The TOR nutrient signalling pathway phosphorylates NPR1 and inhibits turnover of the tryptophan permease.
Identifieur interne : 001A62 ( Main/Corpus ); précédent : 001A61; suivant : 001A63The TOR nutrient signalling pathway phosphorylates NPR1 and inhibits turnover of the tryptophan permease.
Auteurs : A. Schmidt ; T. Beck ; A. Koller ; J. Kunz ; M N HallSource :
- The EMBO journal [ 0261-4189 ] ; 1998.
English descriptors
- KwdEn :
- Adaptor Proteins, Signal Transducing (MeSH), Amino Acid Transport Systems (MeSH), Cell Cycle Proteins (MeSH), Escherichia coli Proteins (MeSH), Fungal Proteins (genetics), Fungal Proteins (metabolism), Membrane Transport Proteins (metabolism), Phosphatidylinositol 3-Kinases (MeSH), Phosphorylation (MeSH), Phosphotransferases (Alcohol Group Acceptor) (genetics), Phosphotransferases (Alcohol Group Acceptor) (metabolism), Protein Kinases (MeSH), Protein-Serine-Threonine Kinases (genetics), Protein-Serine-Threonine Kinases (metabolism), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (MeSH), Signal Transduction (MeSH).
- MESH :
- chemical , genetics : Fungal Proteins, Phosphotransferases (Alcohol Group Acceptor), Protein-Serine-Threonine Kinases.
- chemical , metabolism : Fungal Proteins, Membrane Transport Proteins, Phosphotransferases (Alcohol Group Acceptor), Protein-Serine-Threonine Kinases.
- chemical : Adaptor Proteins, Signal Transducing, Amino Acid Transport Systems, Cell Cycle Proteins, Escherichia coli Proteins, Phosphatidylinositol 3-Kinases, Protein Kinases, Saccharomyces cerevisiae Proteins.
- genetics : Saccharomyces cerevisiae.
- metabolism : Saccharomyces cerevisiae.
- Phosphorylation, Signal Transduction.
Abstract
The Saccharomyces cerevisiae targets of rapamycin, TOR1 and TOR2, signal activation of cell growth in response to nutrient availability. Loss of TOR or rapamycin treatment causes yeast cells to arrest growth in early G1 and to express several other physiological properties of starved (G0) cells. As part of this starvation response, high affinity amino acid permeases such as the tryptophan permease TAT2 are targeted to the vacuole and degraded. Here we show that the TOR signalling pathway phosphorylates the Ser/Thr kinase NPR1 and thereby inhibits the starvation-induced turnover of TAT2. Overexpression of NPR1 inhibits growth and induces the degradation of TAT2, whereas loss of NPR1 confers resistance to rapamycin and to FK506, an inhibitor of amino acid import. NPR1 is controlled by TOR and the type 2A phosphatase-associated protein TAP42. First, overexpression of NPR1 is toxic only when TOR function is reduced. Secondly, NPR1 is rapidly dephosphorylated in the absence of TOR. Thirdly, NPR1 dephosphorylation does not occur in a rapamycin-resistant tap42 mutant. Thus, the TOR nutrient signalling pathway also controls growth by inhibiting a stationary phase (G0) programme. The control of NPR1 by TOR is analogous to the control of p70 s6 kinase and 4E-BP1 by mTOR in mammalian cells.
