TOR signaling is a determinant of cell survival in response to DNA damage.
Identifieur interne : 001676 ( Main/Exploration ); précédent : 001675; suivant : 001677TOR signaling is a determinant of cell survival in response to DNA damage.
Auteurs : Changxian Shen [États-Unis] ; Cynthia S. Lancaster ; Bin Shi ; Hong Guo ; Padma Thimmaiah ; Mary-Ann BjornstiSource :
- Molecular and cellular biology [ 0270-7306 ] ; 2007.
Descripteurs français
- KwdFr :
- Adulte (MeSH), Altération de l'ADN (MeSH), Checkpoint kinase 2 (MeSH), Complexes multiprotéiques (MeSH), Cycloheximide (métabolisme), Facteurs de transcription (génétique), Facteurs de transcription (métabolisme), Humains (MeSH), Mutagènes (métabolisme), Méthanesulfonate de méthyle (métabolisme), Phase S (physiologie), Protein-Serine-Threonine Kinases (génétique), Protein-Serine-Threonine Kinases (métabolisme), Protéines de Saccharomyces cerevisiae (génétique), Protéines de Saccharomyces cerevisiae (métabolisme), Protéines du cycle cellulaire (génétique), Protéines du cycle cellulaire (métabolisme), Ribonucleoside diphosphate reductase (génétique), Ribonucleoside diphosphate reductase (métabolisme), Saccharomyces cerevisiae (cytologie), Saccharomyces cerevisiae (génétique), Saccharomyces cerevisiae (métabolisme), Sirolimus (métabolisme), Sous-unités de protéines (génétique), Sous-unités de protéines (métabolisme), Survie cellulaire (MeSH), Transduction du signal (physiologie).
- MESH :
- cytologie : Saccharomyces cerevisiae.
- génétique : Facteurs de transcription, Protein-Serine-Threonine Kinases, Protéines de Saccharomyces cerevisiae, Protéines du cycle cellulaire, Ribonucleoside diphosphate reductase, Saccharomyces cerevisiae, Sous-unités de protéines.
- métabolisme : Cycloheximide, Facteurs de transcription, Mutagènes, Méthanesulfonate de méthyle, Protein-Serine-Threonine Kinases, Protéines de Saccharomyces cerevisiae, Protéines du cycle cellulaire, Ribonucleoside diphosphate reductase, Saccharomyces cerevisiae, Sirolimus, Sous-unités de protéines.
- physiologie : Phase S, Transduction du signal.
- Adulte, Altération de l'ADN, Checkpoint kinase 2, Complexes multiprotéiques, Humains, Survie cellulaire.
English descriptors
- KwdEn :
- Adult (MeSH), Cell Cycle Proteins (genetics), Cell Cycle Proteins (metabolism), Cell Survival (MeSH), Checkpoint Kinase 2 (MeSH), Cycloheximide (metabolism), DNA Damage (MeSH), Humans (MeSH), Methyl Methanesulfonate (metabolism), Multiprotein Complexes (MeSH), Mutagens (metabolism), Protein Subunits (genetics), Protein Subunits (metabolism), Protein-Serine-Threonine Kinases (genetics), Protein-Serine-Threonine Kinases (metabolism), Ribonucleoside Diphosphate Reductase (genetics), Ribonucleoside Diphosphate Reductase (metabolism), S Phase (physiology), Saccharomyces cerevisiae (cytology), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism), Signal Transduction (physiology), Sirolimus (metabolism), Transcription Factors (genetics), Transcription Factors (metabolism).
- MESH :
- chemical , genetics : Cell Cycle Proteins, Protein Subunits, Protein-Serine-Threonine Kinases, Ribonucleoside Diphosphate Reductase, Saccharomyces cerevisiae Proteins, Transcription Factors.
- chemical , metabolism : Cell Cycle Proteins, Cycloheximide, Methyl Methanesulfonate, Mutagens, Protein Subunits, Protein-Serine-Threonine Kinases, Ribonucleoside Diphosphate Reductase, Saccharomyces cerevisiae Proteins, Sirolimus, Transcription Factors.
- cytology : Saccharomyces cerevisiae.
- genetics : Saccharomyces cerevisiae.
