Novel insights into TOR signalling in Saccharomyces cerevisiae through Torin2.
Identifieur interne : 000536 ( Main/Exploration ); précédent : 000535; suivant : 000537Novel insights into TOR signalling in Saccharomyces cerevisiae through Torin2.
Auteurs : Pavan Kumar [Inde] ; Ankita Awasthi [Inde] ; Vikrant Nain [Inde] ; Biju Issac [États-Unis] ; Rekha Puria [Inde]Source :
- Gene [ 1879-0038 ] ; 2018.
Descripteurs français
- KwdFr :
- Calcineurine (métabolisme), Division cellulaire (effets des médicaments et des substances chimiques), Fer (toxicité), Inhibiteurs de protéines kinases (pharmacologie), Naphtyridines (pharmacologie), Protein-Serine-Threonine Kinases (antagonistes et inhibiteurs), Protein-Serine-Threonine Kinases (métabolisme), Protéines de Saccharomyces cerevisiae (antagonistes et inhibiteurs), Protéines de Saccharomyces cerevisiae (métabolisme), Saccharomyces cerevisiae (croissance et développement), Saccharomyces cerevisiae (effets des médicaments et des substances chimiques), Saccharomyces cerevisiae (enzymologie), Saccharomyces cerevisiae (génétique), Transcription génétique (effets des médicaments et des substances chimiques), Transduction du signal (effets des médicaments et des substances chimiques).
- MESH :
- antagonistes et inhibiteurs : Protein-Serine-Threonine Kinases, Protéines de Saccharomyces cerevisiae.
- croissance et développement : Saccharomyces cerevisiae.
- effets des médicaments et des substances chimiques : Division cellulaire, Saccharomyces cerevisiae, Transcription génétique, Transduction du signal.
- enzymologie : Saccharomyces cerevisiae.
- génétique : Saccharomyces cerevisiae.
- métabolisme : Calcineurine, Protein-Serine-Threonine Kinases, Protéines de Saccharomyces cerevisiae.
- pharmacologie : Inhibiteurs de protéines kinases, Naphtyridines.
- toxicité : Fer.
English descriptors
- KwdEn :
- Calcineurin (metabolism), Cell Division (drug effects), Iron (toxicity), Naphthyridines (pharmacology), Protein Kinase Inhibitors (pharmacology), Protein-Serine-Threonine Kinases (antagonists & inhibitors), Protein-Serine-Threonine Kinases (metabolism), Saccharomyces cerevisiae (drug effects), Saccharomyces cerevisiae (enzymology), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (growth & development), Saccharomyces cerevisiae Proteins (antagonists & inhibitors), Saccharomyces cerevisiae Proteins (metabolism), Signal Transduction (drug effects), Transcription, Genetic (drug effects).
- MESH :
- chemical , antagonists & inhibitors : Protein-Serine-Threonine Kinases, Saccharomyces cerevisiae Proteins.
- chemical , metabolism : Calcineurin, Protein-Serine-Threonine Kinases, Saccharomyces cerevisiae Proteins.
- drug effects : Cell Division, Saccharomyces cerevisiae, Signal Transduction, Transcription, Genetic.
- enzymology : Saccharomyces cerevisiae.
- genetics : Saccharomyces cerevisiae.
- growth & development : Saccharomyces cerevisiae.
- chemical , pharmacology : Naphthyridines, Protein Kinase Inhibitors.
- chemical , toxicity : Iron.
Abstract
Target of rapamycin (TOR) regulates cellular homeostasis by coordinating cellular growth pathways in response to different environmental signals. Rapamycin, an allosteric TOR complex 1 (TORC1) inhibitor, has proven to be invaluable for elucidating various aspects of the TOR signalling pathway; however, its applications are limited due to its inability to completely suppress TORC2. In the present study, we examined the effects of a newly discovered potent TOR inhibitor, Torin2, which inhibits both TORC1 and TORC2, on Saccharomyces cerevisiae growth. Genome-scale expression profiling of Torin2 treated yeast cells showed an expression profile similar to that of other TOR inhibitors such as rapamycin and caffeine. Distinct inhibition of cell growth by Torin2 treatment is indicated by the fact that a smaller number of transcripts are altered, compared to the changes after rapamycin and caffeine treatments. Our results revealed that Torin2 leads to increased expression of the calcineurin pathway genes favouring a synergistic therapeutic response of Torin2 in combination with calcineurin inhibitors. Further, Torin2 causes defective bud site selection during asymmetric cell division, indicating a role of TOR signalling in regulation of the budding pattern. Torin2 treated yeast cells exhibit increased expression of metalloreductases which affects iron homeostasis leading to iron toxicity. Notably, the enhanced expression of TOR1 and TOR2 rescue the Torin2 augmented iron toxicity of yeast cell. This study has revealed novel conduits and our results suggest that using Torin2 will enable the dissection of TORC2 mediated functions of the TOR signalling pathway.
