Isp7 is a novel regulator of amino acid uptake in the TOR signaling pathway.
Identifieur interne : 000E53 ( Main/Exploration ); précédent : 000E52; suivant : 000E54Isp7 is a novel regulator of amino acid uptake in the TOR signaling pathway.
Auteurs : Dana Laor [Israël] ; Adiel Cohen ; Metsada Pasmanik-Chor ; Varda Oron-Karni ; Martin Kupiec ; Ronit WeismanSource :
- Molecular and cellular biology [ 1098-5549 ] ; 2014.
Descripteurs français
- KwdFr :
- Acides aminés (métabolisme), Complexe-2 cible mécanistique de la rapamycine (MeSH), Complexes multiprotéiques (métabolisme), Mutation (effets des médicaments et des substances chimiques), Mutation (génétique), Phosphorylation (effets des médicaments et des substances chimiques), Phosphorylation (génétique), Protein kinases (métabolisme), Protein-Serine-Threonine Kinases (métabolisme), Protéines de Schizosaccharomyces pombe (génétique), Protéines de Schizosaccharomyces pombe (métabolisme), Schizosaccharomyces (effets des médicaments et des substances chimiques), Schizosaccharomyces (génétique), Schizosaccharomyces (métabolisme), Sirolimus (pharmacologie), Systèmes de transport d'acides aminés (métabolisme), Sérine-thréonine kinases TOR (métabolisme), Transcriptome (effets des médicaments et des substances chimiques), Transcriptome (génétique), Transduction du signal (effets des médicaments et des substances chimiques), Transduction du signal (génétique).
- MESH :
- effets des médicaments et des substances chimiques : Mutation, Phosphorylation, Schizosaccharomyces, Transcriptome, Transduction du signal.
- génétique : Mutation, Phosphorylation, Protéines de Schizosaccharomyces pombe, Schizosaccharomyces, Transcriptome, Transduction du signal.
- métabolisme : Acides aminés, Complexes multiprotéiques, Protein kinases, Protein-Serine-Threonine Kinases, Protéines de Schizosaccharomyces pombe, Schizosaccharomyces, Systèmes de transport d'acides aminés, Sérine-thréonine kinases TOR.
- pharmacologie : Sirolimus.
- Complexe-2 cible mécanistique de la rapamycine.
English descriptors
- KwdEn :
- Amino Acid Transport Systems (metabolism), Amino Acids (metabolism), Mechanistic Target of Rapamycin Complex 2 (MeSH), Multiprotein Complexes (metabolism), Mutation (drug effects), Mutation (genetics), Phosphorylation (drug effects), Phosphorylation (genetics), Protein Kinases (metabolism), Protein-Serine-Threonine Kinases (metabolism), Schizosaccharomyces (drug effects), Schizosaccharomyces (genetics), Schizosaccharomyces (metabolism), Schizosaccharomyces pombe Proteins (genetics), Schizosaccharomyces pombe Proteins (metabolism), Signal Transduction (drug effects), Signal Transduction (genetics), Sirolimus (pharmacology), TOR Serine-Threonine Kinases (metabolism), Transcriptome (drug effects), Transcriptome (genetics).
- MESH :
- chemical , genetics : Schizosaccharomyces pombe Proteins.
- chemical , metabolism : Amino Acid Transport Systems, Amino Acids, Multiprotein Complexes, Protein Kinases, Protein-Serine-Threonine Kinases, Schizosaccharomyces pombe Proteins, TOR Serine-Threonine Kinases.
- chemical , pharmacology : Sirolimus.
- chemical : Mechanistic Target of Rapamycin Complex 2.
- drug effects : Mutation, Phosphorylation, Schizosaccharomyces, Signal Transduction, Transcriptome.
- genetics : Mutation, Phosphorylation, Schizosaccharomyces, Signal Transduction, Transcriptome.
- metabolism : Schizosaccharomyces.
Abstract
TOR proteins reside in two distinct complexes, TOR complexes 1 and 2 (TORC1 and TORC2), that are central for the regulation of cellular growth, proliferation, and survival. TOR is also the target for the immunosuppressive and anticancer drug rapamycin. In Schizosaccharomyces pombe, disruption of the TSC complex, mutations in which can lead to the tuberous sclerosis syndrome in humans, results in a rapamycin-sensitive phenotype under poor nitrogen conditions. We show here that the sensitivity to rapamycin is mediated via inhibition of TORC1 and suppressed by overexpression of isp7(+), a member of the family of 2-oxoglutarate-Fe(II)-dependent oxygenase genes. The transcript level of isp7(+) is negatively regulated by TORC1 but positively regulated by TORC2. Yet we find extensive similarity between the transcriptome of cells disrupted for isp7(+) and cells mutated in the catalytic subunit of TORC1. Moreover, Isp7 regulates amino acid permease expression in a fashion similar to that of TORC1 and opposite that of TORC2. Overexpression of isp7(+) induces TORC1-dependent phosphorylation of ribosomal protein Rps6 while inhibiting TORC2-dependent phosphorylation and activation of the AGC-like kinase Gad8. Taken together, our findings suggest a central role for Isp7 in amino acid homeostasis and the presence of isp7(+)-dependent regulatory loops that affect both TORC1 and TORC2.
