RapamycinFungusV1, Main, Exploration, bibRecord, 001A55

Protein kinase activity and identification of a toxic effector domain of the target of rapamycin TOR proteins in yeast.

Identifieur interne : 001A55 ( Main/Exploration ); précédent : 001A54; suivant : 001A56

Protein kinase activity and identification of a toxic effector domain of the target of rapamycin TOR proteins in yeast.

Auteurs : C M Alarcon [États-Unis] ; J. Heitman ; M E Cardenas

Source :

Molecular biology of the cell [ 1059-1524 ] ; 1999.

RBID : pubmed:10436010

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence (MeSH), Androstadienes (pharmacology), Antifungal Agents (pharmacology), Base Sequence (MeSH), Carrier Proteins (MeSH), Cell Division (genetics), Drug Resistance, Microbial (MeSH), Enzyme Inhibitors (pharmacology), Fungal Proteins (genetics), Fungal Proteins (metabolism), Fungal Proteins (toxicity), G1 Phase (genetics), Gene Expression Regulation, Fungal (MeSH), Immunophilins (metabolism), Manganese (pharmacology), Molecular Sequence Data (MeSH), Mutation (MeSH), Phosphatidylinositol 3-Kinases (MeSH), Phosphoproteins (metabolism), Phosphorylation (MeSH), Phosphotransferases (Alcohol Group Acceptor) (genetics), Phosphotransferases (Alcohol Group Acceptor) (metabolism), Phosphotransferases (Alcohol Group Acceptor) (toxicity), Protein Kinases (genetics), Protein Kinases (metabolism), Saccharomyces cerevisiae Proteins (MeSH), Sequence Homology, Amino Acid (MeSH), Sirolimus (pharmacology), Tacrolimus Binding Proteins (MeSH), Type C Phospholipases (genetics), Type C Phospholipases (metabolism), Wortmannin (MeSH), Yeasts (drug effects), Yeasts (physiology).
MESH :
- chemical , genetics : Fungal Proteins, Phosphotransferases (Alcohol Group Acceptor), Protein Kinases, Type C Phospholipases.
- chemical , metabolism : Fungal Proteins, Immunophilins, Phosphoproteins, Phosphotransferases (Alcohol Group Acceptor), Protein Kinases, Type C Phospholipases.
- chemical , pharmacology : Androstadienes, Antifungal Agents, Enzyme Inhibitors, Manganese, Sirolimus.
- drug effects : Yeasts.
- genetics : Cell Division, G1 Phase.
- physiology : Yeasts.
- chemical , toxicity : Fungal Proteins, Phosphotransferases (Alcohol Group Acceptor).
- Amino Acid Sequence, Base Sequence, Carrier Proteins, Drug Resistance, Microbial, Gene Expression Regulation, Fungal, Molecular Sequence Data, Mutation, Phosphatidylinositol 3-Kinases, Phosphorylation, Saccharomyces cerevisiae Proteins, Sequence Homology, Amino Acid, Tacrolimus Binding Proteins, Wortmannin.

Abstract

In complex with FKBP12, the immunosuppressant rapamycin binds to and inhibits the yeast TOR1 and TOR2 proteins and the mammalian homologue mTOR/FRAP/RAFT1. The TOR proteins promote cell cycle progression in yeast and human cells by regulating translation and polarization of the actin cytoskeleton. A C-terminal domain of the TOR proteins shares identity with protein and lipid kinases, but only one substrate (PHAS-I), and no regulators of the TOR-signaling cascade have been identified. We report here that yeast TOR1 has an intrinsic protein kinase activity capable of phosphorylating PHAS-1, and this activity is abolished by an active site mutation and inhibited by FKBP12-rapamycin or wortmannin. We find that an intact TOR1 kinase domain is essential for TOR1 functions in yeast. Overexpression of a TOR1 kinase-inactive mutant, or of a central region of the TOR proteins distinct from the FRB and kinase domains, was toxic in yeast, and overexpression of wild-type TOR1 suppressed this toxic effect. Expression of the TOR-toxic domain leads to a G1 cell cycle arrest, consistent with an inhibition of TOR function in translation. Overexpression of the PLC1 gene, which encodes the yeast phospholipase C homologue, suppressed growth inhibition by the TOR-toxic domains. In conclusion, our findings identify a toxic effector domain of the TOR proteins that may interact with substrates or regulators of the TOR kinase cascade and that shares sequence identity with other PIK family members, including ATR, Rad3, Mei-41, and ATM.

