Gpi19, the
            <i>Saccharomyces cerevisiae</i>
            Homologue of Mammalian PIG-P, Is a Subunit of the Initial Enzyme for Glycosylphosphatidylinositol Anchor Biosynthesis

Newman, Heather; Romeo, Martin J.; Lewis, Sarah; Yan, Benjamin C.; Orlean, Peter; Levin, David E.

doi:10.1128/ec.4.11.1801-1807.2005

Cited by 29 publications

(25 citation statements)

References 45 publications

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“…Cells were isolated, washed and cultured in synthetic defined medium lacking uracil ± Dox for 18 hrs to OD 600 < 1.0. Zymolyase resistance assays were performed according to Newman et al (2005). Cells were grown in synthetic defined medium lacking uracil in the presence or absence of Dox at 30°C for the indicated times.…”

Section: Methodsmentioning

confidence: 99%

A Lipid Transfer Protein Signaling Axis Exerts Dual Control of Cell-Cycle and Membrane Trafficking Systems

et al. 2018

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Kes1/Osh4 is a member of the conserved, but functionally enigmatic, oxysterol binding protein-related protein (ORP) superfamily that inhibits phosphatidylinositol transfer protein (Sec14)-dependent membrane trafficking through the trans-Golgi (TGN)/endosomal network. We now report that Kes1, and select other ORPs, execute cell-cycle control activities as functionally non-redundant inhibitors of the G/S transition when cells confront nutrient-poor environments and promote replicative aging. Kes1-dependent cell-cycle regulation requires the Greatwall/MASTL kinase ortholog Rim15, and is opposed by Sec14 activity in a mechanism independent of Kes1/Sec14 bulk membrane-trafficking functions. Moreover, the data identify Kes1 as a non-histone target for NuA4 through which this lysine acetyltransferase co-modulates membrane-trafficking and cell-cycle activities. We propose the Sec14/Kes1 lipid-exchange protein pair constitutes part of the mechanism for integrating TGN/endosomal lipid signaling with cell-cycle progression and hypothesize that ORPs define a family of stage-specific cell-cycle control factors that execute tumor-suppressor-like functions.

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Section: Methodsmentioning

confidence: 99%

A Lipid Transfer Protein Signaling Axis Exerts Dual Control of Cell-Cycle and Membrane Trafficking Systems

et al. 2018

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“…This transfer reaction occurs at the cytosolic surface of the ER and is critically dependent on Gpi3p, Gpi1p, Gpi2p, and Gpi15p and Gpi19p, which together form a multisubunit enzyme complex in the ER [33][34][35]. For some of them, the corresponding genes have first been cloned in the mammalian system by the group of Taroh Kinoshita, and the interactions of the various partners has been elaborated mainly in this system.…”

Section: Step 1: Pi-glcnac-transferasementioning

confidence: 99%

“…For some of them, the corresponding genes have first been cloned in the mammalian system by the group of Taroh Kinoshita, and the interactions of the various partners has been elaborated mainly in this system. However the strict conservation of all subunits in yeast and limited biochemical analysis suggest that the same multisubunit complex is operating in yeast [35]. Gpi3p contains a glycosyltransferase motif that is utilized by many glycosyltransferases of widely different specificity (Pfam PF00534), as well as a further motif, that is only shared amongst enzymes transferring GlcNAc to PI (Pfam PF08288).…”