DOI: 10.1128/MCB.01473-13
PubMed: 24344203
PubMed Central: PMC4023818
Affiliations:
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(genetics)</term><term>Phosphorylation (drug effects)</term><term>Phosphorylation (genetics)</term><term>Protein Kinases (metabolism)</term><term>Protein-Serine-Threonine Kinases (metabolism)</term><term>Schizosaccharomyces (drug effects)</term><term>Schizosaccharomyces (genetics)</term><term>Schizosaccharomyces (metabolism)</term><term>Schizosaccharomyces pombe Proteins (genetics)</term><term>Schizosaccharomyces pombe Proteins (metabolism)</term><term>Signal Transduction (drug effects)</term><term>Signal Transduction (genetics)</term><term>Sirolimus (pharmacology)</term><term>TOR Serine-Threonine Kinases (metabolism)</term><term>Transcriptome (drug effects)</term><term>Transcriptome (genetics)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acides aminés (métabolisme)</term><term>Complexe-2 cible mécanistique de la rapamycine (MeSH)</term><term>Complexes multiprotéiques (métabolisme)</term><term>Mutation (effets des médicaments et des substances 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(génétique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Schizosaccharomyces pombe Proteins</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>Protein Kinases</term><term>Protein-Serine-Threonine Kinases</term><term>Schizosaccharomyces pombe Proteins</term><term>TOR Serine-Threonine 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>Mechanistic Target of Rapamycin Complex 2</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Mutation</term><term>Phosphorylation</term><term>Schizosaccharomyces</term><term>Signal Transduction</term><term>Transcriptome</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Mutation</term><term>Phosphorylation</term><term>Schizosaccharomyces</term><term>Transcriptome</term><term>Transduction du signal</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Mutation</term><term>Phosphorylation</term><term>Schizosaccharomyces</term><term>Signal Transduction</term><term>Transcriptome</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Mutation</term><term>Phosphorylation</term><term>Protéines de Schizosaccharomyces pombe</term><term>Schizosaccharomyces</term><term>Transcriptome</term><term>Transduction du signal</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Schizosaccharomyces</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Acides aminés</term><term>Complexes multiprotéiques</term><term>Protein kinases</term><term>Protein-Serine-Threonine Kinases</term><term>Protéines de Schizosaccharomyces pombe</term><term>Schizosaccharomyces</term><term>Systèmes de transport d'acides aminés</term><term>Sérine-thréonine kinases TOR</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Sirolimus</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Complexe-2 cible mécanistique de la rapamycine</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">TOR proteins reside in two distinct complexes, TOR complexes 1 and 2 (TORC1 and TORC2), that are central for the regulation of cellular growth, proliferation, and survival. TOR is also the target for the immunosuppressive and anticancer drug rapamycin. In Schizosaccharomyces pombe, disruption of the TSC complex, mutations in which can lead to the tuberous sclerosis syndrome in humans, results in a rapamycin-sensitive phenotype under poor nitrogen conditions. We show here that the sensitivity to rapamycin is mediated via inhibition of TORC1 and suppressed by overexpression of isp7(+), a member of the family of 2-oxoglutarate-Fe(II)-dependent oxygenase genes. The transcript level of isp7(+) is negatively regulated by TORC1 but positively regulated by TORC2. Yet we find extensive similarity between the transcriptome of cells disrupted for isp7(+) and cells mutated in the catalytic subunit of TORC1. Moreover, Isp7 regulates amino acid permease expression in a fashion similar to that of TORC1 and opposite that of TORC2. Overexpression of isp7(+) induces TORC1-dependent phosphorylation of ribosomal protein Rps6 while inhibiting TORC2-dependent phosphorylation and activation of the AGC-like kinase Gad8. Taken together, our findings suggest a central role for Isp7 in amino acid homeostasis and the presence of isp7(+)-dependent regulatory loops that affect both TORC1 and TORC2. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24344203</PMID><DateCompleted><Year>2014</Year><Month>04</Month><Day>24</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1098-5549</ISSN><JournalIssue CitedMedium="Internet"><Volume>34</Volume><Issue>5</Issue><PubDate><Year>2014</Year><Month>Mar</Month></PubDate></JournalIssue><Title>Molecular and cellular biology</Title><ISOAbbreviation>Mol Cell Biol</ISOAbbreviation></Journal><ArticleTitle>Isp7 is a novel regulator of amino acid uptake in the TOR signaling pathway.</ArticleTitle><Pagination><MedlinePgn>794-806</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1128/MCB.01473-13</ELocationID><Abstract><AbstractText>TOR proteins reside in two distinct complexes, TOR complexes 1 and 2 (TORC1 and TORC2), that are central for the regulation of cellular growth, proliferation, and survival. TOR is also the target for the immunosuppressive and anticancer drug rapamycin. In Schizosaccharomyces pombe, disruption of the TSC complex, mutations in which can lead to the tuberous sclerosis syndrome in humans, results in a rapamycin-sensitive phenotype under poor nitrogen conditions. We show here that the sensitivity to rapamycin is mediated via inhibition of TORC1 and suppressed by overexpression of isp7(+), a member of the family of 2-oxoglutarate-Fe(II)-dependent oxygenase genes. The transcript level of isp7(+) is negatively regulated by TORC1 but positively regulated by TORC2. Yet we find extensive similarity between the transcriptome of cells disrupted for isp7(+) and cells mutated in the catalytic subunit of TORC1. Moreover, Isp7 regulates amino acid permease expression in a fashion similar to that of TORC1 and opposite that of TORC2. Overexpression of isp7(+) induces TORC1-dependent phosphorylation of ribosomal protein Rps6 while inhibiting TORC2-dependent phosphorylation and activation of the AGC-like kinase Gad8. Taken together, our findings suggest a central role for Isp7 in amino acid homeostasis and the presence of isp7(+)-dependent regulatory loops that affect both TORC1 and TORC2. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Laor</LastName><ForeName>Dana</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Department of Molecular Microbiology and Biotechnology, Tel Aviv University, Tel Aviv, Israel.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cohen</LastName><ForeName>Adiel</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Pasmanik-Chor</LastName><ForeName>Metsada</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Oron-Karni</LastName><ForeName>Varda</ForeName><Initials>V</Initials></Author><Author ValidYN="Y"><LastName>Kupiec</LastName><ForeName>Martin</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Weisman</LastName><ForeName>Ronit</ForeName><Initials>R</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>12</Month><Day>16</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Mol Cell Biol</MedlineTA><NlmUniqueID>8109087</NlmUniqueID><ISSNLinking>0270-7306</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="D046912">Multiprotein Complexes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029702">Schizosaccharomyces pombe Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C090610">isp7 protein, S pombe</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.-</RegistryNumber><NameOfSubstance UI="D011494">Protein Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.1.-</RegistryNumber><NameOfSubstance UI="C523461">Tor1 protein, S pombe</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="C476401">Gad8 protein, S pombe</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber><NameOfSubstance UI="D000076225">Mechanistic Target of Rapamycin Complex 2</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber><NameOfSubstance UI="D017346">Protein-Serine-Threonine Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>W36ZG6FT64</RegistryNumber><NameOfSubstance UI="D020123">Sirolimus</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CommentsCorrectionsList><CommentsCorrections RefType="ErratumIn"><RefSource>Mol Cell Biol. 2014 Apr;34(8):1535</RefSource></CommentsCorrections></CommentsCorrectionsList><MeshHeadingList><MeshHeading><DescriptorName UI="D026905" MajorTopicYN="N">Amino Acid Transport Systems</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000596" MajorTopicYN="N">Amino Acids</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></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="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010766" MajorTopicYN="N">Phosphorylation</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011494" MajorTopicYN="N">Protein Kinases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017346" MajorTopicYN="N">Protein-Serine-Threonine Kinases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012568" MajorTopicYN="N">Schizosaccharomyces</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029702" MajorTopicYN="N">Schizosaccharomyces pombe Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015398" MajorTopicYN="N">Signal Transduction</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020123" MajorTopicYN="N">Sirolimus</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D058570" MajorTopicYN="N">TOR Serine-Threonine Kinases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D059467" MajorTopicYN="N">Transcriptome</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2013</Year><Month>12</Month><Day>18</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2013</Year><Month>12</Month><Day>18</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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IdType="pubmed">17535257</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>Israël</li></country></list><tree><noCountry><name sortKey="Cohen, Adiel" sort="Cohen, Adiel" uniqKey="Cohen A" first="Adiel" last="Cohen">Adiel Cohen</name><name sortKey="Kupiec, Martin" sort="Kupiec, Martin" uniqKey="Kupiec M" first="Martin" last="Kupiec">Martin Kupiec</name><name sortKey="Oron Karni, Varda" sort="Oron Karni, Varda" uniqKey="Oron Karni V" first="Varda" last="Oron-Karni">Varda Oron-Karni</name><name sortKey="Pasmanik Chor, Metsada" sort="Pasmanik Chor, Metsada" uniqKey="Pasmanik Chor M" first="Metsada" last="Pasmanik-Chor">Metsada Pasmanik-Chor</name><name sortKey="Weisman, Ronit" sort="Weisman, Ronit" uniqKey="Weisman R" first="Ronit" last="Weisman">Ronit Weisman</name></noCountry><country name="Israël"><noRegion><name sortKey="Laor, Dana" sort="Laor, Dana" uniqKey="Laor D" first="Dana" last="Laor">Dana 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