DOI: 10.1091/mbc.10.8.2531
PubMed: 10436010
PubMed Central: PMC25485

Affiliations:

États-Unis

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 001A55
to stream Main, to step Curation: 001A55

Le document en format XML

<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Protein kinase activity and identification of a toxic effector domain of the target of rapamycin TOR proteins in yeast.</title>
<author><name sortKey="Alarcon, C M" sort="Alarcon, C M" uniqKey="Alarcon C" first="C M" last="Alarcon">C M Alarcon</name>
<affiliation wicri:level="1"><nlm:affiliation>Department of Genetics, Duke University Medical Center, Durham, North Carolina 27710, USA.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Genetics, Duke University Medical Center, Durham, North Carolina 27710</wicri:regionArea>
<wicri:noRegion>North Carolina 27710</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Heitman, J" sort="Heitman, J" uniqKey="Heitman J" first="J" last="Heitman">J. Heitman</name>
</author>
<author><name sortKey="Cardenas, M E" sort="Cardenas, M E" uniqKey="Cardenas M" first="M E" last="Cardenas">M E Cardenas</name>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="1999">1999</date>
<idno type="RBID">pubmed:10436010</idno>
<idno type="pmid">10436010</idno>
<idno type="pmc">PMC25485</idno>
<idno type="doi">10.1091/mbc.10.8.2531</idno>
<idno type="wicri:Area/Main/Corpus">001A55</idno>
<idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001A55</idno>
<idno type="wicri:Area/Main/Curation">001A55</idno>
<idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">001A55</idno>
<idno type="wicri:Area/Main/Exploration">001A55</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">Protein kinase activity and identification of a toxic effector domain of the target of rapamycin TOR proteins in yeast.</title>
<author><name sortKey="Alarcon, C M" sort="Alarcon, C M" uniqKey="Alarcon C" first="C M" last="Alarcon">C M Alarcon</name>
<affiliation wicri:level="1"><nlm:affiliation>Department of Genetics, Duke University Medical Center, Durham, North Carolina 27710, USA.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Genetics, Duke University Medical Center, Durham, North Carolina 27710</wicri:regionArea>
<wicri:noRegion>North Carolina 27710</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Heitman, J" sort="Heitman, J" uniqKey="Heitman J" first="J" last="Heitman">J. Heitman</name>
</author>
<author><name sortKey="Cardenas, M E" sort="Cardenas, M E" uniqKey="Cardenas M" first="M E" last="Cardenas">M E Cardenas</name>
</author>
</analytic>
<series><title level="j">Molecular biology of the cell</title>
<idno type="ISSN">1059-1524</idno>
<imprint><date when="1999" type="published">1999</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term>
<term>Androstadienes (pharmacology)</term>
<term>Antifungal Agents (pharmacology)</term>
<term>Base Sequence (MeSH)</term>
<term>Carrier Proteins (MeSH)</term>
<term>Cell Division (genetics)</term>
<term>Drug Resistance, Microbial (MeSH)</term>
<term>Enzyme Inhibitors (pharmacology)</term>
<term>Fungal Proteins (genetics)</term>
<term>Fungal Proteins (metabolism)</term>
<term>Fungal Proteins (toxicity)</term>
<term>G1 Phase (genetics)</term>
<term>Gene Expression Regulation, Fungal (MeSH)</term>
<term>Immunophilins (metabolism)</term>
<term>Manganese (pharmacology)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Mutation (MeSH)</term>
<term>Phosphatidylinositol 3-Kinases (MeSH)</term>
<term>Phosphoproteins (metabolism)</term>
<term>Phosphorylation (MeSH)</term>
<term>Phosphotransferases (Alcohol Group Acceptor) (genetics)</term>
<term>Phosphotransferases (Alcohol Group Acceptor) (metabolism)</term>
<term>Phosphotransferases (Alcohol Group Acceptor) (toxicity)</term>
<term>Protein Kinases (genetics)</term>
<term>Protein Kinases (metabolism)</term>
<term>Saccharomyces cerevisiae Proteins (MeSH)</term>
<term>Sequence Homology, Amino Acid (MeSH)</term>
<term>Sirolimus (pharmacology)</term>
<term>Tacrolimus Binding Proteins (MeSH)</term>
<term>Type C Phospholipases (genetics)</term>
<term>Type C Phospholipases (metabolism)</term>
<term>Wortmannin (MeSH)</term>
<term>Yeasts (drug effects)</term>
<term>Yeasts (physiology)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Androstadiènes (pharmacologie)</term>
<term>Antienzymes (pharmacologie)</term>
<term>Antifongiques (pharmacologie)</term>
<term>Division cellulaire (génétique)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Immunophilines (métabolisme)</term>
<term>Levures (effets des médicaments et des substances chimiques)</term>
<term>Levures (physiologie)</term>
<term>Manganèse (pharmacologie)</term>
<term>Mutation (MeSH)</term>
<term>Phase G1 (génétique)</term>
<term>Phosphatidylinositol 3-kinases (MeSH)</term>
<term>Phosphoprotéines (métabolisme)</term>
<term>Phosphorylation (MeSH)</term>
<term>Phosphotransferases (Alcohol Group Acceptor) (génétique)</term>
<term>Phosphotransferases (Alcohol Group Acceptor) (métabolisme)</term>
<term>Phosphotransferases (Alcohol Group Acceptor) (toxicité)</term>
<term>Protein kinases (génétique)</term>
<term>Protein kinases (métabolisme)</term>
<term>Protéines de Saccharomyces cerevisiae (MeSH)</term>
<term>Protéines de liaison au tacrolimus (MeSH)</term>
