Rapamycin sensitivity of the Schizosaccharomyces pombe tor2 mutant and organization of two highly phosphorylated TOR complexes by specific and common subunits.
Identifieur interne : 001699 ( Main/Exploration ); précédent : 001698; suivant : 001700Rapamycin sensitivity of the Schizosaccharomyces pombe tor2 mutant and organization of two highly phosphorylated TOR complexes by specific and common subunits.
Auteurs : Takeshi Hayashi [Japon] ; Mitsuko Hatanaka ; Koji Nagao ; Yukinobu Nakaseko ; Junko Kanoh ; Aya Kokubu ; Masahiro Ebe ; Mitsuhiro YanagidaSource :
- Genes to cells : devoted to molecular & cellular mechanisms [ 1356-9597 ] ; 2007.
Descripteurs français
- KwdFr :
- Complexes multiprotéiques (MeSH), Phosphatidylinositol 3-kinases (composition chimique), Phosphatidylinositol 3-kinases (métabolisme), Phosphorylation (MeSH), Protéines de Schizosaccharomyces pombe (composition chimique), Protéines de Schizosaccharomyces pombe (génétique), Protéines de Schizosaccharomyces pombe (métabolisme), Régulation de l'expression des gènes fongiques (MeSH), Schizosaccharomyces (effets des médicaments et des substances chimiques), Schizosaccharomyces (enzymologie), Schizosaccharomyces (génétique), Sirolimus (pharmacologie).
- MESH :
- composition chimique : Phosphatidylinositol 3-kinases, Protéines de Schizosaccharomyces pombe.
- effets des médicaments et des substances chimiques : Schizosaccharomyces.
- enzymologie : Schizosaccharomyces.
- génétique : Protéines de Schizosaccharomyces pombe, Schizosaccharomyces.
- métabolisme : Phosphatidylinositol 3-kinases, Protéines de Schizosaccharomyces pombe.
- pharmacologie : Sirolimus.
- Complexes multiprotéiques, Phosphorylation, Régulation de l'expression des gènes fongiques.
English descriptors
- KwdEn :
- Gene Expression Regulation, Fungal (MeSH), Multiprotein Complexes (MeSH), Phosphatidylinositol 3-Kinases (chemistry), Phosphatidylinositol 3-Kinases (metabolism), Phosphorylation (MeSH), Schizosaccharomyces (drug effects), Schizosaccharomyces (enzymology), Schizosaccharomyces (genetics), Schizosaccharomyces pombe Proteins (chemistry), Schizosaccharomyces pombe Proteins (genetics), Schizosaccharomyces pombe Proteins (metabolism), Sirolimus (pharmacology).
- MESH :
- chemical , chemistry : Phosphatidylinositol 3-Kinases, Schizosaccharomyces pombe Proteins.
- chemical , genetics : Schizosaccharomyces pombe Proteins.
- chemical , metabolism : Phosphatidylinositol 3-Kinases, Schizosaccharomyces pombe Proteins.
- chemical , pharmacology : Sirolimus.
- chemical : Multiprotein Complexes.
- drug effects : Schizosaccharomyces.
- enzymology : Schizosaccharomyces.
- genetics : Schizosaccharomyces.
- Gene Expression Regulation, Fungal, Phosphorylation.
Abstract
Nutrients are essential for cell growth and division. Screening of Schizosaccharomyces pombe temperature-sensitive strains led to the isolation of a nutrient-insensitive mutant, tor2-287. This mutant produces a nitrogen starvation-induced arrest phenotype in rich media, fails to recover from the arrest, and is hypersensitive to rapamycin. The L2048S substitution mutation in the catalytic domain in close proximity to the adenine base of ATP is unique as it is the sole known genetic cause of rapamycin hypersensitivity. Localization of Tor2 was speckled in the vegetative cytoplasm, and both speckled and membranous in the arrested cell cytoplasm. Using mass spectroscopic analysis, we identified six subunits (Tco89, Bit61, Toc1, Tel2, Tti1 and Cka1) that, in addition to the six previously identified subunits (Tor1, Tor2, Mip1/Raptor, Ste20/Rictor, Sin1/Avo1 and Wat1/Lst8), comprise the TOR complexes (TORCs). All of the subunits so far examined are multiply phosphorylated. Tel2 bound to Tti1 interacts with various phosphatidyl inositol kinase (PIK)-related kinases including Tra1, Tra2 and Rad3, as well as Tor1 and Tor2. Schizosaccharomyces pombe TORCs should thus be functionally redundant and might be broadly regulated through different subunits that are either common or specific to the two TORCs, or even common to various PIK-related kinases. Functional redundancy of the TORCs may explain the rapamycin hypersensitivity of tor2-287.
