Activation of mTORC2 by association with the ribosome.
Identifieur interne : 001351 ( Main/Exploration ); précédent : 001350; suivant : 001352Activation of mTORC2 by association with the ribosome.
Auteurs : Vittoria Zinzalla [Suisse] ; Daniele Stracka ; Wolfgang Oppliger ; Michael N. HallSource :
- Cell [ 1097-4172 ] ; 2011.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Cellules HeLa (MeSH), Compagnon de mTOR insensible à la rapamycine (MeSH), Complexes multiprotéiques (métabolisme), Humains (MeSH), Insuline (métabolisme), Lignée cellulaire tumorale (MeSH), Phosphatidylinositol 3-kinases (métabolisme), Protéines de transport (métabolisme), Protéines proto-oncogènes c-akt (métabolisme), Ribosomes (métabolisme), Saccharomyces cerevisiae (métabolisme), Sérine-thréonine kinases TOR (métabolisme), Transduction du signal (MeSH).
- MESH :
- métabolisme : Complexes multiprotéiques, Insuline, Phosphatidylinositol 3-kinases, Protéines de transport, Protéines proto-oncogènes c-akt, Ribosomes, Saccharomyces cerevisiae, Sérine-thréonine kinases TOR.
- Animaux, Cellules HeLa, Compagnon de mTOR insensible à la rapamycine, Humains, Lignée cellulaire tumorale, Transduction du signal.
English descriptors
- KwdEn :
- Animals (MeSH), Carrier Proteins (metabolism), Cell Line, Tumor (MeSH), HeLa Cells (MeSH), Humans (MeSH), Insulin (metabolism), Multiprotein Complexes (metabolism), Phosphatidylinositol 3-Kinases (metabolism), Proto-Oncogene Proteins c-akt (metabolism), Rapamycin-Insensitive Companion of mTOR Protein (MeSH), Ribosomes (metabolism), Saccharomyces cerevisiae (metabolism), Signal Transduction (MeSH), TOR Serine-Threonine Kinases (metabolism).
- MESH :
- chemical , metabolism : Carrier Proteins, Insulin, Multiprotein Complexes, Phosphatidylinositol 3-Kinases, Proto-Oncogene Proteins c-akt, TOR Serine-Threonine Kinases.
- metabolism : Ribosomes, Saccharomyces cerevisiae.
- Animals, Cell Line, Tumor, HeLa Cells, Humans, Rapamycin-Insensitive Companion of mTOR Protein, Signal Transduction.
Abstract
The target of rapamycin (TOR) is a highly conserved protein kinase and a central controller of growth. Mammalian TOR complex 2 (mTORC2) regulates AGC kinase family members and is implicated in various disorders, including cancer and diabetes. Here, we investigated the upstream regulation of mTORC2. A genetic screen in yeast and subsequent studies in mammalian cells revealed that ribosomes, but not protein synthesis, are required for mTORC2 signaling. Active mTORC2 was physically associated with the ribosome, and insulin-stimulated PI3K signaling promoted mTORC2-ribosome binding, suggesting that ribosomes activate mTORC2 directly. Findings with melanoma and colon cancer cells suggest that mTORC2-ribosome association is important in oncogenic PI3K signaling. Thus, TORC2-ribosome interaction is a likely conserved mechanism of TORC2 activation that is physiologically relevant in both normal and cancer cells. As ribosome content determines growth capacity of a cell, this mechanism of TORC2 regulation ensures that TORC2 is active only in growing cells.