DOI: 10.1016/j.gene.2018.05.081
PubMed: 29800736
Affiliations:
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Rapamycin, an allosteric TOR complex 1 (TORC1) inhibitor, has proven to be invaluable for elucidating various aspects of the TOR signalling pathway; however, its applications are limited due to its inability to completely suppress TORC2. In the present study, we examined the effects of a newly discovered potent TOR inhibitor, Torin2, which inhibits both TORC1 and TORC2, on Saccharomyces cerevisiae growth. Genome-scale expression profiling of Torin2 treated yeast cells showed an expression profile similar to that of other TOR inhibitors such as rapamycin and caffeine. Distinct inhibition of cell growth by Torin2 treatment is indicated by the fact that a smaller number of transcripts are altered, compared to the changes after rapamycin and caffeine treatments. Our results revealed that Torin2 leads to increased expression of the calcineurin pathway genes favouring a synergistic therapeutic response of Torin2 in combination with calcineurin inhibitors. Further, Torin2 causes defective bud site selection during asymmetric cell division, indicating a role of TOR signalling in regulation of the budding pattern. Torin2 treated yeast cells exhibit increased expression of metalloreductases which affects iron homeostasis leading to iron toxicity. Notably, the enhanced expression of TOR1 and TOR2 rescue the Torin2 augmented iron toxicity of yeast cell. This study has revealed novel conduits and our results suggest that using Torin2 will enable the dissection of TORC2 mediated functions of the TOR signalling pathway.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">29800736</PMID><DateCompleted><Year>2018</Year><Month>06</Month><Day>12</Day></DateCompleted><DateRevised><Year>2018</Year><Month>06</Month><Day>12</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1879-0038</ISSN><JournalIssue CitedMedium="Internet"><Volume>669</Volume><PubDate><Year>2018</Year><Month>Aug</Month><Day>30</Day></PubDate></JournalIssue><Title>Gene</Title><ISOAbbreviation>Gene</ISOAbbreviation></Journal><ArticleTitle>Novel insights into TOR signalling in Saccharomyces cerevisiae through Torin2.</ArticleTitle><Pagination><MedlinePgn>15-27</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0378-1119(18)30578-X</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.gene.2018.05.081</ELocationID><Abstract><AbstractText>Target of rapamycin (TOR) regulates cellular homeostasis by coordinating cellular growth pathways in response to different environmental signals. Rapamycin, an allosteric TOR complex 1 (TORC1) inhibitor, has proven to be invaluable for elucidating various aspects of the TOR signalling pathway; however, its applications are limited due to its inability to completely suppress TORC2. In the present study, we examined the effects of a newly discovered potent TOR inhibitor, Torin2, which inhibits both TORC1 and TORC2, on Saccharomyces cerevisiae growth. Genome-scale expression profiling of Torin2 treated yeast cells showed an expression profile similar to that of other TOR inhibitors such as rapamycin and caffeine. Distinct inhibition of cell growth by Torin2 treatment is indicated by the fact that a smaller number of transcripts are altered, compared to the changes after rapamycin and caffeine treatments. Our results revealed that Torin2 leads to increased expression of the calcineurin pathway genes favouring a synergistic therapeutic response of Torin2 in combination with calcineurin inhibitors. Further, Torin2 causes defective bud site selection during asymmetric cell division, indicating a role of TOR signalling in regulation of the budding pattern. Torin2 treated yeast cells exhibit increased expression of metalloreductases which affects iron homeostasis leading to iron toxicity. Notably, the enhanced expression of TOR1 and TOR2 rescue the Torin2 augmented iron toxicity of yeast cell. This study has revealed novel conduits and our results suggest that using Torin2 will enable the dissection of TORC2 mediated functions of the TOR signalling pathway.</AbstractText><CopyrightInformation>Copyright © 2018 Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kumar</LastName><ForeName>Pavan</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>School of Biotechnology, Gautam Buddha University, Greater NOIDA, Gautam Budh Nagar 201312, India.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Awasthi</LastName><ForeName>Ankita</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>School of Biotechnology, Gautam Buddha University, Greater NOIDA, Gautam Budh Nagar 201312, India.