DOI: 10.1093/emboj/17.23.6924
PubMed: 9843498
PubMed Central: PMC1171040
Links to Exploration step
pubmed:9843498Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">The TOR nutrient signalling pathway phosphorylates NPR1 and inhibits turnover of the tryptophan permease.</title><author><name sortKey="Schmidt, A" sort="Schmidt, A" uniqKey="Schmidt A" first="A" last="Schmidt">A. Schmidt</name><affiliation><nlm:affiliation>Department of Biochemistry, Biozentrum, University of Basel, CH-4056 Basel, Switzerland.</nlm:affiliation></affiliation></author><author><name sortKey="Beck, T" sort="Beck, T" uniqKey="Beck T" first="T" last="Beck">T. Beck</name></author><author><name sortKey="Koller, A" sort="Koller, A" uniqKey="Koller A" first="A" last="Koller">A. Koller</name></author><author><name sortKey="Kunz, J" sort="Kunz, J" uniqKey="Kunz J" first="J" last="Kunz">J. Kunz</name></author><author><name sortKey="Hall, M N" sort="Hall, M N" uniqKey="Hall M" first="M N" last="Hall">M N Hall</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1998">1998</date><idno type="RBID">pubmed:9843498</idno><idno type="pmid">9843498</idno><idno type="doi">10.1093/emboj/17.23.6924</idno><idno type="pmc">PMC1171040</idno><idno type="wicri:Area/Main/Corpus">001A62</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001A62</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">The TOR nutrient signalling pathway phosphorylates NPR1 and inhibits turnover of the tryptophan permease.</title><author><name sortKey="Schmidt, A" sort="Schmidt, A" uniqKey="Schmidt A" first="A" last="Schmidt">A. Schmidt</name><affiliation><nlm:affiliation>Department of Biochemistry, Biozentrum, University of Basel, CH-4056 Basel, Switzerland.</nlm:affiliation></affiliation></author><author><name sortKey="Beck, T" sort="Beck, T" uniqKey="Beck T" first="T" last="Beck">T. Beck</name></author><author><name sortKey="Koller, A" sort="Koller, A" uniqKey="Koller A" first="A" last="Koller">A. Koller</name></author><author><name sortKey="Kunz, J" sort="Kunz, J" uniqKey="Kunz J" first="J" last="Kunz">J. Kunz</name></author><author><name sortKey="Hall, M N" sort="Hall, M N" uniqKey="Hall M" first="M N" last="Hall">M N Hall</name></author></analytic><series><title level="j">The EMBO journal</title><idno type="ISSN">0261-4189</idno><imprint><date when="1998" type="published">1998</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Adaptor Proteins, Signal Transducing (MeSH)</term><term>Amino Acid Transport Systems (MeSH)</term><term>Cell Cycle Proteins (MeSH)</term><term>Escherichia coli Proteins (MeSH)</term><term>Fungal Proteins (genetics)</term><term>Fungal Proteins (metabolism)</term><term>Membrane Transport Proteins (metabolism)</term><term>Phosphatidylinositol 3-Kinases (MeSH)</term><term>Phosphorylation (MeSH)</term><term>Phosphotransferases (Alcohol Group Acceptor) (genetics)</term><term>Phosphotransferases (Alcohol Group Acceptor) (metabolism)</term><term>Protein Kinases (MeSH)</term><term>Protein-Serine-Threonine Kinases (genetics)</term><term>Protein-Serine-Threonine Kinases (metabolism)</term><term>Saccharomyces cerevisiae (genetics)</term><term>Saccharomyces cerevisiae (metabolism)</term><term>Saccharomyces cerevisiae Proteins (MeSH)</term><term>Signal Transduction (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Fungal Proteins</term><term>Phosphotransferases (Alcohol Group Acceptor)</term><term>Protein-Serine-Threonine Kinases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Fungal Proteins</term><term>Membrane Transport Proteins</term><term>Phosphotransferases (Alcohol Group Acceptor)</term><term>Protein-Serine-Threonine Kinases</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Adaptor Proteins, Signal Transducing</term><term>Amino Acid Transport Systems</term><term>Cell Cycle Proteins</term><term>Escherichia coli Proteins</term><term>Phosphatidylinositol 3-Kinases</term><term>Protein Kinases</term><term>Saccharomyces cerevisiae Proteins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Phosphorylation</term><term>Signal Transduction</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The Saccharomyces cerevisiae targets of rapamycin, TOR1 and TOR2, signal activation of cell growth in response to nutrient availability. Loss of TOR or rapamycin treatment causes yeast cells to arrest growth in early G1 and to express several other physiological