<term>Protéines de transport (MeSH)</term>
<term>Protéines fongiques (génétique)</term>
<term>Protéines fongiques (métabolisme)</term>
<term>Protéines fongiques (toxicité)</term>
<term>Régulation de l'expression des gènes fongiques (MeSH)</term>
<term>Résistance microbienne aux médicaments (MeSH)</term>
<term>Similitude de séquences d'acides aminés (MeSH)</term>
<term>Sirolimus (pharmacologie)</term>
<term>Séquence d'acides aminés (MeSH)</term>
<term>Séquence nucléotidique (MeSH)</term>
<term>Type C Phospholipases (génétique)</term>
<term>Type C Phospholipases (métabolisme)</term>
<term>Wortmannine (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Fungal Proteins</term>
<term>Phosphotransferases (Alcohol Group Acceptor)</term>
<term>Protein Kinases</term>
<term>Type C Phospholipases</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Fungal Proteins</term>
<term>Immunophilins</term>
<term>Phosphoproteins</term>
<term>Phosphotransferases (Alcohol Group Acceptor)</term>
<term>Protein Kinases</term>
<term>Type C Phospholipases</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Androstadienes</term>
<term>Antifungal Agents</term>
<term>Enzyme Inhibitors</term>
<term>Manganese</term>
<term>Sirolimus</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>Cell Division</term>
<term>G1 Phase</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Division cellulaire</term>
<term>Phase G1</term>
<term>Phosphotransferases (Alcohol Group Acceptor)</term>
<term>Protein kinases</term>
<term>Protéines fongiques</term>
<term>Type C Phospholipases</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Immunophilines</term>
<term>Phosphoprotéines</term>
<term>Phosphotransferases (Alcohol Group Acceptor)</term>
<term>Protein kinases</term>
<term>Protéines fongiques</term>
<term>Type C Phospholipases</term>
</keywords>
<keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Androstadiènes</term>
<term>Antienzymes</term>
<term>Antifongiques</term>
<term>Manganèse</term>
<term>Sirolimus</term>
</keywords>
<keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Levures</term>
</keywords>
<keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Yeasts</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="toxicity" xml:lang="en"><term>Fungal Proteins</term>
<term>Phosphotransferases (Alcohol Group Acceptor)</term>
</keywords>
<keywords scheme="MESH" qualifier="toxicité" xml:lang="fr"><term>Phosphotransferases (Alcohol Group Acceptor)</term>
<term>Protéines fongiques</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Base Sequence</term>
<term>Carrier Proteins</term>
<term>Drug Resistance, Microbial</term>
<term>Gene Expression Regulation, Fungal</term>
<term>Molecular Sequence Data</term>
<term>Mutation</term>
<term>Phosphatidylinositol 3-Kinases</term>
<term>Phosphorylation</term>
<term>Saccharomyces cerevisiae Proteins</term>
<term>Sequence Homology, Amino Acid</term>
<term>Tacrolimus Binding Proteins</term>
<term>Wortmannin</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Données de séquences moléculaires</term>
<term>Mutation</term>
<term>Phosphatidylinositol 3-kinases</term>
<term>Phosphorylation</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Protéines de liaison au tacrolimus</term>
<term>Protéines de transport</term>
<term>Régulation de l'expression des gènes fongiques</term>
<term>Résistance microbienne aux médicaments</term>
<term>Similitude de séquences d'acides aminés</term>
<term>Séquence d'acides aminés</term>
<term>Séquence nucléotidique</term>
<term>Wortmannine</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">In complex with FKBP12, the immunosuppressant rapamycin binds to and inhibits the yeast TOR1 and TOR2 proteins and the mammalian homologue mTOR/FRAP/RAFT1. The TOR proteins promote cell cycle progression in yeast and human cells by regulating translation and polarization of the actin cytoskeleton. A C-terminal domain of the TOR proteins shares identity with protein and lipid kinases, but only one substrate (PHAS-I), and no regulators of the TOR-signaling cascade have been identified. We report here that yeast TOR1 has an intrinsic protein kinase activity capable of phosphorylating PHAS-1, and this activity is abolished by an active site mutation and inhibited by FKBP12-rapamycin or wortmannin. We find that an intact TOR1 kinase domain is essential for TOR1 functions in yeast. Overexpression of a TOR1 kinase-inactive mutant, or of a central region of the TOR proteins distinct from the FRB and kinase domains, was toxic in yeast, and overexpression of wild-type TOR1 suppressed this toxic effect. Expression of the TOR-toxic domain leads to a G1 cell cycle arrest, consistent with an inhibition of TOR function in translation. Overexpression of the PLC1 gene, which encodes the yeast phospholipase C homologue, suppressed growth inhibition by the TOR-toxic domains. In conclusion, our findings identify a toxic effector domain of the TOR proteins that may interact with substrates or regulators of the TOR kinase cascade and that shares sequence identity with other PIK family members, including ATR, Rad3, Mei-41, and ATM.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">10436010</PMID>
<DateCompleted><Year>1999</Year>
<Month>10</Month>
<Day>12</Day>
