Finding new components of the target of rapamycin (TOR) signaling network through chemical genetics and proteome chips.
Identifieur interne : 001899 ( Main/Exploration ); précédent : 001898; suivant : 001900Finding new components of the target of rapamycin (TOR) signaling network through chemical genetics and proteome chips.
Auteurs : Jing Huang [États-Unis] ; Heng Zhu ; Stephen J. Haggarty ; David R. Spring ; Heejun Hwang ; Fulai Jin ; Michael Snyder ; Stuart L. SchreiberSource :
- Proceedings of the National Academy of Sciences of the United States of America [ 0027-8424 ] ; 2004.
Descripteurs français
- KwdFr :
- Analyse par réseau de protéines (MeSH), Cellules Jurkat (MeSH), Humains (MeSH), Modèles biologiques (MeSH), Protein kinases (génétique), Protein kinases (métabolisme), Protéines de Saccharomyces cerevisiae (génétique), Protéines de Saccharomyces cerevisiae (métabolisme), Protéomique (MeSH), Saccharomyces cerevisiae (effets des médicaments et des substances chimiques), Saccharomyces cerevisiae (génétique), Saccharomyces cerevisiae (métabolisme), Sirolimus (pharmacologie), Sérine-thréonine kinases TOR (MeSH), Transduction du signal (MeSH).
- MESH :
- effets des médicaments et des substances chimiques : Saccharomyces cerevisiae.
- génétique : Protein kinases, Protéines de Saccharomyces cerevisiae, Saccharomyces cerevisiae.
- métabolisme : Protein kinases, Protéines de Saccharomyces cerevisiae, Saccharomyces cerevisiae.
- pharmacologie : Sirolimus.
- Analyse par réseau de protéines, Cellules Jurkat, Humains, Modèles biologiques, Protéomique, Sérine-thréonine kinases TOR, Transduction du signal.
English descriptors
- KwdEn :
- Humans (MeSH), Jurkat Cells (MeSH), Models, Biological (MeSH), Protein Array Analysis (MeSH), Protein Kinases (genetics), Protein Kinases (metabolism), Proteomics (MeSH), Saccharomyces cerevisiae (drug effects), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism), Signal Transduction (MeSH), Sirolimus (pharmacology), TOR Serine-Threonine Kinases (MeSH).
- MESH :
- chemical , genetics : Protein Kinases, Saccharomyces cerevisiae Proteins.
- chemical , metabolism : Protein Kinases, Saccharomyces cerevisiae Proteins.
- drug effects : Saccharomyces cerevisiae.
- genetics : Saccharomyces cerevisiae.
- metabolism : Saccharomyces cerevisiae.
- chemical , pharmacology : Sirolimus.
- Humans, Jurkat Cells, Models, Biological, Protein Array Analysis, Proteomics, Signal Transduction, TOR Serine-Threonine Kinases.
Abstract
The TOR (target of rapamycin) proteins play important roles in nutrient signaling in eukaryotic cells. Rapamycin treatment induces a state reminiscent of the nutrient starvation response, often resulting in growth inhibition. Using a chemical genetic modifier screen, we identified two classes of small molecules, small-molecule inhibitors of rapamycin (SMIRs) and small-molecule enhancers of rapamycin (SMERs), that suppress and augment, respectively, rapamycin's effect in the yeast Saccharomyces cerevisiae. Probing proteome chips with biotinylated SMIRs revealed putative intracellular target proteins, including Tep1p, a homolog of the mammalian PTEN (phosphatase and tensin homologue deleted on chromosome 10) tumor suppressor, and Ybr077cp (Nir1p), a protein of previously unknown function that we show to be a component of the TOR signaling network. Both SMIR target proteins are associated with PI(3,4)P2, suggesting a mechanism of regulation of the TOR pathway involving phosphatidylinositides. Our results illustrate the combined use of chemical genetics and proteomics in biological discovery and map a path for creating useful therapeutics for treating human diseases involving the TOR pathway, such as diabetes and cancer.
