Gaa1p and Gpi8p Are Components of a Glycosylphosphatidylinositol (GPI) Transamidase That Mediates Attachment of GPI to Proteins
Identifieur interne : 001226 ( Pmc/Checkpoint ); précédent : 001225; suivant : 001227Gaa1p and Gpi8p Are Components of a Glycosylphosphatidylinositol (GPI) Transamidase That Mediates Attachment of GPI to Proteins
Auteurs : Kazuhito Ohishi [Japon] ; Norimitsu Inoue [Japon] ; Yusuke Maeda [Japon] ; Junji Takeda [Japon] ; Howard Riezman [Suisse] ; Taroh Kinoshita [Japon]Source :
- Molecular Biology of the Cell [ 1059-1524 ] ; 2000.
Abstract
Many eukaryotic cell surface proteins are anchored to the membrane via glycosylphosphatidylinositol (GPI). The GPI is attached to proteins that have a GPI attachment signal peptide at the carboxyl terminus. The GPI attachment signal peptide is replaced by a preassembled GPI in the endoplasmic reticulum by a transamidation reaction through the formation of a carbonyl intermediate. GPI transamidase is a key enzyme of this posttranslational modification. Here we report that Gaa1p and Gpi8p are components of a GPI transamidase. To determine a role of Gaa1p we disrupted a
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PubMed: 10793132
PubMed Central: 14864
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Gaa1p and Gpi8p Are Components of a Glycosylphosphatidylinositol (GPI) Transamidase That Mediates Attachment of GPI to Proteins</title>
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<author><name sortKey="Inoue, Norimitsu" sort="Inoue, Norimitsu" uniqKey="Inoue N" first="Norimitsu" last="Inoue">Norimitsu Inoue</name>
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<series><title level="j">Molecular Biology of the Cell</title>
<idno type="ISSN">1059-1524</idno>
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<front><div type="abstract" xml:lang="en"><p>Many eukaryotic cell surface proteins are anchored to the membrane via glycosylphosphatidylinositol (GPI). The GPI is attached to proteins that have a GPI attachment signal peptide at the carboxyl terminus. The GPI attachment signal peptide is replaced by a preassembled GPI in the endoplasmic reticulum by a transamidation reaction through the formation of a carbonyl intermediate. GPI transamidase is a key enzyme of this posttranslational modification. Here we report that Gaa1p and Gpi8p are components of a GPI transamidase. To determine a role of Gaa1p we disrupted a <italic>GAA1/GPAA1</italic>
gene in mouse F9 cells by homologous recombination. <italic>GAA1</italic>
knockout cells were defective in the formation of carbonyl intermediates between precursor proteins and transamidase as determined by an in vitro GPI-anchoring assay. We also show that cysteine and histidine residues of Gpi8p, which are conserved in members of a cysteine protease family, are essential for generation of a carbonyl intermediate. This result suggests that Gpi8p is a catalytic component that cleaves the GPI attachment signal peptide. Moreover, Gaa1p and Gpi8p are associated with each other. Therefore, Gaa1p and Gpi8p constitute a GPI transamidase and cooperate in generating a carbonyl intermediate, a prerequisite for GPI attachment.</p>
</div>
</front>
</TEI>
<pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Mol Biol Cell</journal-id>
<journal-id journal-id-type="publisher-id">MOL BIOL CELL</journal-id>
<journal-title>Molecular Biology of the Cell</journal-title>
<issn pub-type="ppub">1059-1524</issn>
<publisher><publisher-name>The American Society for Cell Biology</publisher-name>
</publisher>
</journal-meta>
<article-meta><article-id pub-id-type="pmid">10793132</article-id>
<article-id pub-id-type="pmc">14864</article-id>
<article-id pub-id-type="publisher-id">1184</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Article</subject>
</subj-group>
</article-categories>
<title-group><article-title>Gaa1p and Gpi8p Are Components of a Glycosylphosphatidylinositol (GPI) Transamidase That Mediates Attachment of GPI to Proteins</article-title>
</title-group>
