Branched-Chain Aminotransferases Control TORC1 Signaling in Saccharomyces cerevisiae.
Identifieur interne : 000D40 ( Main/Exploration ); précédent : 000D39; suivant : 000D41Branched-Chain Aminotransferases Control TORC1 Signaling in Saccharomyces cerevisiae.
Auteurs : Joanne M. Kingsbury [États-Unis] ; Neelam D. Sen [États-Unis] ; Maria E. Cardenas [États-Unis]Source :
- PLoS genetics [ 1553-7404 ] ; 2015.
Descripteurs français
- KwdFr :
- Aconitate hydratase (génétique), Aconitate hydratase (métabolisme), Complexe-1 cible mécanistique de la rapamycine (MeSH), Complexes multiprotéiques (métabolisme), Cycle citrique (MeSH), Cétoacides (métabolisme), Domaine catalytique (MeSH), Leucine (métabolisme), Protéines de Saccharomyces cerevisiae (génétique), Protéines de Saccharomyces cerevisiae (métabolisme), Protéines mitochondriales (génétique), Protéines mitochondriales (métabolisme), Saccharomyces cerevisiae (enzymologie), Saccharomyces cerevisiae (génétique), Saccharomyces cerevisiae (métabolisme), Sérine-thréonine kinases TOR (métabolisme), Transaminases (génétique), Transaminases (métabolisme), Transduction du signal (MeSH).
- MESH :
- enzymologie : Saccharomyces cerevisiae.
- génétique : Aconitate hydratase, Protéines de Saccharomyces cerevisiae, Protéines mitochondriales, Saccharomyces cerevisiae, Transaminases.
- métabolisme : Aconitate hydratase, Complexes multiprotéiques, Cétoacides, Leucine, Protéines de Saccharomyces cerevisiae, Protéines mitochondriales, Saccharomyces cerevisiae, Sérine-thréonine kinases TOR, Transaminases.
- Complexe-1 cible mécanistique de la rapamycine, Cycle citrique, Domaine catalytique, Transduction du signal.
English descriptors
- KwdEn :
- Aconitate Hydratase (genetics), Aconitate Hydratase (metabolism), Catalytic Domain (MeSH), Citric Acid Cycle (MeSH), Keto Acids (metabolism), Leucine (metabolism), Mechanistic Target of Rapamycin Complex 1 (MeSH), Mitochondrial Proteins (genetics), Mitochondrial Proteins (metabolism), Multiprotein Complexes (metabolism), Saccharomyces cerevisiae (enzymology), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism), Signal Transduction (MeSH), TOR Serine-Threonine Kinases (metabolism), Transaminases (genetics), Transaminases (metabolism).
- MESH :
- chemical , genetics : Aconitate Hydratase, Mitochondrial Proteins, Saccharomyces cerevisiae Proteins, Transaminases.
- chemical , metabolism : Aconitate Hydratase, Keto Acids, Leucine, Mitochondrial Proteins, Multiprotein Complexes, Saccharomyces cerevisiae Proteins, TOR Serine-Threonine Kinases, Transaminases.
- enzymology : Saccharomyces cerevisiae.
- genetics : Saccharomyces cerevisiae.
- metabolism : Saccharomyces cerevisiae.
- Catalytic Domain, Citric Acid Cycle, Mechanistic Target of Rapamycin Complex 1, Signal Transduction.