</DateCompleted>
<DateRevised><Year>2018</Year>
<Month>12</Month>
<Day>01</Day>
</DateRevised>
<Article PubModel="Print"><Journal><ISSN IssnType="Print">1059-1524</ISSN>
<JournalIssue CitedMedium="Print"><Volume>10</Volume>
<Issue>8</Issue>
<PubDate><Year>1999</Year>
<Month>Aug</Month>
</PubDate>
</JournalIssue>
<Title>Molecular biology of the cell</Title>
<ISOAbbreviation>Mol Biol Cell</ISOAbbreviation>
</Journal>
<ArticleTitle>Protein kinase activity and identification of a toxic effector domain of the target of rapamycin TOR proteins in yeast.</ArticleTitle>
<Pagination><MedlinePgn>2531-46</MedlinePgn>
</Pagination>
<Abstract><AbstractText>In complex with FKBP12, the immunosuppressant rapamycin binds to and inhibits the yeast TOR1 and TOR2 proteins and the mammalian homologue mTOR/FRAP/RAFT1. The TOR proteins promote cell cycle progression in yeast and human cells by regulating translation and polarization of the actin cytoskeleton. A C-terminal domain of the TOR proteins shares identity with protein and lipid kinases, but only one substrate (PHAS-I), and no regulators of the TOR-signaling cascade have been identified. We report here that yeast TOR1 has an intrinsic protein kinase activity capable of phosphorylating PHAS-1, and this activity is abolished by an active site mutation and inhibited by FKBP12-rapamycin or wortmannin. We find that an intact TOR1 kinase domain is essential for TOR1 functions in yeast. Overexpression of a TOR1 kinase-inactive mutant, or of a central region of the TOR proteins distinct from the FRB and kinase domains, was toxic in yeast, and overexpression of wild-type TOR1 suppressed this toxic effect. Expression of the TOR-toxic domain leads to a G1 cell cycle arrest, consistent with an inhibition of TOR function in translation. Overexpression of the PLC1 gene, which encodes the yeast phospholipase C homologue, suppressed growth inhibition by the TOR-toxic domains. In conclusion, our findings identify a toxic effector domain of the TOR proteins that may interact with substrates or regulators of the TOR kinase cascade and that shares sequence identity with other PIK family members, including ATR, Rad3, Mei-41, and ATM.</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>Heitman</LastName>
<ForeName>J</ForeName>
<Initials>J</Initials>
</Author>
<Author ValidYN="Y"><LastName>Cardenas</LastName>
<ForeName>M E</ForeName>
<Initials>ME</Initials>
</Author>
</AuthorList>
<Language>eng</Language>
<GrantList CompleteYN="Y"><Grant><GrantID>AI-41937</GrantID>
<Acronym>AI</Acronym>
<Agency>NIAID NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>CA-77075</GrantID>
<Acronym>CA</Acronym>
<Agency>NCI 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>Mol Biol Cell</MedlineTA>
<NlmUniqueID>9201390</NlmUniqueID>
<ISSNLinking>1059-1524</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D000730">Androstadienes</NameOfSubstance>
</Chemical>
<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="D004791">Enzyme Inhibitors</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D010750">Phosphoproteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>42Z2K6ZL8P</RegistryNumber>
<NameOfSubstance UI="D008345">Manganese</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 2.7.-</RegistryNumber>
<NameOfSubstance UI="D011494">Protein Kinases</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 3.1.4.-</RegistryNumber>
<NameOfSubstance UI="D010738">Type C Phospholipases</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 5.2.1.-</RegistryNumber>
<NameOfSubstance UI="D022021">Tacrolimus Binding Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 5.2.1.8</RegistryNumber>
<NameOfSubstance UI="D020104">Immunophilins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>W36ZG6FT64</RegistryNumber>
<NameOfSubstance UI="D020123">Sirolimus</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>XVA4O219QW</RegistryNumber>
<NameOfSubstance UI="D000077191">Wortmannin</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000730" MajorTopicYN="N">Androstadienes</DescriptorName>
<QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName>
</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="Y">Carrier Proteins</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002455" MajorTopicYN="N">Cell Division</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004352" MajorTopicYN="N">Drug Resistance, Microbial</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004791" MajorTopicYN="N">Enzyme Inhibitors</DescriptorName>
<QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
<QualifierName UI="Q000633" MajorTopicYN="N">toxicity</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D016193" MajorTopicYN="N">G1 Phase</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D015966" MajorTopicYN="N">Gene Expression Regulation, Fungal</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D020104" MajorTopicYN="N">Immunophilins</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008345" MajorTopicYN="N">Manganese</DescriptorName>
<QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D019869" MajorTopicYN="Y">Phosphatidylinositol 3-Kinases</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010750" MajorTopicYN="N">Phosphoproteins</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010766" MajorTopicYN="N">Phosphorylation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D017853" MajorTopicYN="N">Phosphotransferases (Alcohol Group Acceptor)</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