DOI: 10.1016/j.cell.2011.02.014
PubMed: 21376236
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Hall</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2011">2011</date><idno type="RBID">pubmed:21376236</idno><idno type="pmid">21376236</idno><idno type="doi">10.1016/j.cell.2011.02.014</idno><idno type="wicri:Area/Main/Corpus">001320</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001320</idno><idno type="wicri:Area/Main/Curation">001320</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">001320</idno><idno type="wicri:Area/Main/Exploration">001320</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Activation of mTORC2 by association with the ribosome.</title><author><name sortKey="Zinzalla, Vittoria" sort="Zinzalla, Vittoria" uniqKey="Zinzalla V" first="Vittoria" last="Zinzalla">Vittoria Zinzalla</name><affiliation wicri:level="1"><nlm:affiliation>Biozentrum, University of Basel, CH-4056 Basel, Switzerland.</nlm:affiliation><country xml:lang="fr">Suisse</country><wicri:regionArea>Biozentrum, University of Basel, CH-4056 Basel</wicri:regionArea><wicri:noRegion>CH-4056 Basel</wicri:noRegion></affiliation></author><author><name sortKey="Stracka, Daniele" sort="Stracka, Daniele" uniqKey="Stracka D" first="Daniele" last="Stracka">Daniele Stracka</name></author><author><name sortKey="Oppliger, Wolfgang" sort="Oppliger, Wolfgang" uniqKey="Oppliger W" first="Wolfgang" last="Oppliger">Wolfgang Oppliger</name></author><author><name sortKey="Hall, Michael N" sort="Hall, Michael N" uniqKey="Hall M" first="Michael N" last="Hall">Michael N. Hall</name></author></analytic><series><title level="j">Cell</title><idno type="eISSN">1097-4172</idno><imprint><date when="2011" type="published">2011</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Carrier Proteins (metabolism)</term><term>Cell Line, Tumor (MeSH)</term><term>HeLa Cells (MeSH)</term><term>Humans (MeSH)</term><term>Insulin (metabolism)</term><term>Multiprotein Complexes (metabolism)</term><term>Phosphatidylinositol 3-Kinases (metabolism)</term><term>Proto-Oncogene Proteins c-akt (metabolism)</term><term>Rapamycin-Insensitive Companion of mTOR Protein (MeSH)</term><term>Ribosomes (metabolism)</term><term>Saccharomyces cerevisiae (metabolism)</term><term>Signal Transduction (MeSH)</term><term>TOR Serine-Threonine Kinases (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Cellules HeLa (MeSH)</term><term>Compagnon de mTOR insensible à la rapamycine (MeSH)</term><term>Complexes multiprotéiques (métabolisme)</term><term>Humains (MeSH)</term><term>Insuline (métabolisme)</term><term>Lignée cellulaire tumorale (MeSH)</term><term>Phosphatidylinositol 3-kinases (métabolisme)</term><term>Protéines de transport (métabolisme)</term><term>Protéines proto-oncogènes c-akt (métabolisme)</term><term>Ribosomes (métabolisme)</term><term>Saccharomyces cerevisiae (métabolisme)</term><term>Sérine-thréonine kinases TOR (métabolisme)</term><term>Transduction du signal (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Carrier Proteins</term><term>Insulin</term><term>Multiprotein Complexes</term><term>Phosphatidylinositol 3-Kinases</term><term>Proto-Oncogene Proteins c-akt</term><term>TOR Serine-Threonine Kinases</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Ribosomes</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Complexes multiprotéiques</term><term>Insuline</term><term>Phosphatidylinositol 3-kinases</term><term>Protéines de transport</term><term>Protéines proto-oncogènes c-akt</term><term>Ribosomes</term><term>Saccharomyces cerevisiae</term><term>Sérine-thréonine kinases TOR</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cell Line, Tumor</term><term>HeLa Cells</term><term>Humans</term><term>Rapamycin-Insensitive Companion of mTOR Protein</term><term>Signal Transduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Cellules HeLa</term><term>Compagnon de mTOR insensible à la rapamycine</term><term>Humains</term><term>Lignée cellulaire tumorale</term><term>Transduction du signal</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The target of rapamycin (TOR) is a highly conserved protein kinase and a central controller of growth. Mammalian TOR complex 2 (mTORC2) regulates AGC kinase family members and is implicated in various disorders, including cancer and diabetes. Here, we investigated the upstream regulation of mTORC2. A genetic screen in yeast and subsequent studies in mammalian cells revealed that ribosomes, but not protein synthesis, are required for mTORC2 signaling. Active mTORC2 was physically associated with the ribosome, and insulin-stimulated PI3K signaling promoted mTORC2-ribosome binding, suggesting that ribosomes activate mTORC2 directly. Findings with melanoma and colon cancer cells suggest that mTORC2-ribosome association is important in oncogenic PI3K signaling. Thus, TORC2-ribosome interaction is a likely conserved mechanism of TORC2 activation that is physiologically relevant in both normal and cancer cells. As ribosome content determines growth capacity of a cell, this mechanism of TORC2 regulation ensures that TORC2 is active only in growing cells.