properties of starved (G0) cells. As part of this starvation response, high affinity amino acid permeases such as the tryptophan permease TAT2 are targeted to the vacuole and degraded. Here we show that the TOR signalling pathway phosphorylates the Ser/Thr kinase NPR1 and thereby inhibits the starvation-induced turnover of TAT2. Overexpression of NPR1 inhibits growth and induces the degradation of TAT2, whereas loss of NPR1 confers resistance to rapamycin and to FK506, an inhibitor of amino acid import. NPR1 is controlled by TOR and the type 2A phosphatase-associated protein TAP42. First, overexpression of NPR1 is toxic only when TOR function is reduced. Secondly, NPR1 is rapidly dephosphorylated in the absence of TOR. Thirdly, NPR1 dephosphorylation does not occur in a rapamycin-resistant tap42 mutant. Thus, the TOR nutrient signalling pathway also controls growth by inhibiting a stationary phase (G0) programme. The control of NPR1 by TOR is analogous to the control of p70 s6 kinase and 4E-BP1 by mTOR in mammalian cells.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">9843498</PMID><DateCompleted><Year>1999</Year><Month>02</Month><Day>11</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0261-4189</ISSN><JournalIssue CitedMedium="Print"><Volume>17</Volume><Issue>23</Issue><PubDate><Year>1998</Year><Month>Dec</Month><Day>01</Day></PubDate></JournalIssue><Title>The EMBO journal</Title><ISOAbbreviation>EMBO J</ISOAbbreviation></Journal><ArticleTitle>The TOR nutrient signalling pathway phosphorylates NPR1 and inhibits turnover of the tryptophan permease.</ArticleTitle><Pagination><MedlinePgn>6924-31</MedlinePgn></Pagination><Abstract><AbstractText>The Saccharomyces cerevisiae targets of rapamycin, TOR1 and TOR2, signal activation of cell growth in response to nutrient availability. Loss of TOR or rapamycin treatment causes yeast cells to arrest growth in early G1 and to express several other physiological properties of starved (G0) cells. As part of this starvation response, high affinity amino acid permeases such as the tryptophan permease TAT2 are targeted to the vacuole and degraded. Here we show that the TOR signalling pathway phosphorylates the Ser/Thr kinase NPR1 and thereby inhibits the starvation-induced turnover of TAT2. Overexpression of NPR1 inhibits growth and induces the degradation of TAT2, whereas loss of NPR1 confers resistance to rapamycin and to FK506, an inhibitor of amino acid import. NPR1 is controlled by TOR and the type 2A phosphatase-associated protein TAP42. First, overexpression of NPR1 is toxic only when TOR function is reduced. Secondly, NPR1 is rapidly dephosphorylated in the absence of TOR. Thirdly, NPR1 dephosphorylation does not occur in a rapamycin-resistant tap42 mutant. Thus, the TOR nutrient signalling pathway also controls growth by inhibiting a stationary phase (G0) programme. The control of NPR1 by TOR is analogous to the control of p70 s6 kinase and 4E-BP1 by mTOR in mammalian cells.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Schmidt</LastName><ForeName>A</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, Biozentrum, University of Basel, CH-4056 Basel, Switzerland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Beck</LastName><ForeName>T</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Koller</LastName><ForeName>A</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Kunz</LastName><ForeName>J</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Hall</LastName><ForeName>M N</ForeName><Initials>MN</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. 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2.7.1.-</RegistryNumber><NameOfSubstance UI="D017853">Phosphotransferases (Alcohol Group Acceptor)</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.1.137</RegistryNumber><NameOfSubstance UI="C083324">TOR1 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.1.137</RegistryNumber><NameOfSubstance UI="C081135">TOR2 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="D048868" MajorTopicYN="N">Adaptor Proteins, Signal Transducing</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D026905" MajorTopicYN="Y">Amino Acid Transport Systems</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018797" MajorTopicYN="N">Cell Cycle Proteins</DescriptorName></MeshHeading><MeshHeading><DescriptorName 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