- metabolism : Saccharomyces cerevisiae.
- physiology : S Phase, Signal Transduction.
- Adult, Cell Survival, Checkpoint Kinase 2, DNA Damage, Humans, Multiprotein Complexes.
Abstract
The conserved TOR (target of rapamycin) kinase is part of a TORC1 complex that regulates cellular responses to environmental stress, such as amino acid starvation and hypoxia. Dysregulation of Akt-TOR signaling has also been linked to the genesis of cancer, and thus, this pathway presents potential targets for cancer chemotherapeutics. Here we report that rapamycin-sensitive TORC1 signaling is required for the S-phase progression and viability of yeast cells in response to genotoxic stress. In the presence of the DNA-damaging agent methyl methanesulfonate (MMS), TOR-dependent cell survival required a functional S-phase checkpoint. Rapamycin inhibition of TORC1 signaling suppressed the Rad53 checkpoint-mediated induction of ribonucleotide reductase subunits Rnr1 and Rnr3, thereby abrogating MMS-induced mutagenesis and enhancing cell lethality. Moreover, cells deleted for RNR3 were hypersensitive to rapamycin plus MMS, providing the first demonstration that Rnr3 contributes to the survival of cells exposed to DNA damage. Our findings support a model whereby TORC1 acts as a survival pathway in response to genotoxic stress by maintaining the deoxynucleoside triphosphate pools necessary for error-prone translesion DNA polymerases. Thus, TOR-dependent cell survival in response to DNA-damaging agents coincides with increased mutation rates, which may contribute to the acquisition of chemotherapeutic drug resistance.
DOI: 10.1128/MCB.00290-07
PubMed: 17698581
PubMed Central: PMC2168917
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Kinase 2 (MeSH)</term><term>Cycloheximide (metabolism)</term><term>DNA Damage (MeSH)</term><term>Humans (MeSH)</term><term>Methyl Methanesulfonate (metabolism)</term><term>Multiprotein Complexes (MeSH)</term><term>Mutagens (metabolism)</term><term>Protein Subunits (genetics)</term><term>Protein Subunits (metabolism)</term><term>Protein-Serine-Threonine Kinases (genetics)</term><term>Protein-Serine-Threonine Kinases (metabolism)</term><term>Ribonucleoside Diphosphate Reductase (genetics)</term><term>Ribonucleoside Diphosphate Reductase (metabolism)</term><term>S Phase (physiology)</term><term>Saccharomyces cerevisiae (cytology)</term><term>Saccharomyces cerevisiae (genetics)</term><term>Saccharomyces cerevisiae (metabolism)</term><term>Saccharomyces cerevisiae Proteins (genetics)</term><term>Saccharomyces cerevisiae Proteins (metabolism)</term><term>Signal Transduction (physiology)</term><term>Sirolimus (metabolism)</term><term>Transcription Factors (genetics)</term><term>Transcription Factors (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Adulte (MeSH)</term><term>Altération de l'ADN (MeSH)</term><term>Checkpoint kinase 2 (MeSH)</term><term>Complexes multiprotéiques (MeSH)</term><term>Cycloheximide (métabolisme)</term><term>Facteurs de transcription (génétique)</term><term>Facteurs de transcription (métabolisme)</term><term>Humains (MeSH)</term><term>Mutagènes (métabolisme)</term><term>Méthanesulfonate de méthyle (métabolisme)</term><term>Phase S (physiologie)</term><term>Protein-Serine-Threonine Kinases (génétique)</term><term>Protein-Serine-Threonine Kinases (métabolisme)</term><term>Protéines de Saccharomyces cerevisiae (génétique)</term><term>Protéines de Saccharomyces cerevisiae (métabolisme)</term><term>Protéines du cycle cellulaire (génétique)</term><term>Protéines du cycle cellulaire (métabolisme)</term><term>Ribonucleoside diphosphate reductase (génétique)</term><term>Ribonucleoside diphosphate reductase (métabolisme)</term><term>Saccharomyces cerevisiae (cytologie)</term><term>Saccharomyces cerevisiae (génétique)</term><term>Saccharomyces cerevisiae (métabolisme)</term><term>Sirolimus (métabolisme)</term><term>Sous-unités de protéines (génétique)</term><term>Sous-unités de protéines (métabolisme)</term><term>Survie cellulaire (MeSH)</term><term>Transduction du signal (physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Cell Cycle Proteins</term><term>Protein Subunits</term><term>Protein-Serine-Threonine Kinases</term><term>Ribonucleoside Diphosphate Reductase</term><term>Saccharomyces cerevisiae Proteins</term><term>Transcription Factors</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cell Cycle Proteins</term><term>Cycloheximide</term><term>Methyl Methanesulfonate</term><term>Mutagens</term><term>Protein