S. pombe TORC1 activates the ubiquitin-proteasomal degradation of the meiotic regulator Mei2 in cooperation with Pat1 kinase.
Identifieur interne : 000E11 ( Main/Exploration ); précédent : 000E10; suivant : 000E12S. pombe TORC1 activates the ubiquitin-proteasomal degradation of the meiotic regulator Mei2 in cooperation with Pat1 kinase.
Auteurs : Yoko Otsubo [Japon] ; Akira Yamashita [Japon] ; Hayao Ohno [Japon] ; Masayuki Yamamoto [Japon]Source :
- Journal of cell science [ 1477-9137 ] ; 2014.
Descripteurs français
- KwdFr :
- Complexe-1 cible mécanistique de la rapamycine (MeSH), Complexes multiprotéiques (physiologie), Phosphatidylinositol 3-kinases (métabolisme), Phosphorylation (MeSH), Proteasome endopeptidase complex (MeSH), Protein-Serine-Threonine Kinases (métabolisme), Protéines de Schizosaccharomyces pombe (métabolisme), Protéines de liaison à l'ARN (métabolisme), Protéolyse (MeSH), Schizosaccharomyces (croissance et développement), Schizosaccharomyces (enzymologie), Stabilité protéique (MeSH), Sérine-thréonine kinases TOR (physiologie), Ubiquitination (MeSH), Épistasie (MeSH).
- MESH :
- croissance et développement : Schizosaccharomyces.
- enzymologie : Schizosaccharomyces.
- métabolisme : Phosphatidylinositol 3-kinases, Protein-Serine-Threonine Kinases, Protéines de Schizosaccharomyces pombe, Protéines de liaison à l'ARN.
- physiologie : Complexes multiprotéiques, Sérine-thréonine kinases TOR.
- Complexe-1 cible mécanistique de la rapamycine, Phosphorylation, Proteasome endopeptidase complex, Protéolyse, Stabilité protéique, Ubiquitination, Épistasie.
English descriptors
- KwdEn :
- Epistasis, Genetic (MeSH), Mechanistic Target of Rapamycin Complex 1 (MeSH), Multiprotein Complexes (physiology), Phosphatidylinositol 3-Kinases (metabolism), Phosphorylation (MeSH), Proteasome Endopeptidase Complex (MeSH), Protein Stability (MeSH), Protein-Serine-Threonine Kinases (metabolism), Proteolysis (MeSH), RNA-Binding Proteins (metabolism), Schizosaccharomyces (enzymology), Schizosaccharomyces (growth & development), Schizosaccharomyces pombe Proteins (metabolism), TOR Serine-Threonine Kinases (physiology), Ubiquitination (MeSH).
- MESH :
- chemical , metabolism : Phosphatidylinositol 3-Kinases, Protein-Serine-Threonine Kinases, RNA-Binding Proteins, Schizosaccharomyces pombe Proteins.
- chemical , physiology : Multiprotein Complexes, TOR Serine-Threonine Kinases.
- chemical : Mechanistic Target of Rapamycin Complex 1, Proteasome Endopeptidase Complex.
- enzymology : Schizosaccharomyces.
- growth & development : Schizosaccharomyces.
- Epistasis, Genetic, Phosphorylation, Protein Stability, Proteolysis, Ubiquitination.
Abstract
Target of rapamycin (TOR) kinase regulates cell metabolism and growth, acting as a subunit of two multi-protein complexes, TORC1 and TORC2. Known TORC substrates are either kinases or general factors involved in growth control. Here, we show that fission yeast TORC1, which promotes vegetative growth and suppresses sexual development, can phosphorylate Mei2 (a specific factor involved in switching the cell fate) in vitro. Alanine substitutions at the nine Mei2 phosphorylation sites stabilize the protein and promote mating and meiosis in vivo. We found that Mei2 is polyubiquitylated in vivo in a TORC1-dependent manner. Based on these data, we propose that TORC1 contributes to the suppression of sexual development by phosphorylating Mei2, in addition to controlling the cellular metabolic status.
