TOR complex 1 includes a novel component, Tco89p (YPL180w), and cooperates with Ssd1p to maintain cellular integrity in Saccharomyces cerevisiae.
Identifieur interne : 001872 ( Main/Exploration ); précédent : 001871; suivant : 001873TOR complex 1 includes a novel component, Tco89p (YPL180w), and cooperates with Ssd1p to maintain cellular integrity in Saccharomyces cerevisiae.
Auteurs : Aaron Reinke [États-Unis] ; Scott Anderson ; J Michael Mccaffery ; John Yates ; Sofia Aronova ; Stephanie Chu ; Stephen Fairclough ; Cory Iverson ; Karen P. Wedaman ; Ted PowersSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2004.
Descripteurs français
- KwdFr :
- Allèles (MeSH), Antibiotiques antinéoplasiques (pharmacologie), Délétion de gène (MeSH), Liaison aux protéines (MeSH), Microscopie immunoélectronique (MeSH), Phosphatidylinositol 3-kinases (composition chimique), Phosphotransferases (Alcohol Group Acceptor) (composition chimique), Phénotype (MeSH), Plasmides (métabolisme), Protéines adaptatrices de la transduction du signal (MeSH), Protéines de Saccharomyces cerevisiae (composition chimique), Protéines de Saccharomyces cerevisiae (métabolisme), Protéines fongiques (composition chimique), Saccharomyces cerevisiae (métabolisme), Sirolimus (pharmacologie), Spectrométrie de masse (MeSH), Température (MeSH), Tests aux précipitines (MeSH), Électrophorèse sur gel de polyacrylamide (MeSH).
- MESH :
- composition chimique : Phosphatidylinositol 3-kinases, Phosphotransferases (Alcohol Group Acceptor), Protéines de Saccharomyces cerevisiae, Protéines fongiques.
- métabolisme : Plasmides, Protéines de Saccharomyces cerevisiae, Saccharomyces cerevisiae.
- pharmacologie : Antibiotiques antinéoplasiques, Sirolimus.
- Allèles, Délétion de gène, Liaison aux protéines, Microscopie immunoélectronique, Phénotype, Protéines adaptatrices de la transduction du signal, Spectrométrie de masse, Température, Tests aux précipitines, Électrophorèse sur gel de polyacrylamide.
English descriptors
- KwdEn :
- Adaptor Proteins, Signal Transducing (MeSH), Alleles (MeSH), Antibiotics, Antineoplastic (pharmacology), Electrophoresis, Polyacrylamide Gel (MeSH), Fungal Proteins (chemistry), Gene Deletion (MeSH), Mass Spectrometry (MeSH), Microscopy, Immunoelectron (MeSH), Phenotype (MeSH), Phosphatidylinositol 3-Kinases (chemistry), Phosphotransferases (Alcohol Group Acceptor) (chemistry), Plasmids (metabolism), Precipitin Tests (MeSH), Protein Binding (MeSH), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (chemistry), Saccharomyces cerevisiae Proteins (metabolism), Sirolimus (pharmacology), Temperature (MeSH).
- MESH :
- chemical , chemistry : Fungal Proteins, Phosphatidylinositol 3-Kinases, Phosphotransferases (Alcohol Group Acceptor), Saccharomyces cerevisiae Proteins.
- chemical , metabolism : Saccharomyces cerevisiae Proteins.
- chemical , pharmacology : Antibiotics, Antineoplastic, Sirolimus.
- chemical : Adaptor Proteins, Signal Transducing.
- metabolism : Plasmids, Saccharomyces cerevisiae.
- Alleles, Electrophoresis, Polyacrylamide Gel, Gene Deletion, Mass Spectrometry, Microscopy, Immunoelectron, Phenotype, Precipitin Tests, Protein Binding, Temperature.
Abstract
The Tor1p and Tor2p kinases, targets of the therapeutically important antibiotic rapamycin, function as components of two distinct protein complexes in yeast, termed TOR complex 1 (TORC1) and TORC2. TORC1 is responsible for a wide range of rapamycin-sensitive cellular activities and contains, in addition to Tor1p or Tor2p, two highly conserved proteins, Lst8p and Kog1p. By identifying proteins that co-purify with Tor1p, Tor2p, Lst8p, and Kog1p, we have characterized a comprehensive set of protein-protein interactions that define further the composition of TORC1 as well as TORC2. In particular, we have identified Tco89p (YPL180w) and Bit61p (YJL058c) as novel components of TORC1 and TORC2, respectively. Deletion of TOR1 or TCO89 results in two specific and distinct phenotypes, (i) rapamycin-hypersensitivity and (ii) decreased cellular integrity, both of which correlate with the presence of SSD1-d, an allele of SSD1 previously associated with defects in cellular integrity. Furthermore, we link Ssd1p to Tap42p, a component of the TOR pathway that is believed to act uniquely downstream of TORC1. Together, these results define a novel connection between TORC1 and Ssd1p-mediated maintenance of cellular integrity.
