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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and" id="N0x8dd0168.0x8d1aea8">Department of Immunoregulation, Research Institute for Microbial Diseases, Osaka University, Osaka 565-0871, Japan</nlm:aff><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Immunoregulation, Research Institute for Microbial Diseases, Osaka University, Osaka 565-0871</wicri:regionArea><wicri:noRegion>Osaka 565-0871</wicri:noRegion></affiliation></author><author><name sortKey="Takeda, Junji" sort="Takeda, Junji" uniqKey="Takeda J" first="Junji" last="Takeda">Junji Takeda</name><affiliation wicri:level="1"><nlm:aff wicri:cut="; and" id="N0x8dd0168.0x8d1aea8">Department of Immunoregulation, Research Institute for Microbial Diseases, Osaka University, Osaka 565-0871, Japan</nlm:aff><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Immunoregulation, Research Institute for Microbial Diseases, Osaka University, Osaka 565-0871</wicri:regionArea><wicri:noRegion>Osaka 565-0871</wicri:noRegion></affiliation></author><author><name sortKey="Riezman, Howard" sort="Riezman, Howard" uniqKey="Riezman H" first="Howard" last="Riezman">Howard Riezman</name><affiliation wicri:level="1"><nlm:aff id="N0x8dd0168.0x8d1aea8">Biozentrum, University of Basel, Basel CH-4056, Switzerland</nlm:aff><country xml:lang="fr">Suisse</country><wicri:regionArea>Biozentrum, University of Basel, Basel CH-4056</wicri:regionArea><wicri:noRegion>Basel CH-4056</wicri:noRegion></affiliation></author><author><name sortKey="Kinoshita, Taroh" sort="Kinoshita, Taroh" uniqKey="Kinoshita T" first="Taroh" last="Kinoshita">Taroh Kinoshita</name><affiliation wicri:level="1"><nlm:aff wicri:cut="; and" id="N0x8dd0168.0x8d1aea8">Department of Immunoregulation, Research Institute for Microbial Diseases, Osaka University, Osaka 565-0871, Japan</nlm:aff><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Immunoregulation, Research Institute for Microbial Diseases, Osaka University, Osaka 565-0871</wicri:regionArea><wicri:noRegion>Osaka 565-0871</wicri:noRegion></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">10793132</idno><idno type="pmc">14864</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC14864</idno><idno type="RBID">PMC:14864</idno><date when="2000">2000</date><idno type="wicri:Area/Pmc/Corpus">000524</idno><idno type="wicri:Area/Pmc/Curation">000523</idno><idno type="wicri:Area/Pmc/Checkpoint">001226</idno></publicationStmt><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><author><name sortKey="Ohishi, Kazuhito" sort="Ohishi, Kazuhito" uniqKey="Ohishi K" first="Kazuhito" last="Ohishi">Kazuhito Ohishi</name><affiliation wicri:level="1"><nlm:aff wicri:cut="; and" id="N0x8dd0168.0x8d1aea8">Department of Immunoregulation, Research Institute for Microbial Diseases, Osaka University, Osaka 565-0871, Japan</nlm:aff><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Immunoregulation, Research Institute for Microbial Diseases, Osaka University, Osaka 565-0871</wicri:regionArea><wicri:noRegion>Osaka 565-0871</wicri:noRegion></affiliation></author><author><name sortKey="Inoue, Norimitsu" sort="Inoue, Norimitsu" uniqKey="Inoue N" first="Norimitsu" last="Inoue">Norimitsu Inoue</name><affiliation wicri:level="1"><nlm:aff wicri:cut="; and" id="N0x8dd0168.0x8d1aea8">Department of Immunoregulation, Research Institute for Microbial Diseases, Osaka University, Osaka 565-0871, Japan</nlm:aff><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Immunoregulation, Research Institute for Microbial Diseases, Osaka University, Osaka 565-0871</wicri:regionArea><wicri:noRegion>Osaka 565-0871</wicri:noRegion></affiliation></author><author><name sortKey="Maeda, Yusuke" sort="Maeda, Yusuke" uniqKey="Maeda Y" first="Yusuke" last="Maeda">Yusuke Maeda</name><affiliation wicri:level="1"><nlm:aff wicri:cut="; and" id="N0x8dd0168.0x8d1aea8">Department of Immunoregulation, Research Institute for Microbial Diseases, Osaka University, Osaka 565-0871, Japan</nlm:aff><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Immunoregulation, Research Institute for Microbial Diseases, Osaka University, Osaka 565-0871</wicri:regionArea><wicri:noRegion>Osaka 565-0871</wicri:noRegion></affiliation></author><author><name sortKey="Takeda, Junji" sort="Takeda, Junji" uniqKey="Takeda J" first="Junji" last="Takeda">Junji Takeda</name><affiliation wicri:level="1"><nlm:aff wicri:cut="; and" id="N0x8dd0168.0x8d1aea8">Department of Immunoregulation, Research Institute for Microbial Diseases, Osaka University, Osaka 565-0871, Japan</nlm:aff><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Immunoregulation, Research Institute for Microbial Diseases, Osaka University, Osaka 565-0871</wicri:regionArea><wicri:noRegion>Osaka 565-0871</wicri:noRegion></affiliation></author><author><name sortKey="Riezman, Howard" sort="Riezman, Howard" uniqKey="Riezman H" first="Howard" last="Riezman">Howard Riezman</name><affiliation wicri:level="1"><nlm:aff id="N0x8dd0168.0x8d1aea8">Biozentrum, University of Basel, Basel CH-4056, Switzerland</nlm:aff><country xml:lang="fr">Suisse</country><wicri:regionArea>Biozentrum, University of Basel, Basel CH-4056</wicri:regionArea><wicri:noRegion>Basel CH-4056</wicri:noRegion></affiliation></author><author><name sortKey="Kinoshita, Taroh" sort="Kinoshita, Taroh" uniqKey="Kinoshita T" first="Taroh" last="Kinoshita">Taroh Kinoshita</name><affiliation wicri:level="1"><nlm:aff wicri:cut="; and" id="N0x8dd0168.0x8d1aea8">Department of Immunoregulation, Research Institute for Microbial Diseases, Osaka University, Osaka 565-0871, Japan</nlm:aff><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Immunoregulation, Research Institute for Microbial Diseases, Osaka University, Osaka 565-0871</wicri:regionArea><wicri:noRegion>Osaka 565-0871</wicri:noRegion></affiliation></author></analytic><series><title level="j">Molecular Biology of the Cell</title><idno type="ISSN">1059-1524</idno><imprint><date when="2000">2000</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><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><affiliations><list><country><li>Japon</li><li>Suisse</li></country></list><tree><country name="Japon"><noRegion><name sortKey="Ohishi, Kazuhito" sort="Ohishi, Kazuhito" uniqKey="Ohishi K" first="Kazuhito" last="Ohishi">Kazuhito Ohishi</name></noRegion><name sortKey="Inoue, Norimitsu" sort="Inoue, Norimitsu" uniqKey="Inoue N" first="Norimitsu" last="Inoue">Norimitsu Inoue</name><name sortKey="Kinoshita, Taroh" sort="Kinoshita, Taroh" uniqKey="Kinoshita T" first="Taroh" last="Kinoshita">Taroh Kinoshita</name><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></country><country name="Suisse"><noRegion><name sortKey="Riezman, Howard" sort="Riezman, Howard" uniqKey="Riezman H" first="Howard" last="Riezman">Howard Riezman</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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