protein O-fucosyltransferase 2 adds O-fucose to thrombospondin type 1 repeats
    Yi 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...
  16. ncbi request reprint Lunatic fringe, manic fringe, and radical fringe recognize similar specificity determinants in O-fucosylated epidermal growth factor-like repeats
    Raajit 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...
  17. pmc Highly conserved O-fucose sites have distinct effects on Notch1 function
    Raajit 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...
  18. pmc Role of unusual O-glycans in intercellular signaling
    Kelvin 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...
  19. ncbi request reprint Methods for analysis of O-linked modifications on epidermal growth factor-like and thrombospondin type 1 repeats
    Aleksandra 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...
  20. pmc Role of glycosylation of Notch in development
    Hideyuki 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...
  21. pmc Structural and mechanistic insights into lunatic fringe from a kinetic analysis of enzyme mutants
    Kelvin 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...
  22. doi request reprint O-fucosylation of thrombospondin type 1 repeats
    Christina 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...
  23. ncbi request reprint O-fucosylation of notch occurs in the endoplasmic reticulum
    Yi 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...
  24. ncbi request reprint Studies on the N-glycosylation of the subunits of oligosaccharyl transferase in Saccharomyces cerevisiae
    Guangtao 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...
  25. pmc Four-jointed is a Golgi kinase that phosphorylates a subset of cadherin domains
    Hiroyuki 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...
  26. ncbi request reprint In vitro reconstitution of the modulation of Drosophila Notch-ligand binding by Fringe
    Aiguo 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
    ....
  27. ncbi request reprint 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
    ....
  28. ncbi request reprint CADASIL mutations impair Notch3 glycosylation by Fringe
    Joseph 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...
  29. pmc Dual roles of Cripto as a ligand and coreceptor in the nodal signaling pathway
    Yu 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...
  30. ncbi request reprint Identification and characterization of abeta1,3-glucosyltransferase that synthesizes the Glc-beta1,3-Fuc disaccharide on thrombospondin type 1 repeats
    Krisztina 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...
  31. ncbi request reprint O-fucosylation of thrombospondin type 1 repeats in ADAMTS-like-1/punctin-1 regulates secretion: implications for the ADAMTS superfamily
    Lauren 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...
  32. ncbi request reprint The threonine that carries fucose, but not fucose, is required for Cripto to facilitate Nodal signaling
    Shaolin 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...
  33. pmc Rumi is a CAP10 domain glycosyltransferase that modifies Notch and is required for Notch signaling
    Melih 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...
  34. ncbi request reprint O-fucosylation is required for ADAMTS13 secretion
    Lindsay 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...