General Control Nonderepressible 2 (GCN2) Kinase Inhibits Target of Rapamycin Complex 1 in Response to Amino Acid Starvation in Saccharomyces cerevisiae.
Identifieur interne : 000838 ( Main/Exploration ); précédent : 000837; suivant : 000839General Control Nonderepressible 2 (GCN2) Kinase Inhibits Target of Rapamycin Complex 1 in Response to Amino Acid Starvation in Saccharomyces cerevisiae.
Auteurs : Wenjie Yuan [République populaire de Chine] ; Shuguang Guo ; Jiaoqi Gao [République populaire de Chine] ; Mingming Zhong ; Gonghong Yan ; Wangmeng Wu ; Yapeng Chao [République populaire de Chine] ; Yu Jiang [États-Unis]Source :
- The Journal of biological chemistry [ 1083-351X ] ; 2017.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Amino Acids, Membrane Proteins, Protein-Serine-Threonine Kinases, Saccharomyces cerevisiae Proteins.
- metabolism : Saccharomyces cerevisiae.
- Down-Regulation, Protein Binding.
Abstract
In eukaryotic cells, two conserved protein kinases, Gcn2 and TOR complex 1 (TORC1), couple amino acid conditions to protein translation. Gcn2 functions as an amino acid sensor and is activated by uncharged tRNAs that accumulate when intracellular amino acids are limited. Activated Gcn2 phosphorylates and inhibits eukaryotic initiation factor-2α (eIF2α), resulting in repression of general protein synthesis. Like Gcn2, TORC1 is also involved in sensing amino acid conditions. However, the underlying mechanism remains unclear. In the present study, we show that TORC1 is a direct target of Gcn2 kinase in the yeast Saccharomyces cerevisiae In response to amino acid starvation, Gcn2 binds to TORC1 and phosphorylates Kog1, the unique regulatory subunit of TORC1, resulting in down-regulation of TORC1 kinase activity. In the absence of Gcn2, TORC1 signaling activity increases and becomes unresponsive to amino acid starvation. Our findings demonstrate that TORC1 is an effector of Gcn2 in amino acid signaling, hence defining a novel mechanism by which TORC1 senses amino acid starvation.
DOI: 10.1074/jbc.M116.772194
PubMed: 28057755
PubMed Central: PMC5314164
Affiliations:
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Dalian University of Technology, Dalian 116024</wicri:regionArea><wicri:noRegion>Dalian 116024</wicri:noRegion></affiliation><affiliation><nlm:affiliation>the Department of Pharmacology and Chemical Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15213, and.</nlm:affiliation><wicri:noCountry code="subField">and</wicri:noCountry></affiliation></author><author><name sortKey="Guo, Shuguang" sort="Guo, Shuguang" uniqKey="Guo S" first="Shuguang" last="Guo">Shuguang Guo</name><affiliation><nlm:affiliation>the Department of Pharmacology and Chemical Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15213, and.</nlm:affiliation><wicri:noCountry code="subField">and</wicri:noCountry></affiliation></author><author><name sortKey="Gao, Jiaoqi" sort="Gao, Jiaoqi" uniqKey="Gao J" first="Jiaoqi" last="Gao">Jiaoqi Gao</name><affiliation wicri:level="1"><nlm:affiliation>From the School of Life Science and Biotechnology, Dalian University of Technology, Dalian 116024, China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>From the School of Life Science and Biotechnology, Dalian University of Technology, Dalian 116024</wicri:regionArea><wicri:noRegion>Dalian 116024</wicri:noRegion></affiliation><affiliation><nlm:affiliation>the Department of Pharmacology and Chemical Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15213, and.</nlm:affiliation><wicri:noCountry code="subField">and</wicri:noCountry></affiliation></author><author><name sortKey="Zhong, Mingming" sort="Zhong, Mingming" uniqKey="Zhong M" first="Mingming" last="Zhong">Mingming Zhong</name><affiliation><nlm:affiliation>the Department of Pharmacology and Chemical Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15213, and.</nlm:affiliation><wicri:noCountry code="subField">and</wicri:noCountry></affiliation></author><author><name sortKey="Yan, Gonghong" sort="Yan, Gonghong" uniqKey="Yan G" first="Gonghong" last="Yan">Gonghong Yan</name><affiliation><nlm:affiliation>the Department of Pharmacology and Chemical Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15213, and.</nlm:affiliation><wicri:noCountry code="subField">and</wicri:noCountry></affiliation></author><author><name sortKey="Wu, Wangmeng" sort="Wu, Wangmeng" uniqKey="Wu W" first="Wangmeng" last="Wu">Wangmeng Wu</name><affiliation><nlm:affiliation>the Department of Pharmacology and Chemical Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15213, and.