Abstract
The conserved target of rapamycin complex 1 (TORC1) integrates nutrient signals to orchestrate cell growth and proliferation. Leucine availability is conveyed to control TORC1 activity via the leu-tRNA synthetase/EGOC-GTPase module in yeast and mammals, but the mechanisms sensing leucine remain only partially understood. We show here that both leucine and its α-ketoacid metabolite, α-ketoisocaproate, effectively activate the yeast TORC1 kinase via both EGOC GTPase-dependent and -independent mechanisms. Leucine and α-ketoisocaproate are interconverted by ubiquitous branched-chain aminotransferases (BCAT), which in yeast are represented by the mitochondrial and cytosolic enzymes Bat1 and Bat2, respectively. BCAT yeast mutants exhibit severely compromised TORC1 activity, which is partially restored by expression of Bat1 active site mutants, implicating both catalytic and structural roles of BCATs in TORC1 control. We find that Bat1 interacts with branched-chain amino acid metabolic enzymes and, in a leucine-dependent fashion, with the tricarboxylic acid (TCA)-cycle enzyme aconitase. BCAT mutation perturbed TCA-cycle intermediate levels, consistent with a TCA-cycle block, and resulted in low ATP levels, activation of AMPK, and TORC1 inhibition. We propose the biosynthetic capacity of BCAT and its role in forming multicomplex metabolons connecting branched-chain amino acids and TCA-cycle metabolism governs TCA-cycle flux to activate TORC1 signaling. Because mammalian mitochondrial BCAT is known to form a supramolecular branched-chain α-keto acid dehydrogenase enzyme complex that links leucine metabolism to the TCA-cycle, these findings establish a precedent for understanding TORC1 signaling in mammals.
DOI: 10.1371/journal.pgen.1005714
PubMed: 26659116
PubMed Central: PMC4684349
Affiliations:
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Leucine availability is conveyed to control TORC1 activity via the leu-tRNA synthetase/EGOC-GTPase module in yeast and mammals, but the mechanisms sensing leucine remain only partially understood. We show here that both leucine and its α-ketoacid metabolite, α-ketoisocaproate, effectively activate the yeast TORC1 kinase via both EGOC GTPase-dependent and -independent mechanisms. Leucine and α-ketoisocaproate are interconverted by ubiquitous branched-chain aminotransferases (BCAT), which in yeast are represented by the mitochondrial and cytosolic enzymes Bat1 and Bat2, respectively. BCAT yeast mutants exhibit severely compromised TORC1 activity, which is partially restored by expression of Bat1 active site mutants, implicating both catalytic and structural roles of BCATs in TORC1 control. We find that Bat1 interacts with branched-chain amino acid metabolic enzymes and, in a leucine-dependent fashion, with the tricarboxylic acid (TCA)-cycle enzyme aconitase. BCAT mutation perturbed TCA-cycle intermediate levels, consistent with a TCA-cycle block, and resulted in low ATP levels, activation of AMPK, and TORC1 inhibition. We propose the biosynthetic capacity of BCAT and its role in forming multicomplex metabolons connecting branched-chain amino acids and TCA-cycle metabolism governs TCA-cycle flux to activate TORC1 signaling. Because mammalian mitochondrial BCAT is known to form a supramolecular branched-chain α-keto acid dehydrogenase enzyme complex that links leucine metabolism to the TCA-cycle, these findings establish a precedent for understanding TORC1 signaling in mammals. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26659116</PMID><DateCompleted><Year>2016</Year><Month>07</Month><Day>06</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Electronic-eCollection"><Journal><ISSN IssnType="Electronic">1553-7404</ISSN><JournalIssue CitedMedium="Internet"><Volume>11</Volume><Issue>12</Issue><PubDate><Year>2015</Year><Month>Dec</Month></PubDate></JournalIssue><Title>PLoS genetics</Title><ISOAbbreviation>PLoS Genet</ISOAbbreviation></Journal><ArticleTitle>Branched-Chain Aminotransferases Control TORC1 Signaling in Saccharomyces cerevisiae.