Correction of the class H defect in glycosylphosphatidylinositol anchor biosynthesis in Ltk- cells by a human cDNA clone.

Kamitani, Tetsu; Chang, Hui-Ming; Rollins, Carl T.; Waneck, Gerald L.; Yeh, Edward T.H.

doi:10.1016/s0021-9258(19)36842-5

Cited by 91 publications

(15 citation statements)

References 38 publications

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“…The pathway is initiated on the cytoplasmic side of the ER by GPI N-acetylglucosaminyl transferase (GPI-GnT), which catalyses the transfer of N-acetylglucosamine (GlcNAc) from uridine diphosphate (UDP)-GlcNAc to the 6-position of inositol to generate GlcNAc-PI. GPI-GnT is the most complex monoglycosyltransferase, consisting of seven subunits, PIGA [49], PIGC [50], PIGH [51], PIGQ (initially termed GPI1) [52], PIGP [53], PIGY [54] and DPM2 [53], of which PIGA is a catalytic subunit. PIGC, PIGH, PIGP and PIGY are essential for the activity of GPI-GnT although their specific functions are not clear [50,51,53,54].…”

Section: Biosynthetic Assembly Of Gpi Precursorsmentioning

confidence: 99%

Biosynthesis and biology of mammalian GPI-anchored proteins

2020

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At least 150 human proteins are glycosylphosphatidylinositol-anchored proteins (GPI-APs). The protein moiety of GPI-APs lacking transmembrane domains is anchored to the plasma membrane with GPI covalently attached to the C-terminus. The GPI consists of the conserved core glycan, phosphatidylinositol and glycan side chains. The entire GPI-AP is anchored to the outer leaflet of the lipid bilayer by insertion of fatty chains of phosphatidylinositol. Because of GPI-dependent membrane anchoring, GPI-APs have some unique characteristics. The most prominent feature of GPI-APs is their association with membrane microdomains or membrane rafts. In the polarized cells such as epithelial cells, many GPI-APs are exclusively expressed in the apical surfaces, whereas some GPI-APs are preferentially expressed in the basolateral surfaces. Several GPI-APs act as transcytotic transporters carrying their ligands from one compartment to another. Some GPI-APs are shed from the membrane after cleavage within the GPI by a GPI-specific phospholipase or a glycosidase. In this review, I will summarize the current understanding of GPI-AP biosynthesis in mammalian cells and discuss examples of GPI-dependent functions of mammalian GPI-APs.

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Section: Biosynthetic Assembly Of Gpi Precursorsmentioning

confidence: 99%

Biosynthesis and biology of mammalian GPI-anchored proteins

2020

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“…The synthesis of GlcNAc–PI is catalyzed by UDP-GlcNAc–PI α1-6 GlcNAc-transferase (henceforth GPI GlcNAc transferase), a multisubunit, membrane-bound complex consisting of Gpi1/PIG-Q, Gpi2/PIG-C, Gpi3/PIG-A, Gpi15/PIG-H, Gpi19/PIG-P, and Eri1/PIG-Y (nomenclature corresponding to yeast/mammals) ( 11 , 12 , 13 , 14 , 15 , 16 , 17 , 18 , 19 , 20 ); in mammalian cells, a seventh subunit, Dpm2, has been reported ( 20 ). The multisubunit nature of this enzyme is unexpected and enigmatic.…”

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confidence: 99%

Elimination of GPI2 suppresses glycosylphosphatidylinositol GlcNAc transferase activity and alters GPI glycan modification in Trypanosoma brucei

Jenni

Knüsel

Nagar

et al. 2021

Journal of Biological Chemistry

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This is a PDF file of an article that has undergone enhancements after acceptance, such as the addition of a cover page and metadata, and formatting for readability, but it is not yet the definitive version of record. This version will undergo additional copyediting, typesetting and review before it is published in its final form, but we are providing this version to give early visibility of the article. Please note that, during the production process, errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain.

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“…synthesis of GlcNAc-PI. Genes capable of complementing the defect in these cell lines were identifie d and designate d PIG-A (phosphatidyl inositol glycan-A), PIG-C, PIG-H (Kamitani et al 1993, Miyata et al 1993. A fourth gene, GPI1, was first identifie d in the yeast Saccharomyce s cerevisia e, and found also to be involve d in GlcNAc-PI biosynthesis Orlean 1996, Tiede et al 1998).…”

Section: Topological Complexity In Gpi Assemblymentioning

confidence: 99%

Recent developments in the cell biology and biochemistry of glycosylphosphatidylinositol lipids (Review)

McConville

Menon²

2000

Molecular Membrane Biology

136

121

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Glycosylphosphatidylinositols (GPIs) represent an abundant and ubiquitous class of eukaryotic glycolipids. Although these structures were originally discovered in the form of GPI-anchored cell surface glycoproteins, it is becoming increasingly clear that a significant proportion of the GPI synthetic output of a cell is not directed to protein anchoring. Indeed, pools of non-protein-linked GPIs can approach 10(7) molecules per cell in some cell types, especially the protozoa, with a large proportion of these molecules being displayed at the cell surface. Recent studies which form the subject of this review indicate that there is (a) considerable diversity in the range of structural modifications found on GPI glycolipids within and between species and cell types, (b) complexity in the topological arrangement of the GPI biosynthetic pathway in the endoplasmic reticulum, and (c) spatial restriction of the biosynthetic pathway within the endoplasmic reticulum. Furthermore, consistent with additional functional roles for these lipids beyond serving as protein anchor precursors, products of the GPI biosynthetic pathway appear to be widely distributed in the cellular endomembrane system. These studies indicate that there is still much to learn about the organization of glycolipid biosynthetic pathways in eukaryotic cells, the nature and subcellular distribution of the lipid products of these pathways, and the function of these lipids within cells.

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Correction of the class H defect in glycosylphosphatidylinositol anchor biosynthesis in Ltk- cells by a human cDNA clone.

Cited by 91 publications

References 38 publications

Biosynthesis and biology of mammalian GPI-anchored proteins

Biosynthesis and biology of mammalian GPI-anchored proteins

Elimination of GPI2 suppresses glycosylphosphatidylinositol GlcNAc transferase activity and alters GPI glycan modification in Trypanosoma brucei

Recent developments in the cell biology and biochemistry of glycosylphosphatidylinositol lipids (Review)

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