The TOR signalling network from yeast to man.
Identifieur interne : 001749 ( Main/Exploration ); précédent : 001748; suivant : 001750The TOR signalling network from yeast to man.
Auteurs : Claudio De Virgilio [Suisse] ; Robbie LoewithSource :
- The international journal of biochemistry & cell biology [ 1357-2725 ] ; 2006.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , physiology : Protein Kinases, Protein-Serine-Threonine Kinases, Saccharomyces cerevisiae Proteins.
- physiology : Signal Transduction.
- Animals, Humans, TOR Serine-Threonine Kinases.
Abstract
The target of rapamycin, TOR, is an essential ser/thr protein kinase that functions in two distinct multiprotein complexes, TOR complex 1 and 2. The structure and functions of these complexes have been conserved from yeast to man. TOR complex 1 is inhibited by rapamycin and is thought to couple growth cues to cellular metabolism; TOR complex 2 is not inhibited by rapamycin and appears to regulate spatial aspects of growth such as cell polarity. Work done in a variety of model systems, continues to contribute to our current understanding of this TOR signalling network. Recent studies in flies and mammalian tissue culture cells have elucidated many signalling components upstream of TOR complex 1. These studies also suggest that aberrant mammalian TOR complex 1 signalling contributes to a number of pathologies ranging from metabolic diseases to hyperproliferative disorders and cancers. Consequently the efficacies of rapamycin and related compounds in treating such diseases are being evaluated in clinical trials.
DOI: 10.1016/j.biocel.2006.02.013
PubMed: 16647875
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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<author><name sortKey="De Virgilio, Claudio" sort="De Virgilio, Claudio" uniqKey="De Virgilio C" first="Claudio" last="De Virgilio">Claudio De Virgilio</name>
<affiliation wicri:level="4"><nlm:affiliation>Department of Microbiology and Molecular Medicine, University of Geneva, 1211 Geneva 4, Switzerland. Claudio.DeVirgilio@medecine.unige.ch</nlm:affiliation>
<country xml:lang="fr">Suisse</country>
<wicri:regionArea>Department of Microbiology and Molecular Medicine, University of Geneva, 1211 Geneva 4</wicri:regionArea>
<orgName type="university">Université de Genève</orgName>
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<author><name sortKey="Loewith, Robbie" sort="Loewith, Robbie" uniqKey="Loewith R" first="Robbie" last="Loewith">Robbie Loewith</name>
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<series><title level="j">The international journal of biochemistry & cell biology</title>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term>
<term>Humans (MeSH)</term>
<term>Protein Kinases (physiology)</term>
<term>Protein-Serine-Threonine Kinases (physiology)</term>
<term>Saccharomyces cerevisiae Proteins (physiology)</term>
<term>Signal Transduction (physiology)</term>
<term>TOR Serine-Threonine Kinases (MeSH)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term>
<term>Humains (MeSH)</term>
<term>Protein kinases (physiologie)</term>
<term>Protein-Serine-Threonine Kinases (physiologie)</term>
<term>Protéines de Saccharomyces cerevisiae (physiologie)</term>
<term>Sérine-thréonine kinases TOR (MeSH)</term>
<term>Transduction du signal (physiologie)</term>
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<keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Protein Kinases</term>
<term>Protein-Serine-Threonine Kinases</term>
<term>Saccharomyces cerevisiae Proteins</term>
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<keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Protein kinases</term>
<term>Protein-Serine-Threonine Kinases</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Transduction du signal</term>
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<keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Signal Transduction</term>
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<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Humans</term>
<term>TOR Serine-Threonine Kinases</term>
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<keywords scheme="MESH" xml:lang="fr"><term>Animaux</term>
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<front><div type="abstract" xml:lang="en">The target of rapamycin, TOR, is an essential ser/thr protein kinase that functions in two distinct multiprotein complexes, TOR complex 1 and 2. The structure and functions of these complexes have been conserved from yeast to man. TOR complex 1 is inhibited by rapamycin and is thought to couple growth cues to cellular metabolism; TOR complex 2 is not inhibited by rapamycin and appears to regulate spatial aspects of growth such as cell polarity. Work done in a variety of model systems, continues to contribute to our current understanding of this TOR signalling network. Recent studies in flies and mammalian tissue culture cells have elucidated many signalling components upstream of TOR complex 1. These studies also suggest that aberrant mammalian TOR complex 1 signalling contributes to a number of pathologies ranging from metabolic diseases to hyperproliferative disorders and cancers. Consequently the efficacies of rapamycin and related compounds in treating such diseases are being evaluated in clinical trials.</div>
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<Abstract><AbstractText>The target of rapamycin, TOR, is an essential ser/thr protein kinase that functions in two distinct multiprotein complexes, TOR complex 1 and 2. The structure and functions of these complexes have been conserved from yeast to man. TOR complex 1 is inhibited by rapamycin and is thought to couple growth cues to cellular metabolism; TOR complex 2 is not inhibited by rapamycin and appears to regulate spatial aspects of growth such as cell polarity. Work done in a variety of model systems, continues to contribute to our current understanding of this TOR signalling network. Recent studies in flies and mammalian tissue culture cells have elucidated many signalling components upstream of TOR complex 1. These studies also suggest that aberrant mammalian TOR complex 1 signalling contributes to a number of pathologies ranging from metabolic diseases to hyperproliferative disorders and cancers. Consequently the efficacies of rapamycin and related compounds in treating such diseases are being evaluated in clinical trials.</AbstractText>
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