TOR kinase homologs function in a signal transduction pathway that is conserved from yeast to mammals.
Identifieur interne : 001A49 ( Main/Exploration ); précédent : 001A48; suivant : 001A50TOR kinase homologs function in a signal transduction pathway that is conserved from yeast to mammals.
Auteurs : N S Cutler [États-Unis] ; J. Heitman ; M E CardenasSource :
- Molecular and cellular endocrinology [ 0303-7207 ] ; 1999.
Descripteurs français
- KwdFr :
- ARN messager (génétique), Animaux (MeSH), Humains (MeSH), Immunophilines (génétique), Immunophilines (métabolisme), Initiation de la traduction (effets des médicaments et des substances chimiques), Mammifères (MeSH), Peptidylpropyl isomerase (génétique), Peptidylpropyl isomerase (métabolisme), Protéines de Drosophila (MeSH), Protéines de liaison au tacrolimus (MeSH), Récepteurs à activité tyrosine kinase (génétique), Récepteurs à activité tyrosine kinase (métabolisme), Saccharomyces cerevisiae (effets des médicaments et des substances chimiques), Saccharomyces cerevisiae (enzymologie), Saccharomyces cerevisiae (génétique), Sirolimus (pharmacologie), Transduction du signal (MeSH).
- MESH :
- effets des médicaments et des substances chimiques : Initiation de la traduction, Saccharomyces cerevisiae.
- enzymologie : Saccharomyces cerevisiae.
- génétique : ARN messager, Immunophilines, Peptidylpropyl isomerase, Récepteurs à activité tyrosine kinase, Saccharomyces cerevisiae.
- métabolisme : Immunophilines, Peptidylpropyl isomerase, Récepteurs à activité tyrosine kinase.
- pharmacologie : Sirolimus.
- Animaux, Humains, Mammifères, Protéines de Drosophila, Protéines de liaison au tacrolimus, Transduction du signal.
English descriptors
- KwdEn :
- Animals (MeSH), Drosophila Proteins (MeSH), Humans (MeSH), Immunophilins (genetics), Immunophilins (metabolism), Mammals (MeSH), Peptide Chain Initiation, Translational (drug effects), Peptidylprolyl Isomerase (genetics), Peptidylprolyl Isomerase (metabolism), RNA, Messenger (genetics), Receptor Protein-Tyrosine Kinases (genetics), Receptor Protein-Tyrosine Kinases (metabolism), Saccharomyces cerevisiae (drug effects), Saccharomyces cerevisiae (enzymology), Saccharomyces cerevisiae (genetics), Signal Transduction (MeSH), Sirolimus (pharmacology), Tacrolimus Binding Proteins (MeSH).
- MESH :
- chemical , genetics : Immunophilins, Peptidylprolyl Isomerase, RNA, Messenger, Receptor Protein-Tyrosine Kinases.
- chemical , metabolism : Immunophilins, Peptidylprolyl Isomerase, Receptor Protein-Tyrosine Kinases.
- chemical , pharmacology : Sirolimus.
- chemical : Drosophila Proteins, Tacrolimus Binding Proteins.
- drug effects : Peptide Chain Initiation, Translational, Saccharomyces cerevisiae.
- enzymology : Saccharomyces cerevisiae.
- genetics : Saccharomyces cerevisiae.
- Animals, Humans, Mammals, Signal Transduction.
Abstract
Rapamycin is a natural product with potent antifungal and immunosuppressive activities. Rapamycin binds to the FKBP12 prolyl isomerase, and the resulting protein-drug complex inhibits the TOR kinase homologs. Both the FKBP12 and the TOR proteins are highly conserved from yeast to man, and genetic and biochemical studies reveal that these proteins are the targets of rapamycin in vivo. Treatment of yeast or mammalian cells with rapamycin inhibits translational initiation of a subset of mRNAs and dramatically represses ribosomal mRNA and tRNA transcription. Furthermore, rapamycin exposure blocks cell cycle progression in the early G1 phase of the cell cycle, driving cells into a G0 state and, ultimately, triggering autophagy. Recent findings reveal that the upstream factors regulating the TOR signaling cascade are involved in detecting amino acids, nutrients, or growth factors. These findings indicate that the TOR proteins function in a signal transduction pathway that coordinates nutritional and mitogenic signals to control protein biosynthesis and degradation.