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Nain</LastName><ForeName>Vikrant</ForeName><Initials>V</Initials><AffiliationInfo><Affiliation>School of Biotechnology, Gautam Buddha University, Greater NOIDA, Gautam Budh Nagar 201312, India.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Issac</LastName><ForeName>Biju</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Bioinformatics Core, University of Miami, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Puria</LastName><ForeName>Rekha</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>School of Biotechnology, Gautam Buddha University, Greater NOIDA, Gautam Budh Nagar 201312, India. Electronic address: rpuria@gbu.ac.in.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2018</Year><Month>05</Month><Day>22</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Gene</MedlineTA><NlmUniqueID>7706761</NlmUniqueID><ISSNLinking>0378-1119</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C558529">9-(6-aminopyridin-3-yl)-1-(3-(trifluoromethyl)phenyl)benzo(h)(1,6)naphthyridin-2(1H)-one</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009287">Naphthyridines</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D047428">Protein Kinase Inhibitors</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>E1UOL152H7</RegistryNumber><NameOfSubstance UI="D007501">Iron</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 3.1.3.16</RegistryNumber><NameOfSubstance UI="D019703">Calcineurin</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D019703" MajorTopicYN="N">Calcineurin</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002455" MajorTopicYN="N">Cell Division</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007501" MajorTopicYN="N">Iron</DescriptorName><QualifierName UI="Q000633" MajorTopicYN="N">toxicity</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009287" MajorTopicYN="N">Naphthyridines</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D047428" MajorTopicYN="N">Protein Kinase Inhibitors</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017346" MajorTopicYN="N">Protein-Serine-Threonine Kinases</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="Y">antagonists & inhibitors</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000254" MajorTopicYN="N">growth & development</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029701" MajorTopicYN="N">Saccharomyces cerevisiae Proteins</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="Y">antagonists & inhibitors</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015398" MajorTopicYN="N">Signal Transduction</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014158" MajorTopicYN="N">Transcription, Genetic</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Asymmetric cell division</Keyword><Keyword MajorTopicYN="N">Budding pattern</Keyword><Keyword MajorTopicYN="N">Iron toxicity</Keyword><Keyword MajorTopicYN="N">Saccharomyces</Keyword><Keyword MajorTopicYN="N">Torin2</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2017</Year><Month>12</Month><Day>18</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2018</Year><Month>04</Month><Day>06</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2018</Year><Month>05</Month><Day>21</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2018</Year><Month>5</Month><Day>26</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2018</Year><Month>6</Month><Day>13</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2018</Year><Month>5</Month><Day>26</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">29800736</ArticleId><ArticleId IdType="pii">S0378-1119(18)30578-X</ArticleId><ArticleId IdType="doi">10.1016/j.gene.2018.05.081</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Inde</li><li>États-Unis</li></country></list><tree><country name="Inde"><noRegion><name sortKey="Kumar, Pavan" sort="Kumar, Pavan" uniqKey="Kumar P" first="Pavan" last="Kumar">Pavan Kumar</name></noRegion><name sortKey="Awasthi, Ankita" sort="Awasthi, Ankita" uniqKey="Awasthi A" first="Ankita" last="Awasthi">Ankita Awasthi</name><name sortKey="Nain, Vikrant" sort="Nain, Vikrant" uniqKey="Nain V" first="Vikrant" last="Nain">Vikrant Nain</name><name sortKey="Puria, Rekha" sort="Puria, Rekha" uniqKey="Puria R" first="Rekha" last="Puria">Rekha Puria</name></country><country name="États-Unis"><noRegion><name sortKey="Issac, Biju" sort="Issac, Biju" uniqKey="Issac B" first="Biju" last="Issac">Biju Issac</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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