</nlm:affiliation><wicri:noCountry code="subField">and</wicri:noCountry></affiliation></author><author><name sortKey="Chao, Yapeng" sort="Chao, Yapeng" uniqKey="Chao Y" first="Yapeng" last="Chao">Yapeng Chao</name><affiliation wicri:level="1"><nlm:affiliation>the State Key Laboratories of Transducer Technology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>the State Key Laboratories of Transducer Technology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101</wicri:regionArea><placeName><settlement type="city">Pékin</settlement></placeName></affiliation></author><author><name sortKey="Jiang, Yu" sort="Jiang, Yu" uniqKey="Jiang Y" first="Yu" last="Jiang">Yu Jiang</name><affiliation wicri:level="1"><nlm:affiliation>the Department of Pharmacology and Chemical Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15213, and yuj5@pitt.edu.</nlm:affiliation><country wicri:rule="url">États-Unis</country><wicri:regionArea>the Department of Pharmacology and Chemical Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15213</wicri:regionArea><wicri:noRegion>Pennsylvania 15213</wicri:noRegion></affiliation></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="eISSN">1083-351X</idno><imprint><date when="2017" type="published">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acids (metabolism)</term><term>Down-Regulation (MeSH)</term><term>Membrane Proteins (metabolism)</term><term>Protein Binding (MeSH)</term><term>Protein-Serine-Threonine Kinases (metabolism)</term><term>Saccharomyces cerevisiae (metabolism)</term><term>Saccharomyces cerevisiae Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acides aminés (métabolisme)</term><term>Liaison aux protéines (MeSH)</term><term>Protein-Serine-Threonine Kinases (métabolisme)</term><term>Protéines de Saccharomyces cerevisiae (métabolisme)</term><term>Protéines membranaires (métabolisme)</term><term>Régulation négative (MeSH)</term><term>Saccharomyces cerevisiae (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Amino Acids</term><term>Membrane Proteins</term><term>Protein-Serine-Threonine Kinases</term><term>Saccharomyces cerevisiae Proteins</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Acides aminés</term><term>Protein-Serine-Threonine Kinases</term><term>Protéines de Saccharomyces cerevisiae</term><term>Protéines membranaires</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Down-Regulation</term><term>Protein Binding</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Liaison aux protéines</term><term>Régulation négative</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">In eukaryotic cells, two conserved protein kinases, Gcn2 and TOR complex 1 (TORC1), couple amino acid conditions to protein translation. Gcn2 functions as an amino acid sensor and is activated by uncharged tRNAs that accumulate when intracellular amino acids are limited. Activated Gcn2 phosphorylates and inhibits eukaryotic initiation factor-2α (eIF2α), resulting in repression of general protein synthesis. Like Gcn2, TORC1 is also involved in sensing amino acid conditions. However, the underlying mechanism remains unclear. In the present study, we show that TORC1 is a direct target of Gcn2 kinase in the yeast <i>Saccharomyces cerevisiae</i> In response to amino acid starvation, Gcn2 binds to TORC1 and phosphorylates Kog1, the unique regulatory subunit of TORC1, resulting in down-regulation of TORC1 kinase activity. In the absence of Gcn2, TORC1 signaling activity increases and becomes unresponsive to amino acid starvation. Our findings demonstrate that TORC1 is an effector of Gcn2 in amino acid signaling, hence defining a novel mechanism by which TORC1 senses amino acid starvation.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">28057755</PMID><DateCompleted><Year>2017</Year><Month>07</Month><Day>05</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1083-351X</ISSN><JournalIssue CitedMedium="Internet"><Volume>292</Volume><Issue>7</Issue><PubDate><Year>2017</Year><Month>02</Month><Day>17</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>General Control Nonderepressible 2 (GCN2) Kinase Inhibits Target of Rapamycin Complex 1 in Response to Amino Acid Starvation in <i>Saccharomyces cerevisiae</i>.</ArticleTitle><Pagination><MedlinePgn>2660-2669</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1074/jbc.M116.772194</ELocationID><Abstract><AbstractText>In eukaryotic cells, two conserved protein kinases, Gcn2 and TOR complex 1 (TORC1), couple amino acid conditions to protein translation. Gcn2 functions as an amino acid sensor and is activated by uncharged tRNAs that accumulate when intracellular amino acids are limited. Activated Gcn2 phosphorylates and inhibits eukaryotic initiation factor-2α (eIF2α), resulting in repression of general protein synthesis. Like Gcn2, TORC1 is also involved in sensing amino acid conditions. However, the underlying mechanism remains unclear. In the present study, we show that TORC1 is a direct target of Gcn2 kinase in the yeast <i>Saccharomyces cerevisiae</i> In response to amino acid starvation, Gcn2 binds to TORC1 and phosphorylates Kog1, the unique regulatory subunit of TORC1, resulting in down-regulation of TORC1 kinase activity. In the absence of Gcn2, TORC1 signaling activity increases and becomes unresponsive to amino acid starvation. Our findings demonstrate that TORC1 is an effector of Gcn2 in amino acid signaling, hence defining a novel mechanism by which TORC1 senses amino acid starvation.