Target of rapamycin proteins and their kinase activities are required for meiosis.
Identifieur interne : 001A78 ( Main/Exploration ); précédent : 001A77; suivant : 001A79Target of rapamycin proteins and their kinase activities are required for meiosis.
Auteurs : X F Zheng [États-Unis] ; S L SchreiberSource :
- Proceedings of the National Academy of Sciences of the United States of America [ 0027-8424 ] ; 1997.
Descripteurs français
- KwdFr :
- 1-Phosphatidylinositol 4-kinase (MeSH), Milieux de culture (MeSH), Méiose (physiologie), Phosphotransferases (Alcohol Group Acceptor) (métabolisme), Polyènes (métabolisme), Protéines de Saccharomyces cerevisiae (MeSH), Protéines fongiques (métabolisme), Protéines fongiques (physiologie), Saccharomyces cerevisiae (cytologie), Saccharomyces cerevisiae (métabolisme), Sirolimus (MeSH).
- MESH :
- cytologie : Saccharomyces cerevisiae.
- métabolisme : Phosphotransferases (Alcohol Group Acceptor), Polyènes, Protéines fongiques, Saccharomyces cerevisiae.
- physiologie : Méiose, Protéines fongiques.
- 1-Phosphatidylinositol 4-kinase, Milieux de culture, Protéines de Saccharomyces cerevisiae, Sirolimus.
English descriptors
- KwdEn :
- 1-Phosphatidylinositol 4-Kinase (MeSH), Culture Media (MeSH), Fungal Proteins (metabolism), Fungal Proteins (physiology), Meiosis (physiology), Phosphotransferases (Alcohol Group Acceptor) (metabolism), Polyenes (metabolism), Saccharomyces cerevisiae (cytology), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (MeSH), Sirolimus (MeSH).
- MESH :
- chemical , metabolism : Fungal Proteins, Phosphotransferases (Alcohol Group Acceptor), Polyenes.
- chemical , physiology : Fungal Proteins.
- chemical : 1-Phosphatidylinositol 4-Kinase, Culture Media, Saccharomyces cerevisiae Proteins, Sirolimus.
- cytology : Saccharomyces cerevisiae.
- metabolism : Saccharomyces cerevisiae.
- physiology : Meiosis.
Abstract
The phosphatidylinositol kinase-related kinases, including Tor1p, Tor2p, FRAP/RAFT, FRP/ATR, ATM, Mec1p, Rad3, and Tel1p, function in signal transduction pathways involved in cell cycle progression and surveillance. The rapamycin-sensitive kinase activities of Tor1p and Tor2p are required for the nutrient-activated protein translation essential for G1 cell cycle progression in haploid yeast cells. In addition, Tor2p's kinase activity is necessary for its unique rapamycin-insensitive function involved in the assembly of the actin cytoskeleton. In the current study using diploid yeast, we found that the kinase activities of the Tor proteins are also required for two discrete steps during yeast meiosisthe switch between the mitotic and meiotic cell cycles and a later step during meiosis involved in the packaging of resultant haploid cells (spores) into asci. Based on what is known of the mitotic functions of Tor and FRAP proteins, these results likely reflect the requirement for signaling pathways leading to regulated protein translation during meiosis. Mec1p, which is required for meiotic recombination, and the Tor proteins are, therefore, homologous kinases with distinct, yet essential, roles in meiosis.
DOI: 10.1073/pnas.94.7.3070
PubMed: 9096347
PubMed Central: PMC20323
Affiliations:
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xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138</wicri:regionArea><placeName><region type="state">Massachusetts</region><settlement type="city">Cambridge (Massachusetts)</settlement></placeName><orgName type="university">Université Harvard</orgName></affiliation></author><author><name sortKey="Schreiber, S L" sort="Schreiber, S L" uniqKey="Schreiber S" first="S L" last="Schreiber">S L Schreiber</name></author></analytic><series><title level="j">Proceedings of the National Academy of Sciences of the United States of America</title><idno type="ISSN">0027-8424</idno><imprint><date when="1997" type="published">1997</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>1-Phosphatidylinositol 4-Kinase (MeSH)</term><term>Culture Media (MeSH)</term><term>Fungal Proteins (metabolism)</term><term>Fungal Proteins (physiology)</term><term>Meiosis (physiology)</term><term>Phosphotransferases (Alcohol Group Acceptor) (metabolism)</term><term>Polyenes (metabolism)</term><term>Saccharomyces cerevisiae (cytology)</term><term>Saccharomyces cerevisiae (metabolism)</term><term>Saccharomyces cerevisiae Proteins (MeSH)</term><term>Sirolimus (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>1-Phosphatidylinositol 4-kinase (MeSH)</term><term>Milieux de culture (MeSH)</term><term>Méiose (physiologie)</term><term>Phosphotransferases (Alcohol Group Acceptor) (métabolisme)</term><term>Polyènes (métabolisme)</term><term>Protéines de Saccharomyces cerevisiae (MeSH)</term><term>Protéines fongiques (métabolisme)</term><term>Protéines fongiques (physiologie)</term><term>Saccharomyces cerevisiae (cytologie)</term><term>Saccharomyces cerevisiae (métabolisme)</term><term>Sirolimus (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Fungal Proteins</term><term>Phosphotransferases (Alcohol Group Acceptor)</term><term>Polyenes</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Fungal Proteins</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>1-Phosphatidylinositol 4-Kinase</term><term>Culture Media</term><term>Saccharomyces cerevisiae Proteins</term><term>Sirolimus</term></keywords><keywords scheme="MESH" qualifier="cytologie" xml:lang="fr"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Phosphotransferases (Alcohol Group Acceptor)</term><term>Polyènes</term><term>Protéines fongiques</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Méiose</term><term>Protéines