DOI: 10.1111/j.1365-2443.2007.01141.x
PubMed: 18076573
Affiliations:
Links toward previous steps (curation, corpus...)
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multiprotéiques</term><term>Phosphorylation</term><term>Régulation de l'expression des gènes fongiques</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Nutrients are essential for cell growth and division. Screening of Schizosaccharomyces pombe temperature-sensitive strains led to the isolation of a nutrient-insensitive mutant, tor2-287. This mutant produces a nitrogen starvation-induced arrest phenotype in rich media, fails to recover from the arrest, and is hypersensitive to rapamycin. The L2048S substitution mutation in the catalytic domain in close proximity to the adenine base of ATP is unique as it is the sole known genetic cause of rapamycin hypersensitivity. Localization of Tor2 was speckled in the vegetative cytoplasm, and both speckled and membranous in the arrested cell cytoplasm. Using mass spectroscopic analysis, we identified six subunits (Tco89, Bit61, Toc1, Tel2, Tti1 and Cka1) that, in addition to the six previously identified subunits (Tor1, Tor2, Mip1/Raptor, Ste20/Rictor, Sin1/Avo1 and Wat1/Lst8), comprise the TOR complexes (TORCs). All of the subunits so far examined are multiply phosphorylated. Tel2 bound to Tti1 interacts with various phosphatidyl inositol kinase (PIK)-related kinases including Tra1, Tra2 and Rad3, as well as Tor1 and Tor2. Schizosaccharomyces pombe TORCs should thus be functionally redundant and might be broadly regulated through different subunits that are either common or specific to the two TORCs, or even common to various PIK-related kinases. Functional redundancy of the TORCs may explain the rapamycin hypersensitivity of tor2-287.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">18076573</PMID><DateCompleted><Year>2008</Year><Month>03</Month><Day>28</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1356-9597</ISSN><JournalIssue CitedMedium="Print"><Volume>12</Volume><Issue>12</Issue><PubDate><Year>2007</Year><Month>Dec</Month></PubDate></JournalIssue><Title>Genes to cells : devoted to molecular & cellular mechanisms</Title><ISOAbbreviation>Genes Cells</ISOAbbreviation></Journal><ArticleTitle>Rapamycin sensitivity of the Schizosaccharomyces pombe tor2 mutant and organization of two highly phosphorylated TOR complexes by specific and common subunits.</ArticleTitle><Pagination><MedlinePgn>1357-70</MedlinePgn></Pagination><Abstract><AbstractText>Nutrients are essential for cell growth and division. Screening of Schizosaccharomyces pombe temperature-sensitive strains led to the isolation of a nutrient-insensitive mutant, tor2-287. This mutant produces a nitrogen starvation-induced arrest phenotype in rich media, fails to recover from the arrest, and is hypersensitive to rapamycin. The L2048S substitution mutation in the catalytic domain in close proximity to the adenine base of ATP is unique as it is the sole known genetic cause of rapamycin hypersensitivity. Localization of Tor2 was speckled in the vegetative cytoplasm, and both speckled and membranous in the arrested cell cytoplasm. Using mass spectroscopic analysis, we identified six subunits (Tco89, Bit61, Toc1, Tel2, Tti1 and Cka1) that, in addition to the six previously identified subunits (Tor1, Tor2, Mip1/Raptor, Ste20/Rictor, Sin1/Avo1 and Wat1/Lst8), comprise the TOR complexes (TORCs). All of the subunits so far examined are multiply phosphorylated. Tel2 bound to Tti1 interacts with various phosphatidyl inositol kinase (PIK)-related kinases including Tra1, Tra2 and Rad3, as well as Tor1 and Tor2. Schizosaccharomyces pombe TORCs should thus be functionally redundant and might be broadly regulated through different subunits that are either common or specific to the two TORCs, or even common to various PIK-related kinases. Functional redundancy of the TORCs may explain the rapamycin hypersensitivity of tor2-287.