Section: Step 1: Pi-glcnac-transferasementioning

confidence: 99%

Biosynthesis and function of GPI proteins in the yeast Saccharomyces cerevisiae

Pittet¹,

Conzelmann²

2007

Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biolog

214

209

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Like most other eukaryotes, Saccharomyces cerevisiae harbors a GPI anchoring machinery and uses it to attach proteins to membranes. While a few GPI proteins reside permanently at the plasma membrane, a majority of them gets further processed and is integrated into the cell wall by a covalent attachment to cell wall glucans. The GPI biosynthetic pathway is necessary for growth and survival of yeast cells. The GPI lipids are synthesized in the ER and added onto proteins by a pathway comprising 12 steps, carried out by 23 gene products, 19 of which are essential. Some of the estimated 60 GPI proteins predicted from the genome sequence serve enzymatic functions required for the biosynthesis and the continuous shape adaptations of the cell wall, others seem to be structural elements of the cell wall and yet others mediate cell adhesion. Because of its genetic tractability S. cerevisiae is an attractive model organism not only for studying GPI biosynthesis in general, but equally for investigating the intracellular transport of GPI proteins and the peculiar role of GPI anchoring in the elaboration of fungal cell walls.

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“…growth (59,63,64). To date, Ras GTPases have not been found to regulate the activity of mammalian GPI-GnT (65).…”

Section: Biosynthesis Of the Gpi Precursormentioning

confidence: 99%

“…The GlcNAc transfer reaction is unexpectedly complex in that many proteins are involved. The mammalian proteins and their yeast orthologs are PIG-A/Gpi3p, PIG-C/Gpi2p, PIG-H/Gpi15p, PIG-P/Gpi19p, PIG-Q(hGpi1p)/Gpi1p, and PIG-Y/Eri1p (50)(51)(52)(53)(54)(55)(56)(57)(58)(59)(60)(61)(62)(63)(64)(65). In mammalian cells, a seventh protein, Dpm2p, a noncatalytic subunit of Dol-P-Man synthase, physically associates with the PIG-A, -C, and -Q proteins and enhances GlcNAc-PI synthetic activity (58).…”

Section: Biosynthesis Of the Gpi Precursormentioning

confidence: 99%

Thematic review series: Lipid Posttranslational Modifications. GPI anchoring of protein in yeast and mammalian cells, or: how we learned to stop worrying and love glycophospholipids

Orlean

Menon

2007

Journal of Lipid Research

361

293

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Glycosylphosphatidylinositol (GPI) anchoring of cell surface proteins is the most complex and metabolically expensive of the lipid posttranslational modifications described to date. The GPI anchor is synthesized via a membrane-bound multistep pathway in the endoplasmic reticulum (ER) requiring .20 gene products. The pathway is initiated on the cytoplasmic side of the ER and completed in the ER lumen, necessitating flipping of a glycolipid intermediate across the membrane. The completed GPI anchor is attached to proteins that have been translocated across the ER membrane and that display a GPI signal anchor sequence at the C terminus. GPI proteins transit the secretory pathway to the cell surface; in yeast, many become covalently attached to the cell wall. Genes encoding proteins involved in all but one of the predicted steps in the assembly of the GPI precursor glycolipid and its transfer to protein in mammals and yeast have now been identified. Most of these genes encode polytopic membrane proteins, some of which are organized in complexes. The steps in GPI assembly, and the enzymes that carry them out, are highly conserved. GPI biosynthesis is essential for viability in yeast and for embryonic development in mammals. In this review, we describe the biosynthesis of mammalian and yeast GPIs, their transfer to protein, and their subsequent processing.-Orlean, P., and A. K. Menon. GPI anchoring of protein in yeast and mammalian cells, or: how we learned to stop worrying and love glycophospholipids.

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Gpi19, the Saccharomyces cerevisiae Homologue of Mammalian PIG-P, Is a Subunit of the Initial Enzyme for Glycosylphosphatidylinositol Anchor Biosynthesis

Abstract: Glycosylphosphatidylinositols (GPIs

Cited by 29 publications

References 45 publications

A Lipid Transfer Protein Signaling Axis Exerts Dual Control of Cell-Cycle and Membrane Trafficking Systems

A Lipid Transfer Protein Signaling Axis Exerts Dual Control of Cell-Cycle and Membrane Trafficking Systems

Biosynthesis and function of GPI proteins in the yeast Saccharomyces cerevisiae

Thematic review series: Lipid Posttranslational Modifications. GPI anchoring of protein in yeast and mammalian cells, or: how we learned to stop worrying and love glycophospholipids

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