TORC1 signaling is governed by two negative regulators in fission yeast.
Identifieur interne : 000F76 ( Main/Corpus ); précédent : 000F75; suivant : 000F77TORC1 signaling is governed by two negative regulators in fission yeast.
Auteurs : Ning Ma ; Qingbin Liu ; Lili Zhang ; Elizabeth P. Henske ; Yan MaSource :
- Genetics [ 1943-2631 ] ; 2013.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Amino Acid Transport Systems (metabolism), Amino Acids (genetics), Amino Acids (metabolism), Cell Cycle (MeSH), Gene Expression Regulation, Fungal (MeSH), Mechanistic Target of Rapamycin Complex 1 (MeSH), Multiprotein Complexes (genetics), Multiprotein Complexes (metabolism), Mutation (MeSH), Receptors, Atrial Natriuretic Factor (genetics), Schizosaccharomyces (genetics), Schizosaccharomyces pombe Proteins (genetics), Schizosaccharomyces pombe Proteins (metabolism), Signal Transduction (MeSH), TOR Serine-Threonine Kinases (genetics), TOR Serine-Threonine Kinases (metabolism).
- MESH :
- chemical , genetics : Amino Acids, Multiprotein Complexes, Receptors, Atrial Natriuretic Factor, Schizosaccharomyces pombe Proteins, TOR Serine-Threonine Kinases.
- chemical , metabolism : Amino Acid Transport Systems, Amino Acids, Multiprotein Complexes, Schizosaccharomyces pombe Proteins, TOR Serine-Threonine Kinases.
- genetics : Schizosaccharomyces.
- Amino Acid Sequence, Cell Cycle, Gene Expression Regulation, Fungal, Mechanistic Target of Rapamycin Complex 1, Mutation, Signal Transduction.
Abstract
The target of rapamycin (TOR) is a highly conserved protein kinase that regulates cell growth and metabolism. Here we performed a genome-wide screen to identify negative regulators of TOR complex 1 (TORC1) in Schizosaccharomyces pombe by isolating mutants that phenocopy Δtsc2, in which TORC1 signaling is known to be up-regulated. We discovered that Δnpr2 displayed similar phenotypes to Δtsc2 in terms of amino acid uptake defects and mislocalization of the Cat1 permease. However, Δnpr2 and Δtsc2 clearly showed different phenotypes in terms of rapamycin supersensitivity and Isp5 transcription upon various treatments. Furthermore, we showed that Tor2 controls amino acid homeostasis at the transcriptional and post-transcriptional levels. Our data reveal that both Npr2 and Tsc2 negatively regulate TORC1 signaling, and Npr2, but not Tsc2, may be involved in the feedback loop of a nutrient-sensing pathway.
DOI: 10.1534/genetics.113.154674
PubMed: 23934889
PubMed Central: PMC3781973
Links to Exploration step
pubmed:23934889Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">TORC1 signaling is governed by two negative regulators in fission yeast.</title><author><name sortKey="Ma, Ning" sort="Ma, Ning" uniqKey="Ma N" first="Ning" last="Ma">Ning Ma</name><affiliation><nlm:affiliation>Division of Molecular Pharmacology and Pharmacogenomics, Department of Biochemistry and Molecular Biology, Kobe University Graduate School of Medicine, Kobe 650-0017, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Liu, Qingbin" sort="Liu, Qingbin" uniqKey="Liu Q" first="Qingbin" last="Liu">Qingbin Liu</name></author><author><name sortKey="Zhang, Lili" sort="Zhang, Lili" uniqKey="Zhang L" first="Lili" last="Zhang">Lili Zhang</name></author><author><name sortKey="Henske, Elizabeth P" sort="Henske, Elizabeth P" uniqKey="Henske E" first="Elizabeth P" last="Henske">Elizabeth P. Henske</name></author><author><name sortKey="Ma, Yan" sort="Ma, Yan" uniqKey="Ma Y" first="Yan" last="Ma">Yan Ma</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2013">2013</date><idno type="RBID">pubmed:23934889</idno><idno type="pmid">23934889</idno><idno type="doi">10.1534/genetics.113.154674</idno><idno type="pmc">PMC3781973</idno><idno type="wicri:Area/Main/Corpus">000F76</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000F76</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">TORC1 signaling is governed by two negative regulators in fission yeast.</title><author><name sortKey="Ma, Ning" sort="Ma, Ning" uniqKey="Ma N" first="Ning" last="Ma">Ning Ma</name><affiliation><nlm:affiliation>Division of Molecular Pharmacology and Pharmacogenomics, Department of Biochemistry and Molecular Biology, Kobe University Graduate School of Medicine, Kobe 650-0017, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Liu, Qingbin" sort="Liu, Qingbin" uniqKey="Liu Q" first="Qingbin" last="Liu">Qingbin Liu</name></author><author><name sortKey="Zhang, Lili" sort="Zhang, Lili" uniqKey="Zhang L" first="Lili" last="Zhang">Lili Zhang</name></author><author><name sortKey="Henske, Elizabeth P" sort="Henske, Elizabeth P" uniqKey="Henske E" first="Elizabeth P" last="Henske">Elizabeth P. Henske</name></author><author><name sortKey="Ma, Yan" sort="Ma, Yan" uniqKey="Ma Y" first="Yan" last="Ma">Yan Ma</name></author></analytic><series><title level="j">Genetics</title><idno type="eISSN">1943-2631</idno><imprint><date when="2013" type="published">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Amino Acid Transport Systems (metabolism)</term><term>Amino Acids (genetics)</term><term>Amino Acids (metabolism)</term><term>Cell Cycle (MeSH)</term><term>Gene Expression Regulation, Fungal (MeSH)</term><term>Mechanistic Target of Rapamycin Complex 1 (MeSH)</term><term>Multiprotein Complexes (genetics)</term><term>Multiprotein Complexes (metabolism)</term><term>Mutation (MeSH)</term><term>Receptors, Atrial