Structure of TOR and its complex with KOG1.
Identifieur interne : 001681 ( Main/Exploration ); précédent : 001680; suivant : 001682Structure of TOR and its complex with KOG1.
Auteurs : Alessandra Adami [Royaume-Uni] ; Bego A García-Alvarez ; Ernesto Arias-Palomo ; David Barford ; Oscar LlorcaSource :
- Molecular cell [ 1097-2765 ] ; 2007.
Descripteurs français
- KwdFr :
- Conformation des protéines (MeSH), Phosphatidylinositol 3-kinases (composition chimique), Phosphatidylinositol 3-kinases (métabolisme), Phosphatidylinositol 3-kinases (ultrastructure), Phosphotransferases (Alcohol Group Acceptor) (composition chimique), Phosphotransferases (Alcohol Group Acceptor) (métabolisme), Phosphotransferases (Alcohol Group Acceptor) (ultrastructure), Protéines de Saccharomyces cerevisiae (composition chimique), Protéines de Saccharomyces cerevisiae (métabolisme), Protéines de Saccharomyces cerevisiae (ultrastructure), Protéines et peptides de signalisation intracellulaire (métabolisme), Protéines membranaires (composition chimique), Protéines membranaires (métabolisme), Saccharomyces cerevisiae (croissance et développement), Saccharomyces cerevisiae (génétique), Saccharomyces cerevisiae (métabolisme), Sirolimus (métabolisme).
- MESH :
- composition chimique : Phosphatidylinositol 3-kinases, Phosphotransferases (Alcohol Group Acceptor), Protéines de Saccharomyces cerevisiae, Protéines membranaires.
- croissance et développement : Saccharomyces cerevisiae.
- génétique : Saccharomyces cerevisiae.
- métabolisme : Phosphatidylinositol 3-kinases, Phosphotransferases (Alcohol Group Acceptor), Protéines de Saccharomyces cerevisiae, Protéines et peptides de signalisation intracellulaire, Protéines membranaires, Saccharomyces cerevisiae, Sirolimus.
- ultrastructure : Phosphatidylinositol 3-kinases, Phosphotransferases (Alcohol Group Acceptor), Protéines de Saccharomyces cerevisiae.
- Conformation des protéines.
English descriptors
- KwdEn :
- Intracellular Signaling Peptides and Proteins (metabolism), Membrane Proteins (chemistry), Membrane Proteins (metabolism), Phosphatidylinositol 3-Kinases (chemistry), Phosphatidylinositol 3-Kinases (metabolism), Phosphatidylinositol 3-Kinases (ultrastructure), Phosphotransferases (Alcohol Group Acceptor) (chemistry), Phosphotransferases (Alcohol Group Acceptor) (metabolism), Phosphotransferases (Alcohol Group Acceptor) (ultrastructure), Protein Conformation (MeSH), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (growth & development), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (chemistry), Saccharomyces cerevisiae Proteins (metabolism), Saccharomyces cerevisiae Proteins (ultrastructure), Sirolimus (metabolism).
- MESH :
- chemical , chemistry : Membrane Proteins, Phosphatidylinositol 3-Kinases, Phosphotransferases (Alcohol Group Acceptor), Saccharomyces cerevisiae Proteins.
- chemical , metabolism : Intracellular Signaling Peptides and Proteins, Membrane Proteins, Phosphatidylinositol 3-Kinases, Phosphotransferases (Alcohol Group Acceptor), Saccharomyces cerevisiae Proteins, Sirolimus.
- chemical , ultrastructure : Phosphatidylinositol 3-Kinases, Phosphotransferases (Alcohol Group Acceptor), Saccharomyces cerevisiae Proteins.
- genetics : Saccharomyces cerevisiae.
- growth & development : Saccharomyces cerevisiae.
- metabolism : Saccharomyces cerevisiae.
- Protein Conformation.
Abstract
The target of rapamycin (TOR) is a large (281 kDa) conserved Ser/Thr protein kinase that functions as a central controller of cell growth. TOR assembles into two distinct multiprotein complexes: TORC1 and TORC2. A defining feature of TORC1 is the interaction of TOR with KOG1 (Raptor in mammals) and its sensitivity to a rapamycin-FKBP12 complex. Here, we have reconstructed in three dimensions the 25 A resolution structures of endogenous budding yeast TOR1 and a TOR-KOG1 complex, using electron microscopy. TOR features distinctive N-terminal HEAT repeats that form a curved tubular-shaped domain that associates with the C-terminal WD40 repeat domain of KOG1. The N terminus of KOG1 is in proximity to the TOR kinase domain, likely functioning to bring substrates into the vicinity of the catalytic region. A model is proposed for the molecular architecture of the TOR-KOG1 complex explaining its sensitivity to rapamycin.