fongiques</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Meiosis</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>1-Phosphatidylinositol 4-kinase</term><term>Milieux de culture</term><term>Protéines de Saccharomyces cerevisiae</term><term>Sirolimus</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The phosphatidylinositol kinase-related kinases, including Tor1p, Tor2p, FRAP/RAFT, FRP/ATR, ATM, Mec1p, Rad3, and Tel1p, function in signal transduction pathways involved in cell cycle progression and surveillance. The rapamycin-sensitive kinase activities of Tor1p and Tor2p are required for the nutrient-activated protein translation essential for G1 cell cycle progression in haploid yeast cells. In addition, Tor2p's kinase activity is necessary for its unique rapamycin-insensitive function involved in the assembly of the actin cytoskeleton. In the current study using diploid yeast, we found that the kinase activities of the Tor proteins are also required for two discrete steps during yeast meiosisthe switch between the mitotic and meiotic cell cycles and a later step during meiosis involved in the packaging of resultant haploid cells (spores) into asci. Based on what is known of the mitotic functions of Tor and FRAP proteins, these results likely reflect the requirement for signaling pathways leading to regulated protein translation during meiosis. Mec1p, which is required for meiotic recombination, and the Tor proteins are, therefore, homologous kinases with distinct, yet essential, roles in meiosis.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">9096347</PMID><DateCompleted><Year>1997</Year><Month>05</Month><Day>08</Day></DateCompleted><DateRevised><Year>2019</Year><Month>05</Month><Day>01</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0027-8424</ISSN><JournalIssue CitedMedium="Print"><Volume>94</Volume><Issue>7</Issue><PubDate><Year>1997</Year><Month>Apr</Month><Day>01</Day></PubDate></JournalIssue><Title>Proceedings of the National Academy of Sciences of the United States of America</Title><ISOAbbreviation>Proc Natl Acad Sci U S A</ISOAbbreviation></Journal><ArticleTitle>Target of rapamycin proteins and their kinase activities are required for meiosis.</ArticleTitle><Pagination><MedlinePgn>3070-5</MedlinePgn></Pagination><Abstract><AbstractText>The phosphatidylinositol kinase-related kinases, including Tor1p, Tor2p, FRAP/RAFT, FRP/ATR, ATM, Mec1p, Rad3, and Tel1p, function in signal transduction pathways involved in cell cycle progression and surveillance. The rapamycin-sensitive kinase activities of Tor1p and Tor2p are required for the nutrient-activated protein translation essential for G1 cell cycle progression in haploid yeast cells. In addition, Tor2p's kinase activity is necessary for its unique rapamycin-insensitive function involved in the assembly of the actin cytoskeleton. In the current study using diploid yeast, we found that the kinase activities of the Tor proteins are also required for two discrete steps during yeast meiosisthe switch between the mitotic and meiotic cell cycles and a later step during meiosis involved in the packaging of resultant haploid cells (spores) into asci. Based on what is known of the mitotic functions of Tor and FRAP proteins, these results likely reflect the requirement for signaling pathways leading to regulated protein translation during meiosis. Mec1p, which is required for meiotic recombination, and the Tor proteins are, therefore, homologous kinases with distinct, yet essential, roles in meiosis.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Zheng</LastName><ForeName>X F</ForeName><Initials>XF</Initials><AffiliationInfo><Affiliation>Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Schreiber</LastName><ForeName>S L</ForeName><Initials>SL</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 GM038627</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R37 GM038627</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>GM38627</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United 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Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.1.-</RegistryNumber><NameOfSubstance UI="D017853">Phosphotransferases (Alcohol Group Acceptor)</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.1.67</RegistryNumber><NameOfSubstance UI="D019870">1-Phosphatidylinositol 4-Kinase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.1.67</RegistryNumber><NameOfSubstance UI="C441760">PIK1 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>W36ZG6FT64</RegistryNumber><NameOfSubstance UI="D020123">Sirolimus</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D019870" MajorTopicYN="N">1-Phosphatidylinositol 4-Kinase</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003470" MajorTopicYN="N">Culture Media</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008540" MajorTopicYN="N">Meiosis</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017853" MajorTopicYN="N">Phosphotransferases (Alcohol Group Acceptor)</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011090" MajorTopicYN="N">Polyenes</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000166" MajorTopicYN="N">cytology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029701" 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L" uniqKey="Schreiber S" first="S L" last="Schreiber">S L Schreiber</name></noCountry><country name="États-Unis"><region name="Massachusetts"><name sortKey="Zheng, X F" sort="Zheng, X F" uniqKey="Zheng X" first="X F" last="Zheng">X F Zheng</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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