Characterisation of the enzymatic complex for the first step in glycosylphosphatidylinositol biosynthesis

Tiede, Andreas; Nischan, Claudia; Schubert, Jörg; Schmidt, Reinhold

doi:10.1016/s1357-2725(99)00122-3

Cited by 25 publications

(17 citation statements)

References 20 publications

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“…A complex of at least six proteins (GPI-GnT) is involved, of which Gpi3 is catalytic because it can be labeled with a photoactivatable UDP-GlcNAc analog (Kostova et al 2000). GlcNAc transfer occurs at the cytoplasmic face of the ER membrane (Vidugiriene and Menon 1993;Watanabe et al 1996;Tiede et al 2000). Essential Gpi2, Gpi15, and Gpi19 (Leidich et al 1995;Yan et al 2001;Newman et al 2005), and nonessential Gpi1 and Eri1 (Leidich and Orlean 1996;Sobering et al 2004), are also required for GlcNAc-PI synthesis.…”

Section: Gpi Anchoringmentioning

confidence: 99%

“…ERI1 and GPI1 null mutants are temperature-sensitive. The mammalian orthologs of these proteins form a complex (Watanabe et al 1998;Tiede et al 2000;Eisenhaber et al 2003;, and the yeast proteins likely also do, for Eri1 and Gpi19 associate with Gpi2 (Sobering et al 2004;Newman et al 2005). Roles of the noncatalytic subunits are unclear.…”

Section: Gpi Anchoringmentioning

confidence: 99%

“…The acyl chains of the PI species that receive are the same length as those in other membrane phospholipids (Sipos et al 1997). Evidence that GlcNAc transfer occurs at the cytoplasmic face of the ER membrane is that i) the catalytic domain of Gpi3's human orthologue faces the cytoplasm (Watanabe et al 1996;Tiede et al 2000), and ii) GlcNAc--PI can be labeled with membrane topological probes on the cytoplasmic side of the mammalian ER membrane (Vidugiriene and Menon, 1993).…”

Section: Assembly Of the Gpi Precursor And Its Attachment To Protein mentioning

confidence: 99%

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Architecture and Biosynthesis of the Saccharomyces cerevisiae Cell Wall

2012

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The wall gives a Saccharomyces cerevisiae cell its osmotic integrity; defines cell shape during budding growth, mating, sporulation, and pseudohypha formation; and presents adhesive glycoproteins to other yeast cells. The wall consists of b1,3-and b1,6-glucans, a small amount of chitin, and many different proteins that may bear N-and O-linked glycans and a glycolipid anchor. These components become cross-linked in various ways to form higher-order complexes. Wall composition and degree of cross-linking vary during growth and development and change in response to cell wall stress. This article reviews wall biogenesis in vegetative cells, covering the structure of wall components and how they are cross-linked; the biosynthesis of N-and O-linked glycans, glycosylphosphatidylinositol membrane anchors, b1,3-and b1,6-linked glucans, and chitin; the reactions that cross-link wall components; and the possible functions of enzymatic and nonenzymatic cell wall proteins. TABLE OF CONTENTS Abstract 775Introduction 777

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Section: Gpi Anchoringmentioning

confidence: 99%

Section: Gpi Anchoringmentioning

confidence: 99%

Section: Assembly Of the Gpi Precursor And Its Attachment To Protein mentioning

confidence: 99%

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Architecture and Biosynthesis of the Saccharomyces cerevisiae Cell Wall

2012

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“…CD9/CD81 double knockout female mice are completely infertile, suggesting that CD9 and CD81 play complementary roles in fertilization [84]. Interestingly, glycosylphosphatidyl inositol (GPI)-anchored proteins in oocytes have been implicated by an oocyte-specific knockout of Piga, a subunit of an N-acetyl glucosaminyl transferase that participates in first steps of the synthesis of GPI-anchored proteins [85]; female mice with this oocyte-specific Piga knockout are infertile [86]. It is possible that the Piga deficiency and the resulting lack of GPI-anchored proteins in the oocyte membrane alters membrane composition and/or organization so that sperm interactions are not favored.…”