Subunits</term><term>Protein-Serine-Threonine Kinases</term><term>Ribonucleoside Diphosphate Reductase</term><term>Saccharomyces cerevisiae Proteins</term><term>Sirolimus</term><term>Transcription Factors</term></keywords><keywords scheme="MESH" qualifier="cytologie" xml:lang="fr"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Facteurs de transcription</term><term>Protein-Serine-Threonine Kinases</term><term>Protéines de Saccharomyces cerevisiae</term><term>Protéines du cycle cellulaire</term><term>Ribonucleoside diphosphate reductase</term><term>Saccharomyces cerevisiae</term><term>Sous-unités de protéines</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cycloheximide</term><term>Facteurs de transcription</term><term>Mutagènes</term><term>Méthanesulfonate de méthyle</term><term>Protein-Serine-Threonine Kinases</term><term>Protéines de Saccharomyces cerevisiae</term><term>Protéines du cycle cellulaire</term><term>Ribonucleoside diphosphate reductase</term><term>Saccharomyces cerevisiae</term><term>Sirolimus</term><term>Sous-unités de protéines</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Phase S</term><term>Transduction du signal</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>S Phase</term><term>Signal Transduction</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Adult</term><term>Cell Survival</term><term>Checkpoint Kinase 2</term><term>DNA Damage</term><term>Humans</term><term>Multiprotein Complexes</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Adulte</term><term>Altération de l'ADN</term><term>Checkpoint kinase 2</term><term>Complexes multiprotéiques</term><term>Humains</term><term>Survie cellulaire</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The conserved TOR (target of rapamycin) kinase is part of a TORC1 complex that regulates cellular responses to environmental stress, such as amino acid starvation and hypoxia. Dysregulation of Akt-TOR signaling has also been linked to the genesis of cancer, and thus, this pathway presents potential targets for cancer chemotherapeutics. Here we report that rapamycin-sensitive TORC1 signaling is required for the S-phase progression and viability of yeast cells in response to genotoxic stress. In the presence of the DNA-damaging agent methyl methanesulfonate (MMS), TOR-dependent cell survival required a functional S-phase checkpoint. Rapamycin inhibition of TORC1 signaling suppressed the Rad53 checkpoint-mediated induction of ribonucleotide reductase subunits Rnr1 and Rnr3, thereby abrogating MMS-induced mutagenesis and enhancing cell lethality. Moreover, cells deleted for RNR3 were hypersensitive to rapamycin plus MMS, providing the first demonstration that Rnr3 contributes to the survival of cells exposed to DNA damage. Our findings support a model whereby TORC1 acts as a survival pathway in response to genotoxic stress by maintaining the deoxynucleoside triphosphate pools necessary for error-prone translesion DNA polymerases. Thus, TOR-dependent cell survival in response to DNA-damaging agents coincides with increased mutation rates, which may contribute to the acquisition of chemotherapeutic drug resistance.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17698581</PMID><DateCompleted><Year>2008</Year><Month>02</Month><Day>15</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0270-7306</ISSN><JournalIssue CitedMedium="Print"><Volume>27</Volume><Issue>20</Issue><PubDate><Year>2007</Year><Month>Oct</Month></PubDate></JournalIssue><Title>Molecular and cellular biology</Title><ISOAbbreviation>Mol Cell Biol</ISOAbbreviation></Journal><ArticleTitle>TOR signaling is a determinant of cell survival in response to DNA damage.</ArticleTitle><Pagination><MedlinePgn>7007-17</MedlinePgn></Pagination><Abstract><AbstractText>The conserved TOR (target of rapamycin) kinase is part of a TORC1 complex that regulates cellular responses to environmental stress, such as amino acid starvation and hypoxia. Dysregulation of Akt-TOR signaling has also been linked to the genesis of cancer, and thus, this pathway presents potential targets for cancer chemotherapeutics. Here we report that rapamycin-sensitive TORC1 signaling is required for the S-phase progression and viability of yeast cells in response to genotoxic stress. In the presence of the DNA-damaging agent methyl methanesulfonate (MMS), TOR-dependent cell survival required a functional S-phase checkpoint. Rapamycin inhibition of TORC1 signaling suppressed the Rad53 checkpoint-mediated induction of ribonucleotide reductase subunits Rnr1 and Rnr3, thereby abrogating MMS-induced mutagenesis and enhancing cell lethality. Moreover, cells deleted for RNR3 were hypersensitive to rapamycin plus MMS, providing the first demonstration that Rnr3 contributes to the survival of cells exposed to DNA damage. Our findings support a model whereby TORC1 acts as a survival pathway in response to genotoxic stress by maintaining the deoxynucleoside triphosphate pools necessary for error-prone translesion DNA polymerases. Thus, TOR-dependent cell survival in response to DNA-damaging agents coincides with increased mutation rates, which may contribute to the acquisition of chemotherapeutic drug resistance.