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">21376236</PMID><DateCompleted><Year>2011</Year><Month>04</Month><Day>20</Day></DateCompleted><DateRevised><Year>2017</Year><Month>11</Month><Day>16</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1097-4172</ISSN><JournalIssue CitedMedium="Internet"><Volume>144</Volume><Issue>5</Issue><PubDate><Year>2011</Year><Month>Mar</Month><Day>04</Day></PubDate></JournalIssue><Title>Cell</Title><ISOAbbreviation>Cell</ISOAbbreviation></Journal><ArticleTitle>Activation of mTORC2 by association with the ribosome.</ArticleTitle><Pagination><MedlinePgn>757-68</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.cell.2011.02.014</ELocationID><Abstract><AbstractText>The target of rapamycin (TOR) is a highly conserved protein kinase and a central controller of growth. Mammalian TOR complex 2 (mTORC2) regulates AGC kinase family members and is implicated in various disorders, including cancer and diabetes. Here, we investigated the upstream regulation of mTORC2. A genetic screen in yeast and subsequent studies in mammalian cells revealed that ribosomes, but not protein synthesis, are required for mTORC2 signaling. Active mTORC2 was physically associated with the ribosome, and insulin-stimulated PI3K signaling promoted mTORC2-ribosome binding, suggesting that ribosomes activate mTORC2 directly. Findings with melanoma and colon cancer cells suggest that mTORC2-ribosome association is important in oncogenic PI3K signaling. Thus, TORC2-ribosome interaction is a likely conserved mechanism of TORC2 activation that is physiologically relevant in both normal and cancer cells. As ribosome content determines growth capacity of a cell, this mechanism of TORC2 regulation ensures that TORC2 is active only in growing cells.</AbstractText><CopyrightInformation>Copyright © 2011 Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Zinzalla</LastName><ForeName>Vittoria</ForeName><Initials>V</Initials><AffiliationInfo><Affiliation>Biozentrum, University of Basel, CH-4056 Basel, Switzerland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Stracka</LastName><ForeName>Daniele</ForeName><Initials>D</Initials></Author><Author ValidYN="Y"><LastName>Oppliger</LastName><ForeName>Wolfgang</ForeName><Initials>W</Initials></Author><Author ValidYN="Y"><LastName>Hall</LastName><ForeName>Michael N</ForeName><Initials>MN</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United 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MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007328" MajorTopicYN="N">Insulin</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D046912" MajorTopicYN="N">Multiprotein Complexes</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019869" MajorTopicYN="N">Phosphatidylinositol 3-Kinases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051057" MajorTopicYN="N">Proto-Oncogene Proteins c-akt</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000076226" MajorTopicYN="N">Rapamycin-Insensitive Companion of mTOR Protein</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012270" MajorTopicYN="N">Ribosomes</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015398" MajorTopicYN="Y">Signal Transduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D058570" MajorTopicYN="N">TOR Serine-Threonine Kinases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2010</Year><Month>07</Month><Day>14</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2010</Year><Month>10</Month><Day>20</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2011</Year><Month>02</Month><Day>07</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2011</Year><Month>3</Month><Day>8</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2011</Year><Month>3</Month><Day>8</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2011</Year><Month>4</Month><Day>22</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">21376236</ArticleId><ArticleId IdType="pii">S0092-8674(11)00128-0</ArticleId><ArticleId IdType="doi">10.1016/j.cell.2011.02.014</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Suisse</li></country></list><tree><noCountry><name sortKey="Hall, Michael N" sort="Hall, Michael N" uniqKey="Hall M" first="Michael N" last="Hall">Michael N. Hall</name><name sortKey="Oppliger, Wolfgang" sort="Oppliger, Wolfgang" uniqKey="Oppliger W" first="Wolfgang" last="Oppliger">Wolfgang Oppliger</name><name sortKey="Stracka, Daniele" sort="Stracka, Daniele" uniqKey="Stracka D" first="Daniele" last="Stracka">Daniele Stracka</name></noCountry><country name="Suisse"><noRegion><name sortKey="Zinzalla, Vittoria" sort="Zinzalla, Vittoria" uniqKey="Zinzalla V" first="Vittoria" last="Zinzalla">Vittoria Zinzalla</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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