DOI: 10.1073/pnas.0407117101
PubMed: 15539461
PubMed Central: PMC527135
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Schreiber</name></author></analytic><series><title level="j">Proceedings of the National Academy of Sciences of the United States of America</title><idno type="ISSN">0027-8424</idno><imprint><date when="2004" type="published">2004</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Humans (MeSH)</term><term>Jurkat Cells (MeSH)</term><term>Models, Biological (MeSH)</term><term>Protein Array Analysis (MeSH)</term><term>Protein Kinases (genetics)</term><term>Protein Kinases (metabolism)</term><term>Proteomics (MeSH)</term><term>Saccharomyces cerevisiae (drug effects)</term><term>Saccharomyces cerevisiae (genetics)</term><term>Saccharomyces cerevisiae (metabolism)</term><term>Saccharomyces cerevisiae Proteins (genetics)</term><term>Saccharomyces cerevisiae Proteins (metabolism)</term><term>Signal Transduction (MeSH)</term><term>Sirolimus (pharmacology)</term><term>TOR Serine-Threonine Kinases (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Analyse par réseau de protéines (MeSH)</term><term>Cellules Jurkat (MeSH)</term><term>Humains (MeSH)</term><term>Modèles biologiques (MeSH)</term><term>Protein kinases (génétique)</term><term>Protein kinases (métabolisme)</term><term>Protéines de Saccharomyces cerevisiae (génétique)</term><term>Protéines de Saccharomyces cerevisiae (métabolisme)</term><term>Protéomique (MeSH)</term><term>Saccharomyces cerevisiae (effets des médicaments et des substances chimiques)</term><term>Saccharomyces cerevisiae (génétique)</term><term>Saccharomyces cerevisiae (métabolisme)</term><term>Sirolimus (pharmacologie)</term><term>Sérine-thréonine kinases TOR (MeSH)</term><term>Transduction du signal (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Protein Kinases</term><term>Saccharomyces cerevisiae Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Protein Kinases</term><term>Saccharomyces cerevisiae Proteins</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Protein kinases</term><term>Protéines de Saccharomyces cerevisiae</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Protein kinases</term><term>Protéines de Saccharomyces cerevisiae</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Sirolimus</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Sirolimus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Humans</term><term>Jurkat Cells</term><term>Models, Biological</term><term>Protein Array Analysis</term><term>Proteomics</term><term>Signal Transduction</term><term>TOR Serine-Threonine Kinases</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Analyse par réseau de protéines</term><term>Cellules Jurkat</term><term>Humains</term><term>Modèles biologiques</term><term>Protéomique</term><term>Sérine-thréonine kinases TOR</term><term>Transduction du signal</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The TOR (target of rapamycin) proteins play important roles in nutrient signaling in eukaryotic cells. Rapamycin treatment induces a state reminiscent of the nutrient starvation response, often resulting in growth inhibition. Using a chemical genetic modifier screen, we identified two classes of small molecules, small-molecule inhibitors of rapamycin (SMIRs) and small-molecule enhancers of rapamycin (SMERs), that suppress and augment, respectively, rapamycin's effect in the yeast Saccharomyces cerevisiae. Probing proteome chips with biotinylated SMIRs revealed putative intracellular target proteins, including Tep1p, a homolog of the mammalian PTEN (phosphatase and tensin homologue deleted on chromosome 10) tumor suppressor, and Ybr077cp (Nir1p), a protein of previously unknown function that we show to be a component of the TOR signaling network. Both SMIR target proteins are associated with PI(3,4)P2, suggesting a mechanism of regulation of the TOR pathway involving phosphatidylinositides. Our results illustrate the combined use of chemical genetics and proteomics in biological discovery and map a path for creating useful therapeutics for treating human diseases involving the TOR pathway, such as diabetes and cancer.