<QualifierName UI="Q000633" MajorTopicYN="N">toxicity</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011494" MajorTopicYN="N">Protein Kinases</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D029701" MajorTopicYN="Y">Saccharomyces cerevisiae Proteins</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D020123" MajorTopicYN="N">Sirolimus</DescriptorName>
<QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D022021" MajorTopicYN="N">Tacrolimus Binding Proteins</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010738" MajorTopicYN="N">Type C Phospholipases</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000077191" MajorTopicYN="N">Wortmannin</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D015003" MajorTopicYN="N">Yeasts</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
<QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName>
</MeshHeading>
</MeshHeadingList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1999</Year>
<Month>8</Month>
<Day>6</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>1999</Year>
<Month>8</Month>
<Day>6</Day>
<Hour>0</Hour>
<Minute>1</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>1999</Year>
<Month>8</Month>
<Day>6</Day>
<Hour>0</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">10436010</ArticleId>
<ArticleId IdType="pmc">PMC25485</ArticleId>
<ArticleId IdType="doi">10.1091/mbc.10.8.2531</ArticleId>
</ArticleIdList>
<ReferenceList><Reference><Citation>Genes Dev. 1996 Feb 1;10(3):279-88</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8595879</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Cell Biol. 1993 Oct;13(10):6012-23</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8413204</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Science. 1996 Jul 12;273(5272):239-42</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8662507</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell. 1996 Jul 12;86(1):159-71</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8689683</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Genes Dev. 1996 Aug 1;10(15):1904-16</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8756348</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell. 1996 Aug 23;86(4):517-20</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8752206</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Biol Cell. 1996 Jan;7(1):25-42</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8741837</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Genes Dev. 1996 Oct 1;10(19):2401-10</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8843193</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Genes Dev. 1996 Oct 1;10(19):2411-22</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8843194</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>EMBO J. 1996 Oct 1;15(19):5256-67</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8895571</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 1996 Nov 26;93(24):13780-5</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8943012</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell. 1997 Feb 21;88(4):531-42</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9038344</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Cell Biol. 1997 Apr;17(4):2020-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9121450</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 1997 Apr 1;94(7):3070-5</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9096347</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Science. 1997 Jul 4;277(5322):99-101</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9204908</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Trends Biochem Sci. 1997 Sep;22(9):345-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9301335</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1994 Jan 14;269(2):1166-72</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8288577</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>EMBO J. 1994 Feb 1;13(3):522-33</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8313897</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Gen Genet. 1994 Mar;242(6):631-40</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8152413</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Biol Cell. 1994 Jan;5(1):105-18</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8186460</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 1994 Jun 30;369(6483):756-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8008069</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell. 1994 Jul 15;78(1):35-43</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7518356</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1994 Dec 23;269(51):32027-30</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7528205</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 1994 Dec 20;91(26):12574-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7809080</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>EMBO J. 1994 Dec 15;13(24):5944-57</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7529175</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1995 Jan 13;270(2):815-22</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7822316</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Yeast. 