DOI: 10.1074/jbc.M313062200
PubMed: 14736892
Affiliations:
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TORC1 is responsible for a wide range of rapamycin-sensitive cellular activities and contains, in addition to Tor1p or Tor2p, two highly conserved proteins, Lst8p and Kog1p. By identifying proteins that co-purify with Tor1p, Tor2p, Lst8p, and Kog1p, we have characterized a comprehensive set of protein-protein interactions that define further the composition of TORC1 as well as TORC2. In particular, we have identified Tco89p (YPL180w) and Bit61p (YJL058c) as novel components of TORC1 and TORC2, respectively. Deletion of TOR1 or TCO89 results in two specific and distinct phenotypes, (i) rapamycin-hypersensitivity and (ii) decreased cellular integrity, both of which correlate with the presence of SSD1-d, an allele of SSD1 previously associated with defects in cellular integrity. Furthermore, we link Ssd1p to Tap42p, a component of the TOR pathway that is believed to act uniquely downstream of TORC1. Together, these results define a novel connection between TORC1 and Ssd1p-mediated maintenance of cellular integrity.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">14736892</PMID><DateCompleted><Year>2004</Year><Month>06</Month><Day>01</Day></DateCompleted><DateRevised><Year>2016</Year><Month>11</Month><Day>22</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>279</Volume><Issue>15</Issue><PubDate><Year>2004</Year><Month>Apr</Month><Day>09</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>TOR complex 1 includes a novel component, Tco89p (YPL180w), and cooperates with Ssd1p to maintain cellular integrity in Saccharomyces cerevisiae.</ArticleTitle><Pagination><MedlinePgn>14752-62</MedlinePgn></Pagination><Abstract><AbstractText>The Tor1p and Tor2p kinases, targets of the therapeutically important antibiotic rapamycin, function as components of two distinct protein complexes in yeast, termed TOR complex 1 (TORC1) and TORC2. TORC1 is responsible for a wide range of rapamycin-sensitive cellular activities and contains, in addition to Tor1p or Tor2p, two highly conserved proteins, Lst8p and Kog1p. By identifying proteins that co-purify with Tor1p, Tor2p, Lst8p, and Kog1p, we have characterized a comprehensive set of protein-protein interactions that define further the composition of TORC1 as well as TORC2. In particular, we have identified Tco89p (YPL180w) and Bit61p (YJL058c) as novel components of TORC1 and TORC2, respectively. Deletion of TOR1 or TCO89 results in two specific and distinct phenotypes, (i) rapamycin-hypersensitivity and (ii) decreased cellular integrity, both of which correlate with the presence of SSD1-d, an allele of SSD1 previously associated with defects in cellular integrity. Furthermore, we link Ssd1p to Tap42p, a component of the TOR pathway that is believed to act uniquely downstream of TORC1. Together, these results define a novel connection between TORC1 and Ssd1p-mediated maintenance of cellular integrity.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Reinke</LastName><ForeName>Aaron</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Section of Molecular and Cellular Biology and Center for Genetics and Development, Division of Biological Sciences, University of California, Davis, California 95616, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Anderson</LastName><ForeName>Scott</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>McCaffery</LastName><ForeName>J Michael</ForeName><Initials>JM</Initials></Author><Author ValidYN="Y"><LastName>Yates</LastName><ForeName>John</ForeName><Initials>J</Initials><Suffix>3rd</Suffix></Author><Author ValidYN="Y"><LastName>Aronova</LastName><ForeName>Sofia</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Chu</LastName><ForeName>Stephanie</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Fairclough</LastName><ForeName>Stephen</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Iverson</LastName><ForeName>Cory</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Wedaman</LastName><ForeName>Karen P</ForeName><Initials>KP</Initials></Author><Author ValidYN="Y"><LastName>Powers</LastName><ForeName>Ted</ForeName><Initials>T</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>S10 RR019409-01</GrantID><Acronym>RR</Acronym><Agency>NCRR NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>RR-11823</GrantID><Acronym>RR</Acronym><Agency>NCRR NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2004</Year><Month>01</Month><Day>21</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D048868">Adaptor Proteins, Signal Transducing</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000903">Antibiotics, Antineoplastic</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C485219">Ssd1 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C100984">TAP42 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C485218">Tco89 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.1.-</RegistryNumber><NameOfSubstance UI="D019869">Phosphatidylinositol 3-Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 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>W36ZG6FT64</RegistryNumber><NameOfSubstance UI="D020123">Sirolimus</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D048868" MajorTopicYN="N">Adaptor Proteins, Signal Transducing</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000483" MajorTopicYN="N">Alleles</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000903" MajorTopicYN="N">Antibiotics, Antineoplastic</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004591" MajorTopicYN="N">Electrophoresis, Polyacrylamide Gel</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017353" MajorTopicYN="N">Gene Deletion</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013058" MajorTopicYN="N">Mass Spectrometry</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016253" MajorTopicYN="N">Microscopy, Immunoelectron</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010641" MajorTopicYN="N">Phenotype</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019869" MajorTopicYN="N">Phosphatidylinositol 3-Kinases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017853" MajorTopicYN="N">Phosphotransferases (Alcohol Group Acceptor)</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010957" MajorTopicYN="N">Plasmids</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011233" MajorTopicYN="N">Precipitin Tests</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein 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sort="Fairclough, Stephen" uniqKey="Fairclough S" first="Stephen" last="Fairclough">Stephen Fairclough</name><name sortKey="Iverson, Cory" sort="Iverson, Cory" uniqKey="Iverson C" first="Cory" last="Iverson">Cory Iverson</name><name sortKey="Mccaffery, J Michael" sort="Mccaffery, J Michael" uniqKey="Mccaffery J" first="J Michael" last="Mccaffery">J Michael Mccaffery</name><name sortKey="Powers, Ted" sort="Powers, Ted" uniqKey="Powers T" first="Ted" last="Powers">Ted Powers</name><name sortKey="Wedaman, Karen P" sort="Wedaman, Karen P" uniqKey="Wedaman K" first="Karen P" last="Wedaman">Karen P. Wedaman</name><name sortKey="Yates, John" sort="Yates, John" uniqKey="Yates J" first="John" last="Yates">John Yates</name></noCountry><country name="États-Unis"><noRegion><name sortKey="Reinke, Aaron" sort="Reinke, Aaron" uniqKey="Reinke A" first="Aaron" last="Reinke">Aaron Reinke</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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