Probing the membrane environment of the TOR kinases reveals functional interactions between TORC1, actin, and membrane trafficking in Saccharomyces cerevisiae.
Identifieur interne : 001703 ( Main/Exploration ); précédent : 001702; suivant : 001704Probing the membrane environment of the TOR kinases reveals functional interactions between TORC1, actin, and membrane trafficking in Saccharomyces cerevisiae.
Auteurs : Sofia Aronova [États-Unis] ; Karen Wedaman ; Scott Anderson ; John Yates ; Ted PowersSource :
- Molecular biology of the cell [ 1059-1524 ] ; 2007.
Descripteurs français
- KwdFr :
- Actines (métabolisme), Cytosquelette (effets des médicaments et des substances chimiques), Détergents (pharmacologie), Endocytose (effets des médicaments et des substances chimiques), Glucose (déficit), Liaison aux protéines (effets des médicaments et des substances chimiques), Marqueurs biologiques (métabolisme), Membrane cellulaire (effets des médicaments et des substances chimiques), Membrane cellulaire (enzymologie), Octoxinol (pharmacologie), Phosphatidylinositol 3-kinases (métabolisme), Phosphotransferases (Alcohol Group Acceptor) (métabolisme), Polarité de la cellule (effets des médicaments et des substances chimiques), Protéines de Saccharomyces cerevisiae (métabolisme), Protéines du cycle cellulaire (métabolisme), Protéomique (MeSH), Réseaux de régulation génique (effets des médicaments et des substances chimiques), Saccharomyces cerevisiae (cytologie), Saccharomyces cerevisiae (effets des médicaments et des substances chimiques), Saccharomyces cerevisiae (enzymologie), Sirolimus (pharmacologie), Transport biologique (effets des médicaments et des substances chimiques), Vésicules de transport (effets des médicaments et des substances chimiques).
- MESH :
- cytologie : Saccharomyces cerevisiae.
- déficit : Glucose.
- effets des médicaments et des substances chimiques : Cytosquelette, Endocytose, Liaison aux protéines, Membrane cellulaire, Polarité de la cellule, Réseaux de régulation génique, Saccharomyces cerevisiae, Transport biologique, Vésicules de transport.
- enzymologie : Membrane cellulaire, Saccharomyces cerevisiae.
- métabolisme : Actines, Marqueurs biologiques, Phosphatidylinositol 3-kinases, Phosphotransferases (Alcohol Group Acceptor), Protéines de Saccharomyces cerevisiae, Protéines du cycle cellulaire.
- pharmacologie : Détergents, Octoxinol, Sirolimus.
- Protéomique.
English descriptors
- KwdEn :
- Actins (metabolism), Biological Transport (drug effects), Biomarkers (metabolism), Cell Cycle Proteins (metabolism), Cell Membrane (drug effects), Cell Membrane (enzymology), Cell Polarity (drug effects), Cytoskeleton (drug effects), Detergents (pharmacology), Endocytosis (drug effects), Gene Regulatory Networks (drug effects), Glucose (deficiency), Octoxynol (pharmacology), Phosphatidylinositol 3-Kinases (metabolism), Phosphotransferases (Alcohol Group Acceptor) (metabolism), Protein Binding (drug effects), Proteomics (MeSH), Saccharomyces cerevisiae (cytology), Saccharomyces cerevisiae (drug effects), Saccharomyces cerevisiae (enzymology), Saccharomyces cerevisiae Proteins (metabolism), Sirolimus (pharmacology), Transport Vesicles (drug effects).
- MESH :
- chemical , deficiency : Glucose.
- chemical , metabolism : Actins, Biomarkers, Cell Cycle Proteins, Phosphatidylinositol 3-Kinases, Phosphotransferases (Alcohol Group Acceptor), Saccharomyces cerevisiae Proteins.
- cytology : Saccharomyces cerevisiae.