1994 Dec;10(13):1793-808</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7747518</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 1995 May 23;92(11):4947-51</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7539137</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell. 1995 Jul 14;82(1):121-30</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7606777</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1995 Aug 4;270(31):18531-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7629182</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 1995 Aug 1;92(16):7222-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7638171</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1995 Sep 8;270(36):20875-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7673106</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 1995 Oct 5;377(6548):441-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7566123</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1995 Nov 17;270(46):27531-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7499212</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>EMBO J. 1995 Dec 1;14(23):5892-907</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8846782</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Bacteriol. 1997 Oct;179(20):6325-34</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9335279</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1997 Oct 17;272(42):26457-63</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9334222</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1997 Oct 31;272(44):27671-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9346907</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>EMBO J. 1998 Jan 2;17(1):159-69</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9427750</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochem Biophys Res Commun. 1997 Dec 29;241(3):704-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9434772</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1998 Feb 13;273(7):3963-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9461583</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 1998 Feb 17;95(4):1432-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9465032</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Genetics. 1998 Jan;148(1):33-47</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9475719</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Genetics. 1998 Jan;148(1):99-112</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9475724</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Genes Dev. 1998 Feb 15;12(4):502-13</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9472019</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 1981 Oct;78(10):6354-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">6273866</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Genetics. 1987 Aug;116(4):541-5</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3305158</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Gene. 1989 Apr 15;77(1):51-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2744487</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Cell Biol. 1991 Mar;11(3):1718-23</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1996117</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Methods Enzymol. 1991;194:3-21</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2005794</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Science. 1991 Aug 23;253(5022):905-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1715094</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Immunol Today. 1992 Apr;13(4):136-42</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1374612</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>New Biol. 1992 May;4(5):448-60</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1515410</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Science. 1993 Apr 2;260(5104):88-91</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8385367</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Trends Biochem Sci. 1993 Mar;18(3):84-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8480367</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell. 1993 May 7;73(3):585-96</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8387896</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Cell Biol. 1993 Sep;13(9):5861-76</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8395015</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 1996 Apr 30;93(9):4076-80</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8633019</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
</PubmedData>
</pubmed>
<affiliations><list><country><li>États-Unis</li>
</country>
</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"><noRegion><name sortKey="Alarcon, C M" sort="Alarcon, C M" uniqKey="Alarcon C" first="C M" last="Alarcon">C M Alarcon</name>
</noRegion>
</country>
</tree>
</affiliations>
</record>

