Mammalian RAFT1 kinase domain provides rapamycin-sensitive TOR function in yeast.
Identifieur interne : 001A98 ( Main/Exploration ); précédent : 001A97; suivant : 001A99Mammalian RAFT1 kinase domain provides rapamycin-sensitive TOR function in yeast.
Auteurs : C M Alarcon [États-Unis] ; M E Cardenas ; J. HeitmanSource :
- Genes & development [ 0890-9369 ] ; 1996.
Descripteurs français
- KwdFr :
- 1-Phosphatidylinositol 4-kinase (MeSH), ARN fongique (analyse), ARN messager (analyse), Animaux (MeSH), Antifongiques (pharmacologie), Données de séquences moléculaires (MeSH), Levures (effets des médicaments et des substances chimiques), Levures (génétique), Mammifères (MeSH), Membrane cellulaire (composition chimique), Phosphatidylinositol 3-kinases (MeSH), Phosphotransferases (Alcohol Group Acceptor) (génétique), Phosphotransferases (Alcohol Group Acceptor) (physiologie), Polyènes (pharmacologie), Protéines de Saccharomyces cerevisiae (MeSH), Protéines de fusion recombinantes (MeSH), Protéines de transport (analyse), Protéines de transport (génétique), Protéines de transport (physiologie), Protéines du cycle cellulaire (MeSH), Protéines fongiques (physiologie), Résistance microbienne aux médicaments (MeSH), Sirolimus (MeSH), Séquence nucléotidique (MeSH), Test de complémentation (MeSH), Vacuoles (composition chimique).
- MESH :
- analyse : ARN fongique, ARN messager, Protéines de transport.
- composition chimique : Membrane cellulaire, Vacuoles.
- effets des médicaments et des substances chimiques : Levures.
- génétique : Levures, Phosphotransferases (Alcohol Group Acceptor), Protéines de transport.
- pharmacologie : Antifongiques, Polyènes.
- physiologie : Phosphotransferases (Alcohol Group Acceptor), Protéines de transport, Protéines fongiques.
- 1-Phosphatidylinositol 4-kinase, Animaux, Données de séquences moléculaires, Mammifères, Phosphatidylinositol 3-kinases, Protéines de Saccharomyces cerevisiae, Protéines de fusion recombinantes, Protéines du cycle cellulaire, Résistance microbienne aux médicaments, Sirolimus, Séquence nucléotidique, Test de complémentation.
English descriptors
- KwdEn :
- 1-Phosphatidylinositol 4-Kinase (MeSH), Animals (MeSH), Antifungal Agents (pharmacology), Base Sequence (MeSH), Carrier Proteins (analysis), Carrier Proteins (genetics), Carrier Proteins (physiology), Cell Cycle Proteins (MeSH), Cell Membrane (chemistry), Drug Resistance, Microbial (MeSH), Fungal Proteins (physiology), Genetic Complementation Test (MeSH), Mammals (MeSH), Molecular Sequence Data (MeSH), Phosphatidylinositol 3-Kinases (MeSH), Phosphotransferases (Alcohol Group Acceptor) (genetics), Phosphotransferases (Alcohol Group Acceptor) (physiology), Polyenes (pharmacology), RNA, Fungal (analysis), RNA, Messenger (analysis), Recombinant Fusion Proteins (MeSH), Saccharomyces cerevisiae Proteins (MeSH), Sirolimus (MeSH), Vacuoles (chemistry), Yeasts (drug effects), Yeasts (genetics).
- MESH :
- chemical , analysis : Carrier Proteins, RNA, Fungal, RNA, Messenger.
- chemical , genetics : Carrier Proteins, Phosphotransferases (Alcohol Group Acceptor).
- chemical , pharmacology : Antifungal Agents, Polyenes.
- chemical , physiology : Carrier Proteins, Fungal Proteins, Phosphotransferases (Alcohol Group Acceptor).
- chemical : 1-Phosphatidylinositol 4-Kinase, Cell Cycle Proteins, Phosphatidylinositol 3-Kinases, Recombinant Fusion Proteins, Saccharomyces cerevisiae Proteins, Sirolimus.