- drug effects : Biological Transport, Cell Membrane, Cell Polarity, Cytoskeleton, Endocytosis, Gene Regulatory Networks, Protein Binding, Saccharomyces cerevisiae, Transport Vesicles.
- enzymology : Cell Membrane, Saccharomyces cerevisiae.
- chemical , pharmacology : Detergents, Octoxynol, Sirolimus.
- Proteomics.
Abstract
The TOR kinases are regulators of growth in eukaryotic cells that assemble into two distinct protein complexes, TORC1 and TORC2, where TORC1 is inhibited by the antibiotic rapamycin. Present models favor a view wherein TORC1 regulates cell mass accumulation, and TORC2 regulates spatial aspects of growth, including organization of the actin cytoskeleton. Here, we demonstrate that in yeast both TORC1 and TORC2 fractionate with a novel form of detergent-resistant membranes that are distinct from detergent-resistant plasma membrane "rafts." Proteomic analysis of these TOR-associated membranes revealed the presence of regulators of endocytosis and the actin cytoskeleton. Genetic analyses revealed a significant number of interactions between these components and TORC1, demonstrating a functional link between TORC1 and actin/endocytosis-related genes. Moreover, we found that inhibition of TORC1 by rapamycin 1) disrupted actin polarization, 2) delayed actin repolarization after glucose starvation, and 3) delayed accumulation of lucifer yellow within the vacuole. By combining our genetic results with database mining, we constructed a map of interactions that led to the identification of additional genetic interactions between TORC1 and components involved in membrane trafficking. Together, these results reveal the broad scope of cellular processes influenced by TORC1, and they underscore the functional overlap between TORC1 and TORC2.
DOI: 10.1091/mbc.e07-03-0274
PubMed: 17507646
PubMed Central: PMC1949386
Affiliations:
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cerevisiae</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Actines</term><term>Marqueurs biologiques</term><term>Phosphatidylinositol 3-kinases</term><term>Phosphotransferases (Alcohol Group Acceptor)</term><term>Protéines de Saccharomyces cerevisiae</term><term>Protéines du cycle cellulaire</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Détergents</term><term>Octoxinol</term><term>Sirolimus</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Detergents</term><term>Octoxynol</term><term>Sirolimus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Proteomics</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Protéomique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The TOR kinases are regulators of growth in eukaryotic cells that assemble into two distinct protein complexes, TORC1 and TORC2, where TORC1 is inhibited by the antibiotic rapamycin. Present models favor a view wherein TORC1 regulates cell mass accumulation, and TORC2 regulates spatial aspects of growth, including organization of the actin cytoskeleton. Here, we demonstrate that in yeast both TORC1 and TORC2 fractionate with a novel form of detergent-resistant membranes that are distinct from detergent-resistant plasma membrane "rafts." Proteomic analysis of these TOR-associated membranes revealed the presence of regulators of endocytosis and the actin cytoskeleton. Genetic analyses revealed a significant number of interactions between these components and TORC1, demonstrating a functional link between TORC1 and actin/endocytosis-related genes. Moreover, we found that inhibition of TORC1 by rapamycin 1) disrupted actin polarization, 2) delayed actin repolarization after glucose starvation, and 3) delayed accumulation of lucifer yellow within the vacuole. By combining our genetic results with database mining, we constructed a map of interactions that led to the identification of additional genetic interactions between TORC1 and components involved in membrane trafficking. Together, these results reveal the broad scope of cellular processes influenced by TORC1, and they underscore the functional overlap between TORC1 and TORC2.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17507646</PMID><DateCompleted><Year>2007</Year><Month>10</Month><Day>17</Day></DateCompleted><DateRevised><Year>2019</Year><Month>01</Month><Day>08</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">1059-1524</ISSN><JournalIssue CitedMedium="Print"><Volume>18</Volume><Issue>8</Issue><PubDate><Year>2007</Year><Month>Aug</Month></PubDate></JournalIssue><Title>Molecular biology of the cell</Title><ISOAbbreviation>Mol Biol Cell</ISOAbbreviation></Journal><ArticleTitle>Probing the membrane environment of the TOR kinases reveals functional interactions between TORC1, actin, and membrane trafficking in Saccharomyces cerevisiae.