DOI: 10.1016/s0303-7207(99)00121-5
PubMed: 10580846
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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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 and cellular endocrinology</title><idno type="ISSN">0303-7207</idno><imprint><date when="1999" type="published">1999</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Drosophila Proteins (MeSH)</term><term>Humans (MeSH)</term><term>Immunophilins (genetics)</term><term>Immunophilins (metabolism)</term><term>Mammals (MeSH)</term><term>Peptide Chain Initiation, Translational (drug effects)</term><term>Peptidylprolyl Isomerase (genetics)</term><term>Peptidylprolyl Isomerase (metabolism)</term><term>RNA, Messenger (genetics)</term><term>Receptor Protein-Tyrosine Kinases (genetics)</term><term>Receptor Protein-Tyrosine Kinases (metabolism)</term><term>Saccharomyces cerevisiae (drug effects)</term><term>Saccharomyces cerevisiae (enzymology)</term><term>Saccharomyces cerevisiae (genetics)</term><term>Signal Transduction (MeSH)</term><term>Sirolimus (pharmacology)</term><term>Tacrolimus Binding Proteins (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ARN messager (génétique)</term><term>Animaux (MeSH)</term><term>Humains (MeSH)</term><term>Immunophilines (génétique)</term><term>Immunophilines (métabolisme)</term><term>Initiation de la traduction (effets des médicaments et des substances chimiques)</term><term>Mammifères (MeSH)</term><term>Peptidylpropyl isomerase (génétique)</term><term>Peptidylpropyl isomerase (métabolisme)</term><term>Protéines de Drosophila (MeSH)</term><term>Protéines de liaison au tacrolimus (MeSH)</term><term>Récepteurs à activité tyrosine kinase (génétique)</term><term>Récepteurs à activité tyrosine kinase (métabolisme)</term><term>Saccharomyces cerevisiae (effets des médicaments et des substances chimiques)</term><term>Saccharomyces cerevisiae (enzymologie)</term><term>Saccharomyces cerevisiae (génétique)</term><term>Sirolimus (pharmacologie)</term><term>Transduction du signal (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Immunophilins</term><term>Peptidylprolyl Isomerase</term><term>RNA, Messenger</term><term>Receptor Protein-Tyrosine Kinases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Immunophilins</term><term>Peptidylprolyl Isomerase</term><term>Receptor Protein-Tyrosine Kinases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Sirolimus</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Drosophila Proteins</term><term>Tacrolimus Binding Proteins</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Peptide Chain Initiation, Translational</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Initiation de la traduction</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><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>ARN messager</term><term>Immunophilines</term><term>Peptidylpropyl isomerase</term><term>Récepteurs à activité tyrosine kinase</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Immunophilines</term><term>Peptidylpropyl isomerase</term><term>Récepteurs à activité tyrosine kinase</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Sirolimus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Humans</term><term>Mammals</term><term>Signal Transduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Humains</term><term>Mammifères</term><term>Protéines de Drosophila</term><term>Protéines de liaison au tacrolimus</term><term>Transduction du signal</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Rapamycin is a natural product with potent antifungal and immunosuppressive activities. Rapamycin binds to the FKBP12 prolyl isomerase, and the resulting protein-drug complex inhibits the TOR kinase homologs. Both the FKBP12 and the TOR proteins are highly conserved from yeast to man, and genetic and biochemical studies reveal that these proteins are the targets of rapamycin in vivo. Treatment of yeast or mammalian cells with rapamycin inhibits translational initiation of a subset of mRNAs and dramatically represses ribosomal mRNA and tRNA transcription. Furthermore, rapamycin exposure blocks cell cycle progression in the early G1 phase of the cell cycle, driving cells into a G0 state and, ultimately, triggering autophagy. Recent findings reveal that the upstream factors regulating the TOR signaling cascade are involved in detecting amino acids, nutrients, or growth factors. These findings indicate that the TOR proteins function in a signal transduction pathway that coordinates nutritional and mitogenic signals to control protein biosynthesis and degradation.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">10580846</PMID><DateCompleted><Year>1999</Year><Month>12</Month><Day>17</Day></DateCompleted><DateRevised><Year>2019</Year><Month>08</Month><Day>13</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0303-7207</ISSN><JournalIssue CitedMedium="Print"><Volume>155</Volume><Issue>1-2</Issue><PubDate><Year>1999</Year><Month>Sep</Month><Day>10</Day></PubDate></JournalIssue><Title>Molecular and cellular endocrinology</Title><ISOAbbreviation>Mol Cell Endocrinol</ISOAbbreviation></Journal><ArticleTitle>TOR kinase homologs function in a signal transduction pathway that is conserved from yeast to mammals.</ArticleTitle><Pagination><MedlinePgn>135-42</MedlinePgn></Pagination><Abstract><AbstractText>Rapamycin is a natural product with potent antifungal and immunosuppressive activities. Rapamycin binds to the FKBP12 prolyl isomerase, and the resulting protein-drug complex inhibits the TOR kinase homologs. Both the FKBP12 and the TOR proteins are highly conserved from yeast to man, and genetic and biochemical studies reveal that these proteins are the targets of rapamycin in vivo. Treatment of yeast or mammalian cells with rapamycin inhibits translational initiation of a subset of mRNAs and dramatically represses ribosomal mRNA and tRNA transcription. Furthermore, rapamycin exposure blocks cell cycle progression in the early G1 phase of the cell cycle, driving cells into a G0 state and, ultimately, triggering autophagy. Recent findings reveal that the upstream factors regulating the TOR signaling cascade are involved in detecting amino acids, nutrients, or growth factors. These findings indicate that the TOR proteins function in a signal transduction pathway that coordinates nutritional and mitogenic signals to control protein biosynthesis and degradation.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Cutler</LastName><ForeName>N S</ForeName><Initials>NS</Initials><AffiliationInfo><Affiliation>Department of Genetics, Duke University Medical Center, Durham, NC 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>K01 CA77075</GrantID><Acronym>CA</Acronym><Agency>NCI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 AI41937</GrantID><Acronym>AI</Acronym><Agency>NIAID 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><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>Ireland</Country><MedlineTA>Mol Cell Endocrinol</MedlineTA><NlmUniqueID>7500844</NlmUniqueID><ISSNLinking>0303-7207</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029721">Drosophila Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D012333">RNA, Messenger</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.10.1</RegistryNumber><NameOfSubstance UI="D020794">Receptor Protein-Tyrosine Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.10.1</RegistryNumber><NameOfSubstance UI="C080148">tor protein, Drosophila</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>EC 5.2.1.8</RegistryNumber><NameOfSubstance UI="D019696">Peptidylprolyl Isomerase</NameOfSubstance></Chemical><Chemical><RegistryNumber>W36ZG6FT64</RegistryNumber><NameOfSubstance UI="D020123">Sirolimus</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D029721" MajorTopicYN="Y">Drosophila Proteins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020104" MajorTopicYN="N">Immunophilins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008322" MajorTopicYN="N">Mammals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010442" MajorTopicYN="N">Peptide Chain Initiation, Translational</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019696" MajorTopicYN="N">Peptidylprolyl Isomerase</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012333" MajorTopicYN="N">RNA, Messenger</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020794" MajorTopicYN="N">Receptor Protein-Tyrosine Kinases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015398" MajorTopicYN="Y">Signal Transduction</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></MeshHeadingList><NumberOfReferences>82</NumberOfReferences></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1999</Year><Month>12</Month><Day>2</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1999</Year><Month>12</Month><Day>2</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1999</Year><Month>12</Month><Day>2</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">10580846</ArticleId><ArticleId IdType="pii">S0303-7207(99)00121-5</ArticleId><ArticleId IdType="doi">10.1016/s0303-7207(99)00121-5</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="Cutler, N S" sort="Cutler, N S" uniqKey="Cutler N" first="N S" last="Cutler">N S Cutler</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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