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Shen</LastName><ForeName>Changxian</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Department of Molecular Pharmacology, St. Jude Children's Research Hospital, 332 N. Lauderdale, Memphis, TN 38105, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lancaster</LastName><ForeName>Cynthia S</ForeName><Initials>CS</Initials></Author><Author ValidYN="Y"><LastName>Shi</LastName><ForeName>Bin</ForeName><Initials>B</Initials></Author><Author ValidYN="Y"><LastName>Guo</LastName><ForeName>Hong</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Thimmaiah</LastName><ForeName>Padma</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Bjornsti</LastName><ForeName>Mary-Ann</ForeName><Initials>MA</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>P01 CA023099</GrantID><Acronym>CA</Acronym><Agency>NCI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>P30 CA021765</GrantID><Acronym>CA</Acronym><Agency>NCI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>CA21765</GrantID><Acronym>CA</Acronym><Agency>NCI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>CA23099</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>2007</Year><Month>08</Month><Day>13</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="D018797">Cell Cycle Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D046912">Multiprotein Complexes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009153">Mutagens</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D021122">Protein Subunits</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014157">Transcription Factors</NameOfSubstance></Chemical><Chemical><RegistryNumber>98600C0908</RegistryNumber><NameOfSubstance UI="D003513">Cycloheximide</NameOfSubstance></Chemical><Chemical><RegistryNumber>AT5C31J09G</RegistryNumber><NameOfSubstance UI="D008741">Methyl Methanesulfonate</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.17.4.1</RegistryNumber><NameOfSubstance UI="C517042">RNR3 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.17.4.1</RegistryNumber><NameOfSubstance UI="D012262">Ribonucleoside Diphosphate Reductase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.1.11</RegistryNumber><NameOfSubstance UI="D064447">Checkpoint Kinase 2</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber><NameOfSubstance UI="D017346">Protein-Serine-Threonine Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber><NameOfSubstance UI="C500749">target of rapamycin protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.12.1</RegistryNumber><NameOfSubstance UI="C067022">RAD53 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>W36ZG6FT64</RegistryNumber><NameOfSubstance UI="D020123">Sirolimus</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000328" MajorTopicYN="N">Adult</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018797" MajorTopicYN="N">Cell 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MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016196" MajorTopicYN="N">S Phase</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000166" MajorTopicYN="N">cytology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">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="N">Signal Transduction</DescriptorName><QualifierName UI="Q000502" 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Lancaster</name><name sortKey="Shi, Bin" sort="Shi, Bin" uniqKey="Shi B" first="Bin" last="Shi">Bin Shi</name><name sortKey="Thimmaiah, Padma" sort="Thimmaiah, Padma" uniqKey="Thimmaiah P" first="Padma" last="Thimmaiah">Padma Thimmaiah</name></noCountry><country name="États-Unis"><region name="Tennessee"><name sortKey="Shen, Changxian" sort="Shen, Changxian" uniqKey="Shen C" first="Changxian" last="Shen">Changxian Shen</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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