Phosphatidylinositol 4-phosphate is required for translation initiation in Saccharomyces cerevisiae.
Identifieur interne : 001762 ( Main/Exploration ); précédent : 001761; suivant : 001763Phosphatidylinositol 4-phosphate is required for translation initiation in Saccharomyces cerevisiae.
Auteurs : Elisabetta Cameroni [Suisse] ; Claudio De Virgilio ; Olivier DelocheSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2006.
Descripteurs français
- KwdFr :
- MESH :
- génétique : Saccharomyces cerevisiae.
- métabolisme : Facteur-2 d'initiation eucaryote.
- pharmacologie : Androstadiènes, Antienzymes.
- physiologie : Phosphates phosphatidylinositol.
- Biosynthèse des protéines, Phosphorylation, Wortmannine.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Eukaryotic Initiation Factor-2.
- chemical , pharmacology : Androstadienes, Enzyme Inhibitors.
- chemical , physiology : Phosphatidylinositol Phosphates.
- genetics : Saccharomyces cerevisiae.
- Phosphorylation, Protein Biosynthesis, Wortmannin.
Abstract
The small natural product wortmannin inhibits protein synthesis by modulating several phosphatidylinositol (PI) metabolic pathways. A primary target of wortmannin in yeast is the plasma membrane-associated PI 4-kinase (PI4K) Stt4p, which is required for actin cytoskeleton organization. Here we show that wortmannin treatment or inactivation of Stt4p, but not disorganization of the actin cytoskeleton per se, leads to a rapid attenuation of translation initiation. Interestingly, inactivation of Pik1p, a wortmannin-insensitive, functionally distinct PI4K, implicated in the regulation of Golgi functions and secretion, also results in severe translation initiation defects with a marked increase of the phosphorylation of the translation initiation factor eIF2alpha. Because wortmannin largely phenocopies the effects of rapamycin (e.g. it triggers nuclear accumulation of Gln3p), it likely also inhibits the PI kinase-related, target of rapamycin (TOR) kinases. Importantly, however, neither inactivation of Stt4p nor Pik1p significantly affects TOR-controlled readouts other than translation initiation, indicating that these PI4Ks do not simply function upstream of TOR. Together, our results reveal the existence of a novel translation initiation control mechanism in yeast that is tightly coupled to the synthesis of distinct PI4P pools.
DOI: 10.1074/jbc.M601060200
PubMed: 17005563
Affiliations:
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Le document en format XML
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sortKey="Deloche, Olivier" sort="Deloche, Olivier" uniqKey="Deloche O" first="Olivier" last="Deloche">Olivier Deloche</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2006">2006</date><idno type="RBID">pubmed:17005563</idno><idno type="pmid">17005563</idno><idno type="doi">10.1074/jbc.M601060200</idno><idno type="wicri:Area/Main/Corpus">001761</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001761</idno><idno type="wicri:Area/Main/Curation">001761</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">001761</idno><idno type="wicri:Area/Main/Exploration">001761</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Phosphatidylinositol 4-phosphate is required for translation initiation in Saccharomyces cerevisiae.</title><author><name sortKey="Cameroni, Elisabetta" sort="Cameroni, Elisabetta" uniqKey="Cameroni E" first="Elisabetta" last="Cameroni">Elisabetta Cameroni</name><affiliation wicri:level="1"><nlm:affiliation>Department of Microbiology and Molecular Medicine, Centre Médical Universitaire, University of Geneva, 1 rue Michel-Servet, 1211 Geneva, Switzerland.</nlm:affiliation><country xml:lang="fr">Suisse</country><wicri:regionArea>Department of Microbiology and Molecular Medicine, Centre Médical Universitaire, University of Geneva, 1 rue Michel-Servet, 1211 Geneva</wicri:regionArea><wicri:noRegion>1211 Geneva</wicri:noRegion></affiliation></author><author><name sortKey="De Virgilio, Claudio" sort="De Virgilio, Claudio" uniqKey="De Virgilio C" first="Claudio" last="De Virgilio">Claudio De Virgilio</name></author><author><name sortKey="Deloche, Olivier" sort="Deloche, Olivier" uniqKey="Deloche O" first="Olivier" last="Deloche">Olivier Deloche</name></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="ISSN">0021-9258</idno><imprint><date when="2006" 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xml:lang="en"><term>Eukaryotic Initiation Factor-2</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Androstadienes</term><term>Enzyme Inhibitors</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Phosphatidylinositol Phosphates</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Facteur-2 d'initiation eucaryote</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Androstadiènes</term><term>Antienzymes</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Phosphates phosphatidylinositol</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Phosphorylation</term><term>Protein Biosynthesis</term><term>Wortmannin</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Biosynthèse des protéines</term><term>Phosphorylation</term><term>Wortmannine</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The small natural product wortmannin inhibits protein synthesis by modulating several phosphatidylinositol (PI) metabolic pathways. A primary target of wortmannin in yeast is the plasma membrane-associated PI 4-kinase (PI4K) Stt4p, which is required for actin cytoskeleton organization. Here we show that wortmannin treatment or inactivation of Stt4p, but not disorganization of the actin cytoskeleton per se, leads to a rapid attenuation of translation initiation. Interestingly, inactivation of Pik1p, a wortmannin-insensitive, functionally distinct PI4K, implicated in the regulation of Golgi functions and secretion, also results in severe translation initiation defects with a marked increase of the phosphorylation of the translation initiation factor eIF2alpha. Because wortmannin largely phenocopies the effects of rapamycin (e.g. it triggers nuclear accumulation of Gln3p), it likely also inhibits the PI kinase-related, target of rapamycin (TOR) kinases. Importantly, however, neither inactivation of Stt4p nor Pik1p significantly affects TOR-controlled readouts other than translation initiation, indicating that these PI4Ks do not simply function upstream of TOR. Together, our results reveal the existence of a novel translation initiation control mechanism in yeast that is tightly coupled to the synthesis of distinct PI4P pools.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17005563</PMID><DateCompleted><Year>2007</Year><Month>02</Month><Day>27</Day></DateCompleted><DateRevised><Year>2018</Year><Month>12</Month><Day>01</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>281</Volume><Issue>50</Issue><PubDate><Year>2006</Year><Month>Dec</Month><Day>15</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Phosphatidylinositol 4-phosphate is required for translation initiation in Saccharomyces cerevisiae.</ArticleTitle><Pagination><MedlinePgn>38139-49</MedlinePgn></Pagination><Abstract><AbstractText>The small natural product wortmannin inhibits protein synthesis by modulating several phosphatidylinositol (PI) metabolic pathways. A primary target of wortmannin in yeast is the plasma membrane-associated PI 4-kinase (PI4K) Stt4p, which is required for actin cytoskeleton organization. Here we show that wortmannin treatment or inactivation of Stt4p, but not disorganization of the actin cytoskeleton per se, leads to a rapid attenuation of translation initiation. Interestingly, inactivation of Pik1p, a wortmannin-insensitive, functionally distinct PI4K, implicated in the regulation of Golgi functions and secretion, also results in severe translation initiation defects with a marked increase of the phosphorylation of the translation initiation factor eIF2alpha. Because wortmannin largely phenocopies the effects of rapamycin (e.g. it triggers nuclear accumulation of Gln3p), it likely also inhibits the PI kinase-related, target of rapamycin (TOR) kinases. Importantly, however, neither inactivation of Stt4p nor Pik1p significantly affects TOR-controlled readouts other than translation initiation, indicating that these PI4Ks do not simply function upstream of TOR. 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