DOI: 10.1242/jcs.135517
PubMed: 24741065
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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degradation of the meiotic regulator Mei2 in cooperation with Pat1 kinase.</title><author><name sortKey="Otsubo, Yoko" sort="Otsubo, Yoko" uniqKey="Otsubo Y" first="Yoko" last="Otsubo">Yoko Otsubo</name><affiliation wicri:level="1"><nlm:affiliation>Laboratory of Gene Function, Kazusa DNA Research Institute, Kazusa-kamatari, Kisarazu, Chiba 292-0818, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Laboratory of Gene Function, Kazusa DNA Research Institute, Kazusa-kamatari, Kisarazu, Chiba 292-0818</wicri:regionArea><wicri:noRegion>Chiba 292-0818</wicri:noRegion></affiliation></author><author><name sortKey="Yamashita, Akira" sort="Yamashita, Akira" uniqKey="Yamashita A" first="Akira" last="Yamashita">Akira Yamashita</name><affiliation wicri:level="1"><nlm:affiliation>Laboratory of Gene Function, Kazusa DNA Research Institute, Kazusa-kamatari, Kisarazu, Chiba 292-0818, Japan.</nlm:affiliation><country 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(metabolism)</term><term>Schizosaccharomyces (enzymology)</term><term>Schizosaccharomyces (growth & development)</term><term>Schizosaccharomyces pombe Proteins (metabolism)</term><term>TOR Serine-Threonine Kinases (physiology)</term><term>Ubiquitination (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Complexe-1 cible mécanistique de la rapamycine (MeSH)</term><term>Complexes multiprotéiques (physiologie)</term><term>Phosphatidylinositol 3-kinases (métabolisme)</term><term>Phosphorylation (MeSH)</term><term>Proteasome endopeptidase complex (MeSH)</term><term>Protein-Serine-Threonine Kinases (métabolisme)</term><term>Protéines de Schizosaccharomyces pombe (métabolisme)</term><term>Protéines de liaison à l'ARN (métabolisme)</term><term>Protéolyse (MeSH)</term><term>Schizosaccharomyces (croissance et développement)</term><term>Schizosaccharomyces (enzymologie)</term><term>Stabilité protéique (MeSH)</term><term>Sérine-thréonine kinases TOR (physiologie)</term><term>Ubiquitination (MeSH)</term><term>Épistasie (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Phosphatidylinositol 3-Kinases</term><term>Protein-Serine-Threonine Kinases</term><term>RNA-Binding Proteins</term><term>Schizosaccharomyces pombe Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Multiprotein Complexes</term><term>TOR Serine-Threonine Kinases</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Mechanistic Target of Rapamycin Complex 1</term><term>Proteasome Endopeptidase Complex</term></keywords><keywords scheme="MESH" qualifier="croissance et développement" xml:lang="fr"><term>Schizosaccharomyces</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Schizosaccharomyces</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Schizosaccharomyces</term></keywords><keywords scheme="MESH" qualifier="growth & development" xml:lang="en"><term>Schizosaccharomyces</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Phosphatidylinositol 3-kinases</term><term>Protein-Serine-Threonine Kinases</term><term>Protéines de Schizosaccharomyces pombe</term><term>Protéines de liaison à l'ARN</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Complexes multiprotéiques</term><term>Sérine-thréonine kinases TOR</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Epistasis, Genetic</term><term>Phosphorylation</term><term>Protein Stability</term><term>Proteolysis</term><term>Ubiquitination</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Complexe-1 cible mécanistique de la rapamycine</term><term>Phosphorylation</term><term>Proteasome endopeptidase complex</term><term>Protéolyse</term><term>Stabilité protéique</term><term>Ubiquitination</term><term>Épistasie</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Target of rapamycin (TOR) kinase regulates cell metabolism and growth, acting as a subunit of two multi-protein complexes, TORC1 and TORC2. Known TORC substrates are either kinases or general factors involved in growth control. Here, we show that fission yeast TORC1, which promotes vegetative growth and suppresses sexual development, can phosphorylate Mei2 (a specific factor involved in switching the cell fate) in vitro. Alanine substitutions at the nine Mei2 phosphorylation sites stabilize the protein and promote mating and meiosis in vivo. We found that Mei2 is polyubiquitylated in vivo in a TORC1-dependent manner. Based on these data, we propose that TORC1 contributes to the suppression of sexual development by phosphorylating Mei2, in addition to controlling the cellular metabolic status. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24741065</PMID><DateCompleted><Year>2015</Year><Month>01</Month><Day>29</Day></DateCompleted><DateRevised><Year>2017</Year><Month>11</Month><Day>16</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1477-9137</ISSN><JournalIssue CitedMedium="Internet"><Volume>127</Volume><Issue>Pt 12</Issue><PubDate><Year>2014</Year><Month>Jun</Month><Day>15</Day></PubDate></JournalIssue><Title>Journal of cell science</Title><ISOAbbreviation>J Cell Sci</ISOAbbreviation></Journal><ArticleTitle>S. pombe TORC1 activates the ubiquitin-proteasomal degradation of the meiotic regulator Mei2 in cooperation with Pat1 kinase.</ArticleTitle><Pagination><MedlinePgn>2639-46</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1242/jcs.135517</ELocationID><Abstract><AbstractText>Target of rapamycin (TOR) kinase regulates cell metabolism and growth, acting as a subunit of two multi-protein complexes, TORC1 and TORC2. Known TORC substrates are either kinases or general factors involved in growth control. Here, we show that fission yeast TORC1, which promotes vegetative growth and suppresses sexual development, can phosphorylate Mei2 (a specific factor involved in switching the cell fate) in vitro. Alanine substitutions at the nine Mei2 phosphorylation sites stabilize the protein and promote mating and meiosis in vivo. We found that Mei2 is polyubiquitylated in vivo in a TORC1-dependent manner. Based on these data, we propose that TORC1 contributes to the suppression of sexual development by phosphorylating Mei2, in addition to controlling the cellular metabolic status. </AbstractText><CopyrightInformation>© 2014. Published by The Company of Biologists Ltd.