</AbstractText><CopyrightInformation>© 2017 by The American Society for Biochemistry and Molecular Biology, Inc.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Yuan</LastName><ForeName>Wenjie</ForeName><Initials>W</Initials><AffiliationInfo><Affiliation>From the School of Life Science and Biotechnology, Dalian University of Technology, Dalian 116024, China.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>the Department of Pharmacology and Chemical Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15213, and.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Guo</LastName><ForeName>Shuguang</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>the Department of Pharmacology and Chemical Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15213, and.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gao</LastName><ForeName>Jiaoqi</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>From the School of Life Science and Biotechnology, Dalian University of Technology, Dalian 116024, China.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>the Department of Pharmacology and Chemical Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15213, and.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Zhong</LastName><ForeName>Mingming</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>the Department of Pharmacology and Chemical Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15213, and.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yan</LastName><ForeName>Gonghong</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>the Department of Pharmacology and Chemical Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15213, and.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wu</LastName><ForeName>Wangmeng</ForeName><Initials>W</Initials><AffiliationInfo><Affiliation>the Department of Pharmacology and Chemical Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15213, and.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chao</LastName><ForeName>Yapeng</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>the State Key Laboratories of Transducer Technology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Jiang</LastName><ForeName>Yu</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>the Department of Pharmacology and Chemical Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15213, and yuj5@pitt.edu.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R21 CA169186</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><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2017</Year><Month>01</Month><Day>05</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000596">Amino Acids</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C515118">Kog1 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008565">Membrane Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber><NameOfSubstance UI="C512912">GCN2 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber><NameOfSubstance UI="D017346">Protein-Serine-Threonine Kinases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000596" MajorTopicYN="N">Amino Acids</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015536" MajorTopicYN="N">Down-Regulation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008565" MajorTopicYN="N">Membrane Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017346" MajorTopicYN="N">Protein-Serine-Threonine Kinases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029701" MajorTopicYN="N">Saccharomyces cerevisiae 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Guo</name><name sortKey="Wu, Wangmeng" sort="Wu, Wangmeng" uniqKey="Wu W" first="Wangmeng" last="Wu">Wangmeng Wu</name><name sortKey="Yan, Gonghong" sort="Yan, Gonghong" uniqKey="Yan G" first="Gonghong" last="Yan">Gonghong Yan</name><name sortKey="Zhong, Mingming" sort="Zhong, Mingming" uniqKey="Zhong M" first="Mingming" last="Zhong">Mingming Zhong</name></noCountry><country name="République populaire de Chine"><noRegion><name sortKey="Yuan, Wenjie" sort="Yuan, Wenjie" uniqKey="Yuan W" first="Wenjie" last="Yuan">Wenjie Yuan</name></noRegion><name sortKey="Chao, Yapeng" sort="Chao, Yapeng" uniqKey="Chao Y" first="Yapeng" last="Chao">Yapeng Chao</name><name sortKey="Gao, Jiaoqi" sort="Gao, Jiaoqi" uniqKey="Gao J" first="Jiaoqi" last="Gao">Jiaoqi Gao</name></country><country name="États-Unis"><noRegion><name sortKey="Jiang, Yu" sort="Jiang, Yu" uniqKey="Jiang Y" first="Yu" last="Jiang">Yu Jiang</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix 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