</ArticleTitle><Pagination><MedlinePgn>e1005714</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1371/journal.pgen.1005714</ELocationID><Abstract><AbstractText>The conserved target of rapamycin complex 1 (TORC1) integrates nutrient signals to orchestrate cell growth and proliferation. Leucine availability is conveyed to control TORC1 activity via the leu-tRNA synthetase/EGOC-GTPase module in yeast and mammals, but the mechanisms sensing leucine remain only partially understood. We show here that both leucine and its α-ketoacid metabolite, α-ketoisocaproate, effectively activate the yeast TORC1 kinase via both EGOC GTPase-dependent and -independent mechanisms. Leucine and α-ketoisocaproate are interconverted by ubiquitous branched-chain aminotransferases (BCAT), which in yeast are represented by the mitochondrial and cytosolic enzymes Bat1 and Bat2, respectively. BCAT yeast mutants exhibit severely compromised TORC1 activity, which is partially restored by expression of Bat1 active site mutants, implicating both catalytic and structural roles of BCATs in TORC1 control. We find that Bat1 interacts with branched-chain amino acid metabolic enzymes and, in a leucine-dependent fashion, with the tricarboxylic acid (TCA)-cycle enzyme aconitase. BCAT mutation perturbed TCA-cycle intermediate levels, consistent with a TCA-cycle block, and resulted in low ATP levels, activation of AMPK, and TORC1 inhibition. We propose the biosynthetic capacity of BCAT and its role in forming multicomplex metabolons connecting branched-chain amino acids and TCA-cycle metabolism governs TCA-cycle flux to activate TORC1 signaling. Because mammalian mitochondrial BCAT is known to form a supramolecular branched-chain α-keto acid dehydrogenase enzyme complex that links leucine metabolism to the TCA-cycle, these findings establish a precedent for understanding TORC1 signaling in mammals. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kingsbury</LastName><ForeName>Joanne M</ForeName><Initials>JM</Initials><AffiliationInfo><Affiliation>Department of Molecular Genetics and Microbiology, Duke University Medical Center, Durham, North Carolina, United States of America.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sen</LastName><ForeName>Neelam D</ForeName><Initials>ND</Initials><AffiliationInfo><Affiliation>Department of Molecular Genetics and Microbiology, Duke University Medical Center, Durham, North Carolina, United States of America.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cardenas</LastName><ForeName>Maria E</ForeName><Initials>ME</Initials><AffiliationInfo><Affiliation>Department of Molecular Genetics and Microbiology, Duke University Medical Center, Durham, North Carolina, United States of America.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 CA154499</GrantID><Acronym>CA</Acronym><Agency>NCI 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><ArticleDate DateType="Electronic"><Year>2015</Year><Month>12</Month><Day>11</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>PLoS Genet</MedlineTA><NlmUniqueID>101239074</NlmUniqueID><ISSNLinking>1553-7390</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007651">Keto Acids</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D024101">Mitochondrial Proteins</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>816-66-0</RegistryNumber><NameOfSubstance UI="C013082">alpha-ketoisocaproic acid</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.6.1.-</RegistryNumber><NameOfSubstance UI="D000637">Transaminases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.6.1.42</RegistryNumber><NameOfSubstance UI="C101168">BAT1 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.6.1.42</RegistryNumber><NameOfSubstance UI="C101127">BAT2 protein, S cerevisiae</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 4.2.1.3</RegistryNumber><NameOfSubstance UI="D000154">Aconitate Hydratase</NameOfSubstance></Chemical><Chemical><RegistryNumber>GMW67QNF9C</RegistryNumber><NameOfSubstance UI="D007930">Leucine</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000154" MajorTopicYN="N">Aconitate Hydratase</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020134" MajorTopicYN="N">Catalytic Domain</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002952" MajorTopicYN="N">Citric Acid Cycle</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007651" MajorTopicYN="N">Keto Acids</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007930" MajorTopicYN="N">Leucine</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="D024101" MajorTopicYN="N">Mitochondrial Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D046912" MajorTopicYN="N">Multiprotein Complexes</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029701" MajorTopicYN="N">Saccharomyces cerevisiae Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015398" MajorTopicYN="Y">Signal Transduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D058570" MajorTopicYN="N">TOR Serine-Threonine Kinases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000637" 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