Section: Gamete Membrane Fusion and The Oocyte-to-embryo Transitionmentioning

confidence: 99%

Membrane Fusions During Mammalian Fertilization

Gadella

Evans

2011

Advances in Experimental Medicine and Biology

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Successful completion of fertilization in mammals requires three different types of membrane fusion events. Firstly, the sperm cell will need to secrete its acrosome contents (acrosome exocytosis; also known as the acrosome reaction); this allows the sperm to penetrate the extracellular matrix of the oocyte (zona pellucida) and to reach the oocyte plasma membrane, the site of fertilization. Next the sperm cell will bind and fuse with the oocyte plasma membrane (also known as the oolemma), which is a different type of fusion in which two different cells fuse together. Finally, the fertilized oocyte needs to prevent polyspermic fertilization, or fertilization by more than one sperm. To this end, the oocyte secretes the contents of cortical granules by exocytotic fusions of these vesicles with the oocyte plasma membrane over the entire oocyte cell surface (also known as the cortical reaction or cortical granule exocytosis). The secreted cortical contents modify the zona pellucida, converting it to a state that is unreceptive to sperm, constituting a block to polyspermy. In addition, there is a block at the level of the oolemma (also known as the membrane block to polyspermy). IntroductionFertilization of the oocyte involves three membrane fusion events [1] namely, (1) a preparative series of secretion membrane fusions at the apical sperm surface known as acrosome exocytosis [2]. The membrane fusions are induced when the sperm cell binds to specific zona binding proteins at the sperm surface [3][4][5][6][7]. The acrosome exocytosis is a multipoint membrane fusion event between the sperm plasma membrane and the outer acrosomal membrane (see Fig. 5.1 [8,9]) and the exposed acrosomal content is required for sperm to penetrate the zona pellucida [10][11][12]. This so-called zona drilling effectively takes place because the sperm at this stage also has acquired hyperactivated motility [13]. (2) After zona penetration the sperm enters the perivitelline space where it can bind and fuse with the oocyte plasma membrane [14,15]. This is the actual fertilization fusion in which the contents of the sperm are delivered into the oocyte cytoplasm. The plasma membrane of the equatorial segment (see Fig. 5.1) is the site where proteins are located that orchestrate sperm-oocyte binding and fusion [16]. (3) In order to prevent polyspermy the oocyte has to activate defense systems to block redundant sperm-oocyte fusion [17]. To this end the first fertilizing sperm delivers activation factors

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“…The PIG-A gene encodes a subunit of N-acetyl glucosaminyl transferase, which is the enzyme involved in the first step of the biosynthesis of the GPI-anchor (Tiede et al 2000). Participation of oocytespecific GPI-anchored proteins in the sperm -oocyte interaction was suggested earlier in a study in which oocytes were treated with phosphatidylinositol-specific phospholipase C (PI-PLC; Coonrod et al 1999).…”

Section: Glycosylphosphatidylinositol (Gpi)-anchored Proteins On Oocytesmentioning

confidence: 99%

The mechanism of sperm–oocyte fusion in mammals

Kaji¹,

Kudo²

2004

Reproduction

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Sperm-oocyte fusion is one of the most impressive events in sexual reproduction, and the elucidation of its molecular mechanism has fascinated researchers for a long time. Because of the limitation of materials and difficulties in analyzing membrane protein -protein interactions, many attempts have failed to reach this goal. Recent studies involving gene targeting have clearly demonstrated the various molecules that are involved in sperm-oocyte binding and fusion. Sperm ADAMs (family of proteins with a disintegrin and metalloprotease domain), including fertilin a, fertilin b and cyritestin, have been investigated and found to be important for binding rather than for fusion and painstaking studies have raised suspicions that their putative receptors, oocyte integrins, are necessary for the sperm -oocyte interaction. Recently, several studies have focused the spotlight on CD9 and glycosylphosphatidylinositol (GPI)-anchored proteins on oocytes, and epididymal protein DE on sperm, as candidate molecules involved in sperm-oocyte fusion. Lack of, or interference with the function of, these proteins can disrupt the sperm -oocyte fusion without changing the binding. In this review we highlight the candidate molecules involved in the sperm-oocyte interaction suggested from the recent progress in this research field.

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Characterisation of the enzymatic complex for the first step in glycosylphosphatidylinositol biosynthesis

Cited by 25 publications

References 20 publications

Architecture and Biosynthesis of the Saccharomyces cerevisiae Cell Wall

Architecture and Biosynthesis of the Saccharomyces cerevisiae Cell Wall

Membrane Fusions During Mammalian Fertilization

The mechanism of sperm–oocyte fusion in mammals

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