Natriuretic Factor (genetics)</term><term>Schizosaccharomyces (genetics)</term><term>Schizosaccharomyces pombe Proteins (genetics)</term><term>Schizosaccharomyces pombe Proteins (metabolism)</term><term>Signal Transduction (MeSH)</term><term>TOR Serine-Threonine Kinases (genetics)</term><term>TOR Serine-Threonine Kinases (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Amino Acids</term><term>Multiprotein Complexes</term><term>Receptors, Atrial Natriuretic Factor</term><term>Schizosaccharomyces pombe Proteins</term><term>TOR Serine-Threonine Kinases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Amino Acid Transport Systems</term><term>Amino Acids</term><term>Multiprotein Complexes</term><term>Schizosaccharomyces pombe Proteins</term><term>TOR Serine-Threonine Kinases</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Schizosaccharomyces</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Cell Cycle</term><term>Gene Expression Regulation, Fungal</term><term>Mechanistic Target of Rapamycin Complex 1</term><term>Mutation</term><term>Signal Transduction</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The target of rapamycin (TOR) is a highly conserved protein kinase that regulates cell growth and metabolism. Here we performed a genome-wide screen to identify negative regulators of TOR complex 1 (TORC1) in Schizosaccharomyces pombe by isolating mutants that phenocopy Δtsc2, in which TORC1 signaling is known to be up-regulated. We discovered that Δnpr2 displayed similar phenotypes to Δtsc2 in terms of amino acid uptake defects and mislocalization of the Cat1 permease. However, Δnpr2 and Δtsc2 clearly showed different phenotypes in terms of rapamycin supersensitivity and Isp5 transcription upon various treatments. Furthermore, we showed that Tor2 controls amino acid homeostasis at the transcriptional and post-transcriptional levels. Our data reveal that both Npr2 and Tsc2 negatively regulate TORC1 signaling, and Npr2, but not Tsc2, may be involved in the feedback loop of a nutrient-sensing pathway. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23934889</PMID><DateCompleted><Year>2014</Year><Month>05</Month><Day>15</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1943-2631</ISSN><JournalIssue CitedMedium="Internet"><Volume>195</Volume><Issue>2</Issue><PubDate><Year>2013</Year><Month>Oct</Month></PubDate></JournalIssue><Title>Genetics</Title><ISOAbbreviation>Genetics</ISOAbbreviation></Journal><ArticleTitle>TORC1 signaling is governed by two negative regulators in fission yeast.</ArticleTitle><Pagination><MedlinePgn>457-68</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1534/genetics.113.154674</ELocationID><Abstract><AbstractText>The target of rapamycin (TOR) is a highly conserved protein kinase that regulates cell growth and metabolism. Here we performed a genome-wide screen to identify negative regulators of TOR complex 1 (TORC1) in Schizosaccharomyces pombe by isolating mutants that phenocopy Δtsc2, in which TORC1 signaling is known to be up-regulated. We discovered that Δnpr2 displayed similar phenotypes to Δtsc2 in terms of amino acid uptake defects and mislocalization of the Cat1 permease. However, Δnpr2 and Δtsc2 clearly showed different phenotypes in terms of rapamycin supersensitivity and Isp5 transcription upon various treatments. Furthermore, we showed that Tor2 controls amino acid homeostasis at the transcriptional and post-transcriptional levels. Our data reveal that both Npr2 and Tsc2 negatively regulate TORC1 signaling, and Npr2, but not Tsc2, may be involved in the feedback loop of a nutrient-sensing pathway. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Ma</LastName><ForeName>Ning</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Division of Molecular Pharmacology and Pharmacogenomics, Department of Biochemistry and Molecular Biology, Kobe University Graduate School of Medicine, Kobe 650-0017, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Liu</LastName><ForeName>Qingbin</ForeName><Initials>Q</Initials></Author><Author ValidYN="Y"><LastName>Zhang</LastName><ForeName>Lili</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Henske</LastName><ForeName>Elizabeth P</ForeName><Initials>EP</Initials></Author><Author ValidYN="Y"><LastName>Ma</LastName><ForeName>Yan</ForeName><Initials>Y</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2013</Year><Month>08</Month><Day>09</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Genetics</MedlineTA><NlmUniqueID>0374636</NlmUniqueID><ISSNLinking>0016-6731</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D026905">Amino Acid Transport Systems</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000596">Amino Acids</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C530694">Cat1 protein, S 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1</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D046912" MajorTopicYN="N">Multiprotein Complexes</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017461" MajorTopicYN="N">Receptors, Atrial Natriuretic Factor</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012568" MajorTopicYN="N">Schizosaccharomyces</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029702" MajorTopicYN="N">Schizosaccharomyces pombe Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" 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