Requirement of PIG-F and PIG-O for Transferring Phosphoethanolamine to the Third Mannose in Glycosylphosphatidylinositol

Hong, Yeongjin; Maeda, Yusuke; Watanabe, Reika; Inoue, Norimitsu; Ohishi, Kazuhito; Kinoshita, Taroh

doi:10.1074/jbc.m001913200

Cited by 75 publications

(92 citation statements)

References 41 publications

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“…The major GPI accumulated upon Gpi13 depletion is a Man 4 -GPI with a single Etn-P on Man-1 (Flury et al 2000;Taron et al 2000). Gpi11 is likely involved in the GPI-Etn-P-T-III reaction because a gpi11-Ts mutant also accumulates a Man 4 -GPI with its Etn-P on Man-1 (K. Willis and P. Orlean, unpublished results), and human Gpi11 interacts with and stabilizes human Gpi13 (Hong et al 2000).…”

Section: Gpi Anchoringmentioning

confidence: 99%

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%

Architecture and Biosynthesis of the Saccharomyces cerevisiae Cell Wall

2012

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“…The presence of these side chains on CP2 came as a surprise in as much as a previous analysis of the pool of the protein-linked GPI anchors of S. cerevisiae had failed to reveal EtN-P or other substituents on Man1 or Man2 (14). Candidate EtN-P transferase genes required for the attachment of these substituents have been identified in humans and yeast: PIG-N and MCD4 are involved in the transfer of EtN-P from phosphatidylethanolamine (PE) onto Man1 (13,15,16), GPI7 in the transfer onto Man2 (12), and PIG-O and GPI13 in the transfer of EtN-P from PE onto Man3 (17)(18)(19)(20)(21). These genes are homologous to each other, are found throughout the eukaryotic kingdom, possess an N-terminal globular domain facing the lumen of the ER or the extracellular space and multiple transmembrane domains in their C terminus.…”

Section: From the Department Of Medicine University Of Fribourg Ch-mentioning

confidence: 99%

Glycosylphosphatidylinositol (GPI) Proteins of Saccharomyces cerevisiae Contain Ethanolamine Phosphate Groups on the α1,4-linked Mannose of the GPI Anchor

Imhof¹,

Flury²,

Vionnet

et al. 2004

Journal of Biological Chemistry

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In humans and Saccharomyces cerevisiae the free glycosylphosphatidylinositol (GPI) lipid precursor contains several ethanolamine phosphate side chains, but these side chains had been found on the protein-bound GPI anchors only in humans, not yeast. Here we confirm that the ethanolamine phosphate side chain added by Mcd4p to the first mannose is a prerequisite for the addition of the third mannose to the GPI precursor lipid and demonstrate that, contrary to an earlier report, an ethanolamine phosphate can equally be found on the majority of yeast GPI protein anchors. Curiously, the stability of this substituent during preparation of anchors is much greater in gpi7⌬ sec18 double mutants than in either single mutant or wild type cells, indicating that the lack of a substituent on the second mannose (caused by the deletion of GPI7) influences the stability of the one on the first mannose. The phosphodiesterlinked substituent on the second mannose, probably a further ethanolamine phosphate, is added to GPI lipids by endoplasmic reticulum-derived microsomes in vitro but cannot be detected on GPI proteins of wild type cells and undergoes spontaneous hydrolysis in saline. Genetic manipulations to increase phosphatidylethanolamine levels in gpi7⌬ cells by overexpression of PSD1 restore cell growth at 37°C without restoring the addition of a substituent to Man2. The three putative ethanolamine-phosphate transferases Gpi13p, Gpi7p, and Mcd4p cannot replace each other even when overexpressed. Various models trying to explain how Gpi7p, a plasma membrane protein, directs the addition of ethanolamine phosphate to mannose 2 of the GPI core have been formulated and put to the test.

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“…A GPI(Ϫ).O cell line that was deficient in the PIG-O gene (Hong et al, 2000) was isolated from the CHO(wt) cells (Hong et al, 2002). CHO-K1 and class L CHO mutant (M2S2; Nakamura et al, 1997) cells were cultured in Ham's F-12 medium containing 10% FCS.…”

Section: Other Cellsmentioning

confidence: 99%

Human PIG-U and Yeast Cdc91p Are the Fifth Subunit of GPI Transamidase That Attaches GPI-Anchors to Proteins

Hong

Ohishi

Kang

et al. 2003

MBoC

Self Cite

112

123

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Many eukaryotic proteins are anchored to the cell surface via glycosylphosphatidylinositol (GPI), which is posttranslationally attached to the carboxyl-terminus by GPI transamidase. The mammalian GPI transamidase is a complex of at least four subunits, GPI8, GAA1, PIG-S, and PIG-T. Here, we report Chinese hamster ovary cells representing a new complementation group of GPI-anchored protein-deficient mutants, class U. The class U cells accumulated mature and immature GPI and did not have in vitro GPI transamidase activity. We cloned the gene responsible, termed PIG-U, that encoded a 435-amino-acid hydrophobic protein. The GPI transamidase complex affinity-purified from cells expressing epitope-tagged-GPI8 contained PIG-U and four other known components. Cells lacking PIG-U formed complexes of the four other components normally but had no ability to cleave the GPI attachment signal peptide. Saccharomyces cerevisiae Cdc91p, with 28% amino acid identity to PIG-U, partially restored GPI-anchored proteins on the surface of class U cells. PIG-U and Cdc91p have a functionally important short region with similarity to a region conserved in long-chain fatty acid elongases. Taken together, PIG-U and the yeast orthologue Cdc91p are the fifth component of GPI transamidase that may be involved in the recognition of either the GPI attachment signal or the lipid portion of GPI

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Requirement of PIG-F and PIG-O for Transferring Phosphoethanolamine to the Third Mannose in Glycosylphosphatidylinositol

Cited by 75 publications

References 41 publications

Architecture and Biosynthesis of the Saccharomyces cerevisiae Cell Wall

Architecture and Biosynthesis of the Saccharomyces cerevisiae Cell Wall

Glycosylphosphatidylinositol (GPI) Proteins of Saccharomyces cerevisiae Contain Ethanolamine Phosphate Groups on the α1,4-linked Mannose of the GPI Anchor

Human PIG-U and Yeast Cdc91p Are the Fifth Subunit of GPI Transamidase That Attaches GPI-Anchors to Proteins

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