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Semisynthesis of a Glycosylphosphatidylinositol‐Anchored Prion Protein
Angewandte Chemie - International Edition, 2008Pinning down the role of the anchor: The chemical synthesis of a cysteine-modified glycosylphosphatidylinositol (GPI) anchor provides access to homogeneous GPI-anchored prion protein through expressed protein ligation (see scheme). By this method, it should be possible to investigate the influence of the complex posttranslational GPI modification on ...
Christian F W Becker +2 more
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Structure of human glycosylphosphatidylinositol transamidase
Nature Structural & Molecular Biology, 2022Glycosylphosphatidylinositol (GPI) molecules are complex glycophospholipids and serve as membrane anchors for tethering many proteins to the cell surface. Attaching GPI to the protein in the endoplasmic reticulum (ER) is catalyzed by the transmembrane GPI transamidase (GPIT) complex, which is essential for maturation of the GPI-anchored proteins.
Hongwei Zhang +9 more
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Chemical Biology of Glycosylphosphatidylinositol Anchors
Angewandte Chemie International Edition, 2012AbstractGlycosylphosphatidylinositols (GPIs) are complex glycolipids that are covalently linked to the C‐terminus of proteins as a posttranslational modification. They anchor the attached protein to the cell membrane and are essential for normal functioning of eukaryotic cells. GPI‐anchored proteins are structurally and functionally diverse.
Tsai, Y., Liu, X., Seeberger, P.
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Analytical Biochemistry, 1995
Glycosylphosphatidylinositol (GPI) membrane anchors are synthesized in the endoplasmic reticulum of eukaryotic cells. Synthesis of the core GPI structure is achieved by the sequential transfer of monosaccharides and phosphoethanolamine to phosphatidylinositol. The assembly process can be reproduced in vitro using membrane preparations supplemented with
Bütikofer P, Boschung M, Menon AK
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Glycosylphosphatidylinositol (GPI) membrane anchors are synthesized in the endoplasmic reticulum of eukaryotic cells. Synthesis of the core GPI structure is achieved by the sequential transfer of monosaccharides and phosphoethanolamine to phosphatidylinositol. The assembly process can be reproduced in vitro using membrane preparations supplemented with
Bütikofer P, Boschung M, Menon AK
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Structure, biosynthesis, and function of glycosylphosphatidylinositols
Biochemistry, 1990The last few years have witnessed an explosion in our knowledge of GPI membrane anchors and related glycolipids and molecules where structure details are available, as illustrated in Figure 2. There is now sufficient information on a handful of these molecules to allow a detailed comparison of their chemical structures.
J R, Thomas, R A, Dwek, T W, Rademacher
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Synthetic Glycosylphosphatidylinositol as Tools for Glycoparasitology Research
OMICS: A Journal of Integrative Biology, 2010Abstract Carbohydrate–protein interactions are involved in various intracellular functions and play an essential role in biological system, particularly at the level of cell–cell recognition, cell adhesion, and cell signaling processes.
Azzouz, N., Kamena, F., Seeberger, P.
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Anchoring of Glycosylphosphatidylinositol–Proteins to Liposomes
2003Publisher Summary This chapter presents the anchoring of glycosylphosphatidylinositol (GPI) proteins to liposomes. In vivo , GPI-anchored proteins concentrate exclusively into the exoleaflet of eukaryotic cell plasma membranes, together with cholesterol and most of the glycolipids.
Olivier, Nosjean, Bernard, Roux
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Methods in enzymology, 1995
Cleavage by the GPI-PLD provides definitive evidence of a minimal GPI structure: glucosamine-phosphatidylinositol. Unlike the case for PI-PLC, cleavage by the GPI-PLD is unaffected by acylation of the inositol ring. Thus the GPI-PLD provides an excellent simple enzymatic tool for analyzing the basic core structure of GPI anchors.
M A, Deeg, M A, Davitz
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Cleavage by the GPI-PLD provides definitive evidence of a minimal GPI structure: glucosamine-phosphatidylinositol. Unlike the case for PI-PLC, cleavage by the GPI-PLD is unaffected by acylation of the inositol ring. Thus the GPI-PLD provides an excellent simple enzymatic tool for analyzing the basic core structure of GPI anchors.
M A, Deeg, M A, Davitz
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1995
Publisher Summary This chapter discusses the use of the enzyme glycosylphosphatidylinositol–phospholipase D (GPI-PLD) as a tool for structural analysis of GPI-anchored proteins. The GPI–PLD is a phospholipase D present in all mammalian plasma.
Mark A. Deeg, Michael A. Davitz
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Publisher Summary This chapter discusses the use of the enzyme glycosylphosphatidylinositol–phospholipase D (GPI-PLD) as a tool for structural analysis of GPI-anchored proteins. The GPI–PLD is a phospholipase D present in all mammalian plasma.
Mark A. Deeg, Michael A. Davitz
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