- chemistry : Cell Membrane, Vacuoles.
- drug effects : Yeasts.
- genetics : Yeasts.
- Animals, Base Sequence, Drug Resistance, Microbial, Genetic Complementation Test, Mammals, Molecular Sequence Data.
Abstract
In complex with the prolyl isomerase FKBP12, the natural product rapamycin blocks signal transduction in organisms as diverse as yeast and man. The yeast targets of FKBP12-rapamycin, TOR1 and TOR2, are large proteins with homology to lipid and protein kinases. A mammalian FKBP12-rapamycin binding protein, RAFT1, shares 39% and 43% identity with TOR1 and TOR2 proteins, respectively but has not been linked to rapamycin action in vivo. We find that when expressed in yeast, neither wild-type nor mutant RAFT1 complemented tor mutations or conferred rapamycin resistance. In contrast, TOR1-RAFT1 and TOR1-RAFT1 hybrid proteins containing the carboxy-terminal RAFT1 kinase domain complemented tor2 and tor1 mutant strains, respectively. Moreover, TOR2-RAFT1 and TOR1-RAFT1 hybrid proteins mutated at the position corresponding to rapamycin-resistant TOR mutants (S20351) conferred rapamycin resistance. Like the TOR2 protein, the TOR2-RAFT1 proteins were stably expressed, localized to the vacuolar surface, and associated with a phosphatidylinositol-4 kinase activity. These findings directly link the mammalian TOR homolog RAFT1 to rapamycin action in vivo and indicate that the TOR/RAFT1 kinase domain has been functionally conserved from yeast to man.
DOI: 10.1101/gad.10.3.279
PubMed: 8595879
Affiliations:
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Le document en format XML
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(Alcohol Group Acceptor) (physiology)</term><term>Polyenes (pharmacology)</term><term>RNA, Fungal (analysis)</term><term>RNA, Messenger (analysis)</term><term>Recombinant Fusion Proteins (MeSH)</term><term>Saccharomyces cerevisiae Proteins (MeSH)</term><term>Sirolimus (MeSH)</term><term>Vacuoles (chemistry)</term><term>Yeasts (drug effects)</term><term>Yeasts (genetics)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>1-Phosphatidylinositol 4-kinase (MeSH)</term><term>ARN fongique (analyse)</term><term>ARN messager (analyse)</term><term>Animaux (MeSH)</term><term>Antifongiques (pharmacologie)</term><term>Données de séquences moléculaires (MeSH)</term><term>Levures (effets des médicaments et des substances chimiques)</term><term>Levures (génétique)</term><term>Mammifères (MeSH)</term><term>Membrane cellulaire (composition chimique)</term><term>Phosphatidylinositol 3-kinases (MeSH)</term><term>Phosphotransferases (Alcohol Group Acceptor) (génétique)</term><term>Phosphotransferases (Alcohol Group Acceptor) (physiologie)</term><term>Polyènes (pharmacologie)</term><term>Protéines de Saccharomyces cerevisiae (MeSH)</term><term>Protéines de fusion recombinantes (MeSH)</term><term>Protéines de transport (analyse)</term><term>Protéines de transport (génétique)</term><term>Protéines de transport (physiologie)</term><term>Protéines du cycle cellulaire (MeSH)</term><term>Protéines fongiques (physiologie)</term><term>Résistance microbienne aux médicaments (MeSH)</term><term>Sirolimus (MeSH)</term><term>Séquence nucléotidique (MeSH)</term><term>Test de complémentation (MeSH)</term><term>Vacuoles (composition chimique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Carrier Proteins</term><term>RNA, Fungal</term><term>RNA, Messenger</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Carrier Proteins</term><term>Phosphotransferases (Alcohol Group Acceptor)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Antifungal Agents</term><term>Polyenes</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Carrier Proteins</term><term>Fungal Proteins</term><term>Phosphotransferases (Alcohol Group Acceptor)</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>1-Phosphatidylinositol 4-Kinase</term><term>Cell Cycle Proteins</term><term>Phosphatidylinositol 3-Kinases</term><term>Recombinant Fusion Proteins</term><term>Saccharomyces cerevisiae Proteins</term><term>Sirolimus</term></keywords><keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>ARN fongique</term><term>ARN messager</term><term>Protéines de transport</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Cell Membrane</term><term>Vacuoles</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Membrane cellulaire</term><term>Vacuoles</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Yeasts</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Levures</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Yeasts</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Levures</term><term>Phosphotransferases (Alcohol Group Acceptor)</term><term>Protéines de transport</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Antifongiques</term><term>Polyènes</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Phosphotransferases (Alcohol Group Acceptor)</term><term>Protéines de transport</term><term>Protéines fongiques</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Base Sequence</term><term>Drug Resistance, Microbial</term><term>Genetic Complementation Test</term><term>Mammals</term><term>Molecular Sequence Data</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>1-Phosphatidylinositol 4-kinase</term><term>Animaux</term><term>Données de séquences moléculaires</term><term>Mammifères</term><term>Phosphatidylinositol 3-kinases</term><term>Protéines de Saccharomyces cerevisiae</term><term>Protéines de fusion recombinantes</term><term>Protéines du cycle cellulaire</term><term>Résistance microbienne aux médicaments</term><term>Sirolimus</term><term>Séquence nucléotidique</term><term>Test de complémentation</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">In complex with the prolyl isomerase FKBP12, the natural product rapamycin blocks signal transduction in organisms as diverse as yeast and man. The yeast targets of FKBP12-rapamycin, TOR1 and TOR2, are large proteins with homology to lipid and protein kinases. A mammalian FKBP12-rapamycin binding protein, RAFT1, shares 39% and 43% identity with TOR1 and TOR2 proteins, respectively but has not been linked to rapamycin action in vivo. We find that when expressed in yeast, neither wild-type nor mutant RAFT1 complemented tor mutations or conferred rapamycin resistance. In contrast, TOR1-RAFT1 and TOR1-RAFT1 hybrid proteins containing the carboxy-terminal RAFT1 kinase domain complemented tor2 and tor1 mutant strains, respectively. Moreover, TOR2-RAFT1 and TOR1-RAFT1 hybrid proteins mutated at the position corresponding to rapamycin-resistant TOR mutants (S20351) conferred rapamycin resistance. Like the TOR2 protein, the TOR2-RAFT1 proteins were stably expressed, localized to the vacuolar surface, and associated with a phosphatidylinositol-4 kinase activity. These findings directly link the mammalian TOR homolog RAFT1 to rapamycin action in vivo and indicate that the TOR/RAFT1 kinase domain has been functionally conserved from yeast to man.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">8595879</PMID><DateCompleted><Year>1996</Year><Month>04</Month><Day>16</Day></DateCompleted><DateRevised><Year>2019</Year><Month>05</Month><Day>16</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0890-9369</ISSN><JournalIssue CitedMedium="Print"><Volume>10</Volume><Issue>3</Issue><PubDate><Year>1996</Year><Month>Feb</Month><Day>01</Day></PubDate></JournalIssue><Title>Genes & development</Title><ISOAbbreviation>Genes Dev</ISOAbbreviation></Journal><ArticleTitle>Mammalian RAFT1 kinase domain provides rapamycin-sensitive TOR function in yeast.</ArticleTitle><Pagination><MedlinePgn>279-88</MedlinePgn></Pagination><Abstract><AbstractText>In complex with the prolyl isomerase FKBP12, the natural product rapamycin blocks signal transduction in organisms as diverse as yeast and man. The yeast targets of FKBP12-rapamycin, TOR1 and TOR2, are large proteins with homology to lipid and protein kinases. A mammalian FKBP12-rapamycin binding protein, RAFT1, shares 39% and 43% identity with TOR1 and TOR2 proteins, respectively but has not been linked to rapamycin action in vivo. We find that when expressed in yeast, neither wild-type nor mutant RAFT1 complemented tor mutations or conferred rapamycin resistance. In contrast, TOR1-RAFT1 and TOR1-RAFT1 hybrid proteins containing the carboxy-terminal RAFT1 kinase domain complemented tor2 and tor1 mutant strains, respectively. Moreover, TOR2-RAFT1 and TOR1-RAFT1 hybrid proteins mutated at the position corresponding to rapamycin-resistant TOR mutants (S20351) conferred rapamycin resistance. Like the TOR2 protein, the TOR2-RAFT1 proteins were stably expressed, localized to the vacuolar surface, and associated with a phosphatidylinositol-4 kinase activity. These findings directly link the mammalian TOR homolog RAFT1 to rapamycin action in vivo and indicate that the TOR/RAFT1 kinase domain has been functionally conserved from yeast to man.