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Hayashi</LastName><ForeName>Takeshi</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>The G0 Cell Unit, Okinawa Institute of Science and Technology Promotion Corporation, Suzaki 12-22, Uruma, Okinawa 904-2234, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hatanaka</LastName><ForeName>Mitsuko</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Nagao</LastName><ForeName>Koji</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Nakaseko</LastName><ForeName>Yukinobu</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Kanoh</LastName><ForeName>Junko</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Kokubu</LastName><ForeName>Aya</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Ebe</LastName><ForeName>Masahiro</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Yanagida</LastName><ForeName>Mitsuhiro</ForeName><Initials>M</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Genes Cells</MedlineTA><NlmUniqueID>9607379</NlmUniqueID><ISSNLinking>1356-9597</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D046912">Multiprotein Complexes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029702">Schizosaccharomyces pombe Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.1.-</RegistryNumber><NameOfSubstance UI="D019869">Phosphatidylinositol 3-Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.1.137</RegistryNumber><NameOfSubstance UI="C513100">tor2 protein, S pombe</NameOfSubstance></Chemical><Chemical><RegistryNumber>W36ZG6FT64</RegistryNumber><NameOfSubstance UI="D020123">Sirolimus</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CommentsCorrectionsList><CommentsCorrections RefType="CommentIn"><RefSource>Genes Cells. 2007 Dec;12(12):1301-4</RefSource><PMID Version="1">18076567</PMID></CommentsCorrections></CommentsCorrectionsList><MeshHeadingList><MeshHeading><DescriptorName UI="D015966" MajorTopicYN="N">Gene Expression Regulation, Fungal</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D046912" MajorTopicYN="N">Multiprotein Complexes</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019869" MajorTopicYN="N">Phosphatidylinositol 3-Kinases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010766" MajorTopicYN="N">Phosphorylation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012568" MajorTopicYN="N">Schizosaccharomyces</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029702" MajorTopicYN="N">Schizosaccharomyces pombe Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020123" MajorTopicYN="N">Sirolimus</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2007</Year><Month>12</Month><Day>14</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2008</Year><Month>3</Month><Day>29</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2007</Year><Month>12</Month><Day>14</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">18076573</ArticleId><ArticleId IdType="pii">GTC1141</ArticleId><ArticleId IdType="doi">10.1111/j.1365-2443.2007.01141.x</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Japon</li></country></list><tree><noCountry><name sortKey="Ebe, Masahiro" sort="Ebe, Masahiro" uniqKey="Ebe M" first="Masahiro" last="Ebe">Masahiro Ebe</name><name sortKey="Hatanaka, Mitsuko" sort="Hatanaka, Mitsuko" uniqKey="Hatanaka M" first="Mitsuko" last="Hatanaka">Mitsuko Hatanaka</name><name sortKey="Kanoh, Junko" sort="Kanoh, Junko" uniqKey="Kanoh J" first="Junko" last="Kanoh">Junko Kanoh</name><name sortKey="Kokubu, Aya" sort="Kokubu, Aya" uniqKey="Kokubu A" first="Aya" last="Kokubu">Aya Kokubu</name><name sortKey="Nagao, Koji" sort="Nagao, Koji" uniqKey="Nagao K" first="Koji" last="Nagao">Koji Nagao</name><name sortKey="Nakaseko, Yukinobu" sort="Nakaseko, Yukinobu" uniqKey="Nakaseko Y" first="Yukinobu" last="Nakaseko">Yukinobu Nakaseko</name><name sortKey="Yanagida, Mitsuhiro" sort="Yanagida, Mitsuhiro" uniqKey="Yanagida M" first="Mitsuhiro" last="Yanagida">Mitsuhiro Yanagida</name></noCountry><country name="Japon"><noRegion><name sortKey="Hayashi, Takeshi" sort="Hayashi, Takeshi" uniqKey="Hayashi T" first="Takeshi" last="Hayashi">Takeshi Hayashi</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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