DOI: 10.1016/j.molcel.2007.05.040
PubMed: 17679098
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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A model is proposed for the molecular architecture of the TOR-KOG1 complex explaining its sensitivity to rapamycin.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17679098</PMID><DateCompleted><Year>2007</Year><Month>08</Month><Day>27</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1097-2765</ISSN><JournalIssue CitedMedium="Print"><Volume>27</Volume><Issue>3</Issue><PubDate><Year>2007</Year><Month>Aug</Month><Day>03</Day></PubDate></JournalIssue><Title>Molecular cell</Title><ISOAbbreviation>Mol Cell</ISOAbbreviation></Journal><ArticleTitle>Structure of TOR and its complex with KOG1.</ArticleTitle><Pagination><MedlinePgn>509-16</MedlinePgn></Pagination><Abstract><AbstractText>The target of rapamycin (TOR) is a large (281 kDa) conserved Ser/Thr protein kinase that functions as a central controller of cell growth. TOR assembles into two distinct multiprotein complexes: TORC1 and TORC2. A defining feature of TORC1 is the interaction of TOR with KOG1 (Raptor in mammals) and its sensitivity to a rapamycin-FKBP12 complex. Here, we have reconstructed in three dimensions the 25 A resolution structures of endogenous budding yeast TOR1 and a TOR-KOG1 complex, using electron microscopy. TOR features distinctive N-terminal HEAT repeats that form a curved tubular-shaped domain that associates with the C-terminal WD40 repeat domain of KOG1. The N terminus of KOG1 is in proximity to the TOR kinase domain, likely functioning to bring substrates into the vicinity of the catalytic region. A model is proposed for the molecular architecture of the TOR-KOG1 complex explaining its sensitivity to rapamycin.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Adami</LastName><ForeName>Alessandra</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Section of Structural Biology, Chester Beatty Laboratories, Institute of Cancer Research, 237 Fulham Road, London, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>García-Alvarez</LastName><ForeName>Begoña</ForeName><Initials>B</Initials></Author><Author ValidYN="Y"><LastName>Arias-Palomo</LastName><ForeName>Ernesto</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Barford</LastName><ForeName>David</ForeName><Initials>D</Initials></Author><Author ValidYN="Y"><LastName>Llorca</LastName><ForeName>Oscar</ForeName><Initials>O</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>United States</Country><MedlineTA>Mol Cell</MedlineTA><NlmUniqueID>9802571</NlmUniqueID><ISSNLinking>1097-2765</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D047908">Intracellular Signaling Peptides and Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C515118">Kog1 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C110280">LST8 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008565">Membrane Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029701">Saccharomyces cerevisiae 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PubStatus="revised"><Year>2007</Year><Month>05</Month><Day>06</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2007</Year><Month>05</Month><Day>31</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2007</Year><Month>8</Month><Day>7</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2007</Year><Month>8</Month><Day>28</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2007</Year><Month>8</Month><Day>7</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">17679098</ArticleId><ArticleId IdType="pii">S1097-2765(07)00372-3</ArticleId><ArticleId IdType="doi">10.1016/j.molcel.2007.05.040</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Royaume-Uni</li></country><region><li>Angleterre</li><li>Grand Londres</li></region><settlement><li>Londres</li></settlement></list><tree><noCountry><name sortKey="Arias Palomo, Ernesto" sort="Arias Palomo, Ernesto" uniqKey="Arias Palomo E" first="Ernesto" last="Arias-Palomo">Ernesto Arias-Palomo</name><name sortKey="Barford, David" sort="Barford, David" uniqKey="Barford D" first="David" last="Barford">David Barford</name><name sortKey="Garcia Alvarez, Bego A" sort="Garcia Alvarez, Bego A" uniqKey="Garcia Alvarez B" first="Bego A" last="García-Alvarez">Bego A García-Alvarez</name><name sortKey="Llorca, Oscar" sort="Llorca, Oscar" uniqKey="Llorca O" first="Oscar" last="Llorca">Oscar Llorca</name></noCountry><country name="Royaume-Uni"><region name="Angleterre"><name sortKey="Adami, Alessandra" sort="Adami, Alessandra" uniqKey="Adami A" first="Alessandra" last="Adami">Alessandra Adami</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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