<contrib-group><contrib contrib-type="author"><name><surname>Ohishi</surname>
<given-names>Kazuhito</given-names>
</name>
<xref ref-type="aff" rid="N0x8dd0168.0x8d1aea8">*</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Inoue</surname>
<given-names>Norimitsu</given-names>
</name>
<xref ref-type="aff" rid="N0x8dd0168.0x8d1aea8">*</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Maeda</surname>
<given-names>Yusuke</given-names>
</name>
<xref ref-type="aff" rid="N0x8dd0168.0x8d1aea8">*</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Takeda</surname>
<given-names>Junji</given-names>
</name>
<xref ref-type="aff" rid="N0x8dd0168.0x8d1aea8">*</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Riezman</surname>
<given-names>Howard</given-names>
</name>
<xref ref-type="aff" rid="N0x8dd0168.0x8d1aea8">†</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Kinoshita</surname>
<given-names>Taroh</given-names>
</name>
<xref ref-type="aff" rid="N0x8dd0168.0x8d1aea8">*</xref>
<xref ref-type="author-notes" rid="FN152">‡</xref>
</contrib>
</contrib-group>
<aff id="N0x8dd0168.0x8d1aea8"><label>*</label>
Department of Immunoregulation, Research Institute for Microbial Diseases, Osaka University, Osaka 565-0871, Japan; and<label>†</label>
Biozentrum, University of Basel, Basel CH-4056, Switzerland</aff>
<contrib-group><contrib contrib-type="editor"><name><surname>Guidotti</surname>
<given-names>Guido</given-names>
</name>
<role>Monitoring Editor</role>
</contrib>
</contrib-group>
<author-notes><fn id="FN152"><label>‡</label>
<p>Corresponding author. E-mail address: <email>tkinoshi@biken.osaka-u.ac.jp</email>
.</p>
</fn>
</author-notes>
<pub-date pub-type="ppub"><month>5</month>
<year>2000</year>
</pub-date>
<volume>11</volume>
<issue>5</issue>
<fpage>1523</fpage>
<lpage>1533</lpage>
<history><date date-type="received"><day>16</day>
<month>12</month>
<year>1999</year>
</date>
<date date-type="accepted"><day>17</day>
<month>2</month>
<year>2000</year>
</date>
</history>
<copyright-statement>Copyright © 2000, The American Society for Cell Biology</copyright-statement>
<copyright-year>2000</copyright-year>
<abstract><p>Many eukaryotic cell surface proteins are anchored to the membrane via glycosylphosphatidylinositol (GPI). The GPI is attached to proteins that have a GPI attachment signal peptide at the carboxyl terminus. The GPI attachment signal peptide is replaced by a preassembled GPI in the endoplasmic reticulum by a transamidation reaction through the formation of a carbonyl intermediate. GPI transamidase is a key enzyme of this posttranslational modification. Here we report that Gaa1p and Gpi8p are components of a GPI transamidase. To determine a role of Gaa1p we disrupted a <italic>GAA1/GPAA1</italic>
gene in mouse F9 cells by homologous recombination. <italic>GAA1</italic>
knockout cells were defective in the formation of carbonyl intermediates between precursor proteins and transamidase as determined by an in vitro GPI-anchoring assay. We also show that cysteine and histidine residues of Gpi8p, which are conserved in members of a cysteine protease family, are essential for generation of a carbonyl intermediate. This result suggests that Gpi8p is a catalytic component that cleaves the GPI attachment signal peptide. Moreover, Gaa1p and Gpi8p are associated with each other. Therefore, Gaa1p and Gpi8p constitute a GPI transamidase and cooperate in generating a carbonyl intermediate, a prerequisite for GPI attachment.</p>
</abstract>
</article-meta>
</front>
</pmc>
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<name sortKey="Maeda, Yusuke" sort="Maeda, Yusuke" uniqKey="Maeda Y" first="Yusuke" last="Maeda">Yusuke Maeda</name>
<name sortKey="Takeda, Junji" sort="Takeda, Junji" uniqKey="Takeda J" first="Junji" last="Takeda">Junji Takeda</name>
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<country name="Suisse"><noRegion><name sortKey="Riezman, Howard" sort="Riezman, Howard" uniqKey="Riezman H" first="Howard" last="Riezman">Howard Riezman</name>
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