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15539461</PMID><DateCompleted><Year>2004</Year><Month>12</Month><Day>27</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0027-8424</ISSN><JournalIssue CitedMedium="Print"><Volume>101</Volume><Issue>47</Issue><PubDate><Year>2004</Year><Month>Nov</Month><Day>23</Day></PubDate></JournalIssue><Title>Proceedings of the National Academy of Sciences of the United States of America</Title><ISOAbbreviation>Proc Natl Acad Sci U S A</ISOAbbreviation></Journal><ArticleTitle>Finding new components of the target of rapamycin (TOR) signaling network through chemical genetics and proteome chips.</ArticleTitle><Pagination><MedlinePgn>16594-9</MedlinePgn></Pagination><Abstract><AbstractText>The TOR (target of rapamycin) proteins play important roles in nutrient signaling in eukaryotic cells. Rapamycin treatment induces a state reminiscent of the nutrient starvation response, often resulting in growth inhibition. Using a chemical genetic modifier screen, we identified two classes of small molecules, small-molecule inhibitors of rapamycin (SMIRs) and small-molecule enhancers of rapamycin (SMERs), that suppress and augment, respectively, rapamycin's effect in the yeast Saccharomyces cerevisiae. Probing proteome chips with biotinylated SMIRs revealed putative intracellular target proteins, including Tep1p, a homolog of the mammalian PTEN (phosphatase and tensin homologue deleted on chromosome 10) tumor suppressor, and Ybr077cp (Nir1p), a protein of previously unknown function that we show to be a component of the TOR signaling network. Both SMIR target proteins are associated with PI(3,4)P2, suggesting a mechanism of regulation of the TOR pathway involving phosphatidylinositides. Our results illustrate the combined use of chemical genetics and proteomics in biological discovery and map a path for creating useful therapeutics for treating human diseases involving the TOR pathway, such as diabetes and cancer.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Huang</LastName><ForeName>Jing</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Howard Hughes Medical Institute, Harvard Institute of Chemistry and Cell Biology, and Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA. jinghuang@mednet.ucla.edu</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Zhu</LastName><ForeName>Heng</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Haggarty</LastName><ForeName>Stephen J</ForeName><Initials>SJ</Initials></Author><Author ValidYN="Y"><LastName>Spring</LastName><ForeName>David R</ForeName><Initials>DR</Initials></Author><Author ValidYN="Y"><LastName>Hwang</LastName><ForeName>Heejun</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Jin</LastName><ForeName>Fulai</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Snyder</LastName><ForeName>Michael</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Schreiber</LastName><ForeName>Stuart L</ForeName><Initials>SL</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2004</Year><Month>11</Month><Day>11</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Proc Natl Acad Sci U S 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J" sort="Haggarty, Stephen J" uniqKey="Haggarty S" first="Stephen J" last="Haggarty">Stephen J. Haggarty</name><name sortKey="Hwang, Heejun" sort="Hwang, Heejun" uniqKey="Hwang H" first="Heejun" last="Hwang">Heejun Hwang</name><name sortKey="Jin, Fulai" sort="Jin, Fulai" uniqKey="Jin F" first="Fulai" last="Jin">Fulai Jin</name><name sortKey="Schreiber, Stuart L" sort="Schreiber, Stuart L" uniqKey="Schreiber S" first="Stuart L" last="Schreiber">Stuart L. Schreiber</name><name sortKey="Snyder, Michael" sort="Snyder, Michael" uniqKey="Snyder M" first="Michael" last="Snyder">Michael Snyder</name><name sortKey="Spring, David R" sort="Spring, David R" uniqKey="Spring D" first="David R" last="Spring">David R. Spring</name><name sortKey="Zhu, Heng" sort="Zhu, Heng" uniqKey="Zhu H" first="Heng" last="Zhu">Heng Zhu</name></noCountry><country name="États-Unis"><region name="Massachusetts"><name sortKey="Huang, Jing" sort="Huang, Jing" uniqKey="Huang J" first="Jing" last="Huang">Jing Huang</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:15539461" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a RapamycinFungusV1
| This area was generated with Dilib version V0.6.38. |  |