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Alarcon</LastName><ForeName>C M</ForeName><Initials>CM</Initials><AffiliationInfo><Affiliation>Department of Genetics, Duke University Medical Center, Durham, North Carolina 27710 USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cardenas</LastName><ForeName>M E</ForeName><Initials>ME</Initials></Author><Author ValidYN="Y"><LastName>Heitman</LastName><ForeName>J</ForeName><Initials>J</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>P01 HL50985-1</GrantID><Acronym>HL</Acronym><Agency>NHLBI NIH HHS</Agency><Country>United States</Country></Grant></GrantList><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></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Genes Dev</MedlineTA><NlmUniqueID>8711660</NlmUniqueID><ISSNLinking>0890-9369</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000935">Antifungal Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002352">Carrier Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018797">Cell Cycle Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011090">Polyenes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D012331">RNA, Fungal</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D012333">RNA, Messenger</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011993">Recombinant Fusion Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.1.-</RegistryNumber><NameOfSubstance UI="D019869">Phosphatidylinositol 3-Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.1.-</RegistryNumber><NameOfSubstance UI="D017853">Phosphotransferases (Alcohol Group Acceptor)</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.1.137</RegistryNumber><NameOfSubstance UI="C083324">TOR1 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.1.67</RegistryNumber><NameOfSubstance UI="D019870">1-Phosphatidylinositol 4-Kinase</NameOfSubstance></Chemical><Chemical><RegistryNumber>W36ZG6FT64</RegistryNumber><NameOfSubstance UI="D020123">Sirolimus</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D019870" MajorTopicYN="N">1-Phosphatidylinositol 4-Kinase</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000935" MajorTopicYN="N">Antifungal Agents</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001483" MajorTopicYN="N">Base Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002352" MajorTopicYN="N">Carrier Proteins</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018797" MajorTopicYN="N">Cell Cycle Proteins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002462" MajorTopicYN="N">Cell Membrane</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004352" MajorTopicYN="N">Drug Resistance, Microbial</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005816" MajorTopicYN="N">Genetic Complementation Test</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008322" MajorTopicYN="N">Mammals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019869" MajorTopicYN="Y">Phosphatidylinositol 3-Kinases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017853" MajorTopicYN="N">Phosphotransferases (Alcohol Group Acceptor)</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011090" MajorTopicYN="N">Polyenes</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012331" MajorTopicYN="N">RNA, Fungal</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012333" MajorTopicYN="N">RNA, Messenger</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011993" MajorTopicYN="N">Recombinant Fusion Proteins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D029701" MajorTopicYN="Y">Saccharomyces cerevisiae Proteins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020123" MajorTopicYN="N">Sirolimus</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014617" MajorTopicYN="N">Vacuoles</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015003" MajorTopicYN="N">Yeasts</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1996</Year><Month>2</Month><Day>1</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1996</Year><Month>2</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1996</Year><Month>2</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">8595879</ArticleId><ArticleId IdType="doi">10.1101/gad.10.3.279</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Caroline du Nord</li></region></list><tree><noCountry><name sortKey="Cardenas, M E" sort="Cardenas, M E" uniqKey="Cardenas M" first="M E" last="Cardenas">M E Cardenas</name><name sortKey="Heitman, J" sort="Heitman, J" uniqKey="Heitman J" first="J" last="Heitman">J. Heitman</name></noCountry><country name="États-Unis"><region name="Caroline du Nord"><name sortKey="Alarcon, C M" sort="Alarcon, C M" uniqKey="Alarcon C" first="C M" last="Alarcon">C M Alarcon</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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