</ArticleTitle><Pagination><MedlinePgn>2779-94</MedlinePgn></Pagination><Abstract><AbstractText>The TOR kinases are regulators of growth in eukaryotic cells that assemble into two distinct protein complexes, TORC1 and TORC2, where TORC1 is inhibited by the antibiotic rapamycin. Present models favor a view wherein TORC1 regulates cell mass accumulation, and TORC2 regulates spatial aspects of growth, including organization of the actin cytoskeleton. Here, we demonstrate that in yeast both TORC1 and TORC2 fractionate with a novel form of detergent-resistant membranes that are distinct from detergent-resistant plasma membrane "rafts." Proteomic analysis of these TOR-associated membranes revealed the presence of regulators of endocytosis and the actin cytoskeleton. Genetic analyses revealed a significant number of interactions between these components and TORC1, demonstrating a functional link between TORC1 and actin/endocytosis-related genes. Moreover, we found that inhibition of TORC1 by rapamycin 1) disrupted actin polarization, 2) delayed actin repolarization after glucose starvation, and 3) delayed accumulation of lucifer yellow within the vacuole. By combining our genetic results with database mining, we constructed a map of interactions that led to the identification of additional genetic interactions between TORC1 and components involved in membrane trafficking. Together, these results reveal the broad scope of cellular processes influenced by TORC1, and they underscore the functional overlap between TORC1 and TORC2.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Aronova</LastName><ForeName>Sofia</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Section of Molecular and Cellular Biology, College of Biological Sciences, University of California, Davis, Davis, CA 95616, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wedaman</LastName><ForeName>Karen</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Anderson</LastName><ForeName>Scott</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Yates</LastName><ForeName>John</ForeName><Initials>J</Initials><Suffix>3rd</Suffix></Author><Author ValidYN="Y"><LastName>Powers</LastName><ForeName>Ted</ForeName><Initials>T</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2007</Year><Month>05</Month><Day>16</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Mol Biol Cell</MedlineTA><NlmUniqueID>9201390</NlmUniqueID><ISSNLinking>1059-1524</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000199">Actins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D015415">Biomarkers</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018797">Cell Cycle Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D003902">Detergents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>9002-93-1</RegistryNumber><NameOfSubstance UI="D017830">Octoxynol</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>EC 2.7.1.137</RegistryNumber><NameOfSubstance UI="C081135">TOR2 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>IY9XDZ35W2</RegistryNumber><NameOfSubstance UI="D005947">Glucose</NameOfSubstance></Chemical><Chemical><RegistryNumber>W36ZG6FT64</RegistryNumber><NameOfSubstance UI="D020123">Sirolimus</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000199" MajorTopicYN="N">Actins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001692" MajorTopicYN="N">Biological Transport</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015415" MajorTopicYN="N">Biomarkers</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018797" MajorTopicYN="N">Cell Cycle Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002462" MajorTopicYN="N">Cell Membrane</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016764" MajorTopicYN="N">Cell Polarity</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003599" MajorTopicYN="N">Cytoskeleton</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003902" MajorTopicYN="N">Detergents</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004705" MajorTopicYN="N">Endocytosis</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D053263" MajorTopicYN="N">Gene Regulatory Networks</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005947" MajorTopicYN="N">Glucose</DescriptorName><QualifierName UI="Q000172" MajorTopicYN="N">deficiency</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017830" MajorTopicYN="N">Octoxynol</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019869" MajorTopicYN="N">Phosphatidylinositol 3-Kinases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017853" MajorTopicYN="N">Phosphotransferases (Alcohol Group Acceptor)</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName 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