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Otsubo</LastName><ForeName>Yoko</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Laboratory of Gene Function, Kazusa DNA Research Institute, Kazusa-kamatari, Kisarazu, Chiba 292-0818, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yamashita</LastName><ForeName>Akira</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Laboratory of Gene Function, Kazusa DNA Research Institute, Kazusa-kamatari, Kisarazu, Chiba 292-0818, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ohno</LastName><ForeName>Hayao</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, Hongo, Tokyo 113-0033, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yamamoto</LastName><ForeName>Masayuki</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Laboratory of Gene Function, Kazusa DNA Research Institute, Kazusa-kamatari, Kisarazu, Chiba 292-0818, Japan Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, Hongo, Tokyo 113-0033, Japan Laboratory of Cell Responses, National Institute for Basic Biology, Nishigonaka 38, Myodaiji, Okazaki, Aichi, 444-8585, Japan yamamoto@nibb.ac.jp.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2014</Year><Month>04</Month><Day>16</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>J Cell Sci</MedlineTA><NlmUniqueID>0052457</NlmUniqueID><ISSNLinking>0021-9533</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D046912">Multiprotein Complexes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D016601">RNA-Binding Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029702">Schizosaccharomyces pombe Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C088896">mei2 protein, S pombe</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="C087019">ran1 protein, S pombe</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.1.1</RegistryNumber><NameOfSubstance UI="D058570">TOR Serine-Threonine Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.1.137</RegistryNumber><NameOfSubstance UI="C513100">tor2 protein, S pombe</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber><NameOfSubstance UI="D000076222">Mechanistic Target of Rapamycin Complex 1</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber><NameOfSubstance UI="D017346">Protein-Serine-Threonine Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.25.1</RegistryNumber><NameOfSubstance UI="D046988">Proteasome Endopeptidase Complex</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D004843" MajorTopicYN="N">Epistasis, Genetic</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000076222" MajorTopicYN="N">Mechanistic Target of Rapamycin Complex 1</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D046912" MajorTopicYN="N">Multiprotein Complexes</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019869" MajorTopicYN="N">Phosphatidylinositol 3-Kinases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010766" MajorTopicYN="N">Phosphorylation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D046988" MajorTopicYN="N">Proteasome Endopeptidase Complex</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D055550" MajorTopicYN="N">Protein Stability</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017346" MajorTopicYN="N">Protein-Serine-Threonine Kinases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D059748" MajorTopicYN="N">Proteolysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016601" MajorTopicYN="N">RNA-Binding Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012568" MajorTopicYN="N">Schizosaccharomyces</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000254" MajorTopicYN="N">growth & development</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029702" MajorTopicYN="N">Schizosaccharomyces pombe Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D058570" MajorTopicYN="N">TOR Serine-Threonine Kinases</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054875" MajorTopicYN="Y">Ubiquitination</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Fission yeast</Keyword><Keyword MajorTopicYN="N">Mating</Keyword><Keyword MajorTopicYN="N">Mei2</Keyword><Keyword MajorTopicYN="N">Meiosis</Keyword><Keyword MajorTopicYN="N">Proteasome</Keyword><Keyword MajorTopicYN="N">TOR kinase</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2014</Year><Month>4</Month><Day>18</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2014</Year><Month>4</Month><Day>18</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2015</Year><Month>1</Month><Day>30</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">24741065</ArticleId><ArticleId IdType="pii">jcs.135517</ArticleId><ArticleId IdType="doi">10.1242/jcs.135517</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Japon</li></country><region><li>Région de Kantō</li></region><settlement><li>Tokyo</li></settlement><orgName><li>Université de Tokyo</li></orgName></list><tree><country name="Japon"><noRegion><name sortKey="Otsubo, Yoko" sort="Otsubo, Yoko" uniqKey="Otsubo Y" first="Yoko" last="Otsubo">Yoko Otsubo</name></noRegion><name sortKey="Ohno, Hayao" sort="Ohno, Hayao" uniqKey="Ohno H" first="Hayao" last="Ohno">Hayao Ohno</name><name sortKey="Yamamoto, Masayuki" sort="Yamamoto, Masayuki" uniqKey="Yamamoto M" first="Masayuki" last="Yamamoto">Masayuki Yamamoto</name><name sortKey="Yamashita, Akira" sort="Yamashita, Akira" uniqKey="Yamashita A" first="Akira" last="Yamashita">Akira Yamashita</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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