Pour manipuler ce document sous Unix (Dilib)

EXPLOR_STEP=$WICRI_ROOT/Bois/explor/RapamycinFungusV1/Data/Main/Exploration

HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 001A55 | SxmlIndent | more

HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 001A55 | SxmlIndent | more

Pour mettre un lien sur cette page dans le réseau Wicri

{{Explor lien
   |wiki=    Bois
   |area=    RapamycinFungusV1
   |flux=    Main
   |étape=   Exploration
   |type=    RBID
   |clé=     pubmed:10436010
   |texte=   Protein kinase activity and identification of a toxic effector domain of the target of rapamycin TOR proteins in yeast.
}}

Pour générer des pages wiki

HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i   -Sk "pubmed:10436010" \
       | HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd   \
       | NlmPubMed2Wicri -a RapamycinFungusV1

This area was generated with Dilib version V0.6.38.
Data generation: Thu Nov 19 21:55:41 2020. Site generation: Thu Nov 19 22:00:39 2020

	Serveur d'exploration sur la rapamycine et les champignons
	Attention, ce site est en cours de développement ! Attention, site généré par des moyens informatiques à partir de corpus bruts. Les informations ne sont donc pas validées.

Serveur d'exploration sur la rapamycine et les champignons

Protein kinase activity and identification of a toxic effector domain of the target of rapamycin TOR proteins in yeast.

Protein kinase activity and identification of a toxic effector domain of the target of rapamycin TOR proteins in yeast.

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki