A role for TOR complex 2 signaling in promoting autophagy.
Identifieur interne : 000F30 ( Main/Exploration ); précédent : 000F29; suivant : 000F31A role for TOR complex 2 signaling in promoting autophagy.
Auteurs : Ariadne Vlahakis [États-Unis] ; Ted PowersSource :
- Autophagy [ 1554-8635 ] ; 2014.
Descripteurs français
- KwdFr :
- Acides aminés (composition chimique), Autophagie (MeSH), Azote (composition chimique), Calcineurine (métabolisme), Calcium (composition chimique), Calcium (métabolisme), Complexe-1 cible mécanistique de la rapamycine (MeSH), Complexe-2 cible mécanistique de la rapamycine (MeSH), Complexes multiprotéiques (métabolisme), Glycogen Synthase Kinase 3 (métabolisme), Protéines de Saccharomyces cerevisiae (métabolisme), Saccharomyces cerevisiae (métabolisme), Sérine-thréonine kinases TOR (métabolisme), Transduction du signal (MeSH), Évolution de la maladie (MeSH).
- MESH :
- composition chimique : Acides aminés, Azote, Calcium.
- métabolisme : Calcineurine, Calcium, Complexes multiprotéiques, Glycogen Synthase Kinase 3, Protéines de Saccharomyces cerevisiae, Saccharomyces cerevisiae, Sérine-thréonine kinases TOR.
- Autophagie, Complexe-1 cible mécanistique de la rapamycine, Complexe-2 cible mécanistique de la rapamycine, Transduction du signal, Évolution de la maladie.
English descriptors
- KwdEn :
- Amino Acids (chemistry), Autophagy (MeSH), Calcineurin (metabolism), Calcium (chemistry), Calcium (metabolism), Disease Progression (MeSH), Glycogen Synthase Kinase 3 (metabolism), Mechanistic Target of Rapamycin Complex 1 (MeSH), Mechanistic Target of Rapamycin Complex 2 (MeSH), Multiprotein Complexes (metabolism), Nitrogen (chemistry), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (metabolism), Signal Transduction (MeSH), TOR Serine-Threonine Kinases (metabolism).
- MESH :
- chemical , chemistry : Amino Acids, Calcium, Nitrogen.
- chemical , metabolism : Calcineurin, Calcium, Glycogen Synthase Kinase 3, Multiprotein Complexes, Saccharomyces cerevisiae Proteins, TOR Serine-Threonine Kinases.
- metabolism : Saccharomyces cerevisiae.
- Autophagy, Disease Progression, Mechanistic Target of Rapamycin Complex 1, Mechanistic Target of Rapamycin Complex 2, Signal Transduction.
Abstract
The conserved target of rapamycin (TOR) kinase is a central regulator of cell growth in response to nutrient availability. TOR forms 2 structurally and functionally distinct complexes, TORC1 and TORC2, and negatively regulates autophagy via TORC1. Here we demonstrate TOR also operates independently through the TORC2 signaling pathway to promote autophagy upon amino acid limitation. Under these conditions, TORC2, through its downstream target kinase Ypk1, inhibits the Ca(2+)- and Cmd1/calmodulin-dependent phosphatase, calcineurin, to enable the activation of the amino acid-sensing EIF2S1/eIF2α kinase, Gcn2, and promote autophagy. Thus TORC2 signaling regulates autophagy in a pathway distinct from TORC1 to provide a tunable response to the cellular metabolic state.
DOI: 10.4161/auto.36262
PubMed: 25426890
PubMed Central: PMC4502789
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">A role for TOR complex 2 signaling in promoting autophagy.</title><author><name sortKey="Vlahakis, Ariadne" sort="Vlahakis, Ariadne" uniqKey="Vlahakis A" first="Ariadne" last="Vlahakis">Ariadne Vlahakis</name><affiliation wicri:level="2"><nlm:affiliation>a Department of Molecular and Cellular Biology; College of Biological Sciences ; University of California, Davis ; Davis , CA USA.</nlm:affiliation><country>États-Unis</country><placeName><region type="state">Californie</region></placeName><wicri:cityArea>a Department of Molecular and Cellular Biology; College of Biological Sciences ; University of California, Davis ; Davis </wicri:cityArea></affiliation></author><author><name sortKey="Powers, Ted" sort="Powers, Ted" uniqKey="Powers T" first="Ted" last="Powers">Ted Powers</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2014">2014</date><idno type="RBID">pubmed:25426890</idno><idno type="pmid">25426890</idno><idno type="doi">10.4161/auto.36262</idno><idno type="pmc">PMC4502789</idno><idno type="wicri:Area/Main/Corpus">000D51</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000D51</idno><idno type="wicri:Area/Main/Curation">000D51</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000D51</idno><idno type="wicri:Area/Main/Exploration">000D51</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">A role for TOR complex 2 signaling in promoting autophagy.</title><author><name sortKey="Vlahakis, Ariadne" sort="Vlahakis, Ariadne" uniqKey="Vlahakis A" first="Ariadne" last="Vlahakis">Ariadne Vlahakis</name><affiliation wicri:level="2"><nlm:affiliation>a Department of Molecular and Cellular Biology; College of Biological Sciences ; University of California, Davis ; Davis , CA USA.</nlm:affiliation><country>États-Unis</country><placeName><region type="state">Californie</region></placeName><wicri:cityArea>a Department of Molecular and Cellular Biology; College of Biological Sciences ; University of California, Davis ; Davis </wicri:cityArea></affiliation></author><author><name sortKey="Powers, Ted" sort="Powers, Ted" uniqKey="Powers T" first="Ted" last="Powers">Ted Powers</name></author></analytic><series><title level="j">Autophagy</title><idno type="eISSN">1554-8635</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acids (chemistry)</term><term>Autophagy (MeSH)</term><term>Calcineurin (metabolism)</term><term>Calcium (chemistry)</term><term>Calcium (metabolism)</term><term>Disease Progression (MeSH)</term><term>Glycogen Synthase Kinase 3 (metabolism)</term><term>Mechanistic Target of Rapamycin Complex 1 (MeSH)</term><term>Mechanistic Target of Rapamycin Complex 2 (MeSH)</term><term>Multiprotein Complexes (metabolism)</term><term>Nitrogen (chemistry)</term><term>Saccharomyces cerevisiae (metabolism)</term><term>Saccharomyces cerevisiae Proteins (metabolism)</term><term>Signal Transduction (MeSH)</term><term>TOR Serine-Threonine Kinases (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acides aminés (composition chimique)</term><term>Autophagie (MeSH)</term><term>Azote (composition chimique)</term><term>Calcineurine (métabolisme)</term><term>Calcium (composition chimique)</term><term>Calcium (métabolisme)</term><term>Complexe-1 cible mécanistique de la rapamycine (MeSH)</term><term>Complexe-2 cible mécanistique de la rapamycine (MeSH)</term><term>Complexes multiprotéiques (métabolisme)</term><term>Glycogen Synthase Kinase 3 (métabolisme)</term><term>Protéines de Saccharomyces cerevisiae (métabolisme)</term><term>Saccharomyces cerevisiae (métabolisme)</term><term>Sérine-thréonine kinases TOR (métabolisme)</term><term>Transduction du signal (MeSH)</term><term>Évolution de la maladie (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Amino Acids</term><term>Calcium</term><term>Nitrogen</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Calcineurin</term><term>Calcium</term><term>Glycogen Synthase Kinase 3</term><term>Multiprotein Complexes</term><term>Saccharomyces cerevisiae Proteins</term><term>TOR Serine-Threonine Kinases</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Acides aminés</term><term>Azote</term><term>Calcium</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Calcineurine</term><term>Calcium</term><term>Complexes multiprotéiques</term><term>Glycogen Synthase Kinase 3</term><term>Protéines de Saccharomyces cerevisiae</term><term>Saccharomyces cerevisiae</term><term>Sérine-thréonine kinases TOR</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Autophagy</term><term>Disease Progression</term><term>Mechanistic Target of Rapamycin Complex 1</term><term>Mechanistic Target of Rapamycin Complex 2</term><term>Signal Transduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Autophagie</term><term>Complexe-1 cible mécanistique de la rapamycine</term><term>Complexe-2 cible mécanistique de la rapamycine</term><term>Transduction du signal</term><term>Évolution de la maladie</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The conserved target of rapamycin (TOR) kinase is a central regulator of cell growth in response to nutrient availability. TOR forms 2 structurally and functionally distinct complexes, TORC1 and TORC2, and negatively regulates autophagy via TORC1. Here we demonstrate TOR also operates independently through the TORC2 signaling pathway to promote autophagy upon amino acid limitation. Under these conditions, TORC2, through its downstream target kinase Ypk1, inhibits the Ca(2+)- and Cmd1/calmodulin-dependent phosphatase, calcineurin, to enable the activation of the amino acid-sensing EIF2S1/eIF2α kinase, Gcn2, and promote autophagy. Thus TORC2 signaling regulates autophagy in a pathway distinct from TORC1 to provide a tunable response to the cellular metabolic state. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25426890</PMID><DateCompleted><Year>2015</Year><Month>09</Month><Day>14</Day></DateCompleted><DateRevised><Year>2017</Year><Month>11</Month><Day>16</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1554-8635</ISSN><JournalIssue CitedMedium="Internet"><Volume>10</Volume><Issue>11</Issue><PubDate><Year>2014</Year></PubDate></JournalIssue><Title>Autophagy</Title><ISOAbbreviation>Autophagy</ISOAbbreviation></Journal><ArticleTitle>A role for TOR complex 2 signaling in promoting autophagy.</ArticleTitle><Pagination><MedlinePgn>2085-6</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.4161/auto.36262</ELocationID><Abstract><AbstractText>The conserved target of rapamycin (TOR) kinase is a central regulator of cell growth in response to nutrient availability. TOR forms 2 structurally and functionally distinct complexes, TORC1 and TORC2, and negatively regulates autophagy via TORC1. Here we demonstrate TOR also operates independently through the TORC2 signaling pathway to promote autophagy upon amino acid limitation. Under these conditions, TORC2, through its downstream target kinase Ypk1, inhibits the Ca(2+)- and Cmd1/calmodulin-dependent phosphatase, calcineurin, to enable the activation of the amino acid-sensing EIF2S1/eIF2α kinase, Gcn2, and promote autophagy. Thus TORC2 signaling regulates autophagy in a pathway distinct from TORC1 to provide a tunable response to the cellular metabolic state. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Vlahakis</LastName><ForeName>Ariadne</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>a Department of Molecular and Cellular Biology; College of Biological Sciences ; University of California, Davis ; Davis , CA USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Powers</LastName><ForeName>Ted</ForeName><Initials>T</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>T32 GM007377</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>GM086387</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Autophagy</MedlineTA><NlmUniqueID>101265188</NlmUniqueID><ISSNLinking>1554-8627</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000596">Amino Acids</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D046912">Multiprotein Complexes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.1.1</RegistryNumber><NameOfSubstance UI="D058570">TOR Serine-Threonine Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber><NameOfSubstance UI="D000076222">Mechanistic Target of Rapamycin Complex 1</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber><NameOfSubstance UI="D000076225">Mechanistic Target of Rapamycin Complex 2</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.26</RegistryNumber><NameOfSubstance UI="D038362">Glycogen Synthase Kinase 3</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.12.1</RegistryNumber><NameOfSubstance UI="C068124">MCK1 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.3.16</RegistryNumber><NameOfSubstance UI="D019703">Calcineurin</NameOfSubstance></Chemical><Chemical><RegistryNumber>N762921K75</RegistryNumber><NameOfSubstance UI="D009584">Nitrogen</NameOfSubstance></Chemical><Chemical><RegistryNumber>SY7Q814VUP</RegistryNumber><NameOfSubstance UI="D002118">Calcium</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000596" MajorTopicYN="N">Amino Acids</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001343" MajorTopicYN="Y">Autophagy</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019703" MajorTopicYN="N">Calcineurin</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002118" MajorTopicYN="N">Calcium</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018450" MajorTopicYN="N">Disease Progression</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D038362" MajorTopicYN="N">Glycogen Synthase Kinase 3</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000076222" MajorTopicYN="N">Mechanistic Target of Rapamycin Complex 1</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000076225" MajorTopicYN="N">Mechanistic Target of Rapamycin Complex 2</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D046912" MajorTopicYN="N">Multiprotein Complexes</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009584" MajorTopicYN="N">Nitrogen</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029701" MajorTopicYN="N">Saccharomyces cerevisiae Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015398" MajorTopicYN="N">Signal Transduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D058570" MajorTopicYN="N">TOR Serine-Threonine Kinases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">GAAC</Keyword><Keyword MajorTopicYN="N">Gcn2</Keyword><Keyword MajorTopicYN="N">Gcn4</Keyword><Keyword MajorTopicYN="N">TOR</Keyword><Keyword MajorTopicYN="N">TORC1</Keyword><Keyword MajorTopicYN="N">TORC2</Keyword><Keyword MajorTopicYN="N">Ypk1</Keyword><Keyword MajorTopicYN="N">amino acid</Keyword><Keyword MajorTopicYN="N">calcineurin</Keyword><Keyword MajorTopicYN="N">nitrogen</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2014</Year><Month>11</Month><Day>27</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2014</Year><Month>11</Month><Day>27</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2015</Year><Month>9</Month><Day>15</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">25426890</ArticleId><ArticleId IdType="doi">10.4161/auto.36262</ArticleId><ArticleId IdType="pmc">PMC4502789</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Californie</li></region></list><tree><noCountry><name sortKey="Powers, Ted" sort="Powers, Ted" uniqKey="Powers T" first="Ted" last="Powers">Ted Powers</name></noCountry><country name="États-Unis"><region name="Californie"><name sortKey="Vlahakis, Ariadne" sort="Vlahakis, Ariadne" uniqKey="Vlahakis A" first="Ariadne" last="Vlahakis">Ariadne Vlahakis</name></region></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 000F30 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 000F30 | 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:25426890
|texte= A role for TOR complex 2 signaling in promoting autophagy.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:25426890" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a RapamycinFungusV1
| This area was generated with Dilib version V0.6.38. |  |