RapamycinFungusV1, Main, Exploration, bibRecord, 001101

Tor1 regulates protein solubility in Saccharomyces cerevisiae.

Identifieur interne : 001101 ( Main/Exploration ); précédent : 001100; suivant : 001102

Tor1 regulates protein solubility in Saccharomyces cerevisiae.

Auteurs : Theodore W. Peters [États-Unis] ; Matthew J. Rardin ; Gregg Czerwieniec ; Uday S. Evani ; Pedro Reis-Rodrigues ; Gordon J. Lithgow ; Sean D. Mooney ; Bradford W. Gibson ; Robert E. Hughes

Source :

Molecular biology of the cell [ 1939-4586 ] ; 2012.

RBID : pubmed:23097491

Descripteurs français

English descriptors

KwdEn :
- Autophagy (MeSH), Autophagy-Related Protein 7 (MeSH), Autophagy-Related Proteins (MeSH), Electrophoresis, Polyacrylamide Gel (MeSH), Mass Spectrometry (MeSH), Mechanistic Target of Rapamycin Complex 1 (MeSH), Mitosis (MeSH), Multiprotein Complexes (metabolism), Mutation (MeSH), Nitrogen (metabolism), Phosphatidylinositol 3-Kinases (genetics), Phosphatidylinositol 3-Kinases (metabolism), Phosphorylation (MeSH), Protein Kinases (genetics), Protein Kinases (metabolism), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (growth & development), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism), Sodium Dodecyl Sulfate (chemistry), Solubility (MeSH), TOR Serine-Threonine Kinases (metabolism), Time Factors (MeSH).
MESH :
- chemical , chemistry : Sodium Dodecyl Sulfate.
- chemical , genetics : Phosphatidylinositol 3-Kinases, Protein Kinases, Saccharomyces cerevisiae Proteins.
- chemical , metabolism : Multiprotein Complexes, Nitrogen, Phosphatidylinositol 3-Kinases, Protein Kinases, Saccharomyces cerevisiae Proteins, TOR Serine-Threonine Kinases.
- chemical : Autophagy-Related Protein 7, Autophagy-Related Proteins, Mechanistic Target of Rapamycin Complex 1.
- genetics : Saccharomyces cerevisiae.
- growth & development : Saccharomyces cerevisiae.
- metabolism : Saccharomyces cerevisiae.
- Autophagy, Electrophoresis, Polyacrylamide Gel, Mass Spectrometry, Mitosis, Mutation, Phosphorylation, Solubility, Time Factors.

Abstract

Accumulation of insoluble protein in cells is associated with aging and aging-related diseases; however, the roles of insoluble protein in these processes are uncertain. The nature and impact of changes to protein solubility during normal aging are less well understood. Using quantitative mass spectrometry, we identify 480 proteins that become insoluble during postmitotic aging in Saccharomyces cerevisiae and show that this ensemble of insoluble proteins is similar to those that accumulate in aging nematodes. SDS-insoluble protein is present exclusively in a nonquiescent subpopulation of postmitotic cells, indicating an asymmetrical distribution of this protein. In addition, we show that nitrogen starvation of young cells is sufficient to cause accumulation of a similar group of insoluble proteins. Although many of the insoluble proteins identified are known to be autophagic substrates, induction of macroautophagy is not required for insoluble protein formation. However, genetic or chemical inhibition of the Tor1 kinase is sufficient to promote accumulation of insoluble protein. We conclude that target of rapamycin complex 1 regulates accumulation of insoluble proteins via mechanisms acting upstream of macroautophagy. Our data indicate that the accumulation of proteins in an SDS-insoluble state in postmitotic cells represents a novel autophagic cargo preparation process that is regulated by the Tor1 kinase.

DOI: 10.1091/mbc.E12-08-0620
PubMed: 23097491
PubMed Central: PMC3521677

Affiliations:

Links toward previous steps (curation, corpus...)

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to stream Main, to step Curation: 001095

Le document en format XML

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<term>Autophagy-Related Protein 7 (MeSH)</term>
<term>Autophagy-Related Proteins (MeSH)</term>
<term>Electrophoresis, Polyacrylamide Gel (MeSH)</term>
<term>Mass Spectrometry (MeSH)</term>
<term>Mechanistic Target of Rapamycin Complex 1 (MeSH)</term>
<term>Mitosis (MeSH)</term>
<term>Multiprotein Complexes (metabolism)</term>
<term>Mutation (MeSH)</term>
<term>Nitrogen (metabolism)</term>
<term>Phosphatidylinositol 3-Kinases (genetics)</term>
<term>Phosphatidylinositol 3-Kinases (metabolism)</term>
<term>Phosphorylation (MeSH)</term>
<term>Protein Kinases (genetics)</term>
<term>Protein Kinases (metabolism)</term>
<term>Saccharomyces cerevisiae (genetics)</term>
<term>Saccharomyces cerevisiae (growth & development)</term>
<term>Saccharomyces cerevisiae (metabolism)</term>
<term>Saccharomyces cerevisiae Proteins (genetics)</term>
<term>Saccharomyces cerevisiae Proteins (metabolism)</term>
<term>Sodium Dodecyl Sulfate (chemistry)</term>
<term>Solubility (MeSH)</term>
<term>TOR Serine-Threonine Kinases (metabolism)</term>
<term>Time Factors (MeSH)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Autophagie (MeSH)</term>
<term>Azote (métabolisme)</term>
<term>Complexe-1 cible mécanistique de la rapamycine (MeSH)</term>
<term>Complexes multiprotéiques (métabolisme)</term>
<term>Dodécyl-sulfate de sodium (composition chimique)</term>
<term>Facteurs temps (MeSH)</term>
<term>Mitose (MeSH)</term>
<term>Mutation (MeSH)</term>
<term>Phosphatidylinositol 3-kinases (génétique)</term>
<term>Phosphatidylinositol 3-kinases (métabolisme)</term>
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<term>Protein kinases (génétique)</term>
<term>Protein kinases (métabolisme)</term>
<term>Protéine-7 associée à l'autophagie (MeSH)</term>
<term>Protéines associées à l'autophagie (MeSH)</term>
<term>Protéines de Saccharomyces cerevisiae (génétique)</term>
<term>Protéines de Saccharomyces cerevisiae (métabolisme)</term>
<term>Saccharomyces cerevisiae (croissance et développement)</term>
<term>Saccharomyces cerevisiae (génétique)</term>
<term>Saccharomyces cerevisiae (métabolisme)</term>
<term>Solubilité (MeSH)</term>
<term>Spectrométrie de masse (MeSH)</term>
<term>Sérine-thréonine kinases TOR (métabolisme)</term>
<term>Électrophorèse sur gel de polyacrylamide (MeSH)</term>
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<term>Protein Kinases</term>
<term>Saccharomyces cerevisiae Proteins</term>
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<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Multiprotein Complexes</term>
<term>Nitrogen</term>
<term>Phosphatidylinositol 3-Kinases</term>
<term>Protein Kinases</term>
<term>Saccharomyces cerevisiae Proteins</term>
<term>TOR Serine-Threonine Kinases</term>
</keywords>
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<term>Autophagy-Related Proteins</term>
<term>Mechanistic Target of Rapamycin Complex 1</term>
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<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Saccharomyces cerevisiae</term>
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<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Phosphatidylinositol 3-kinases</term>
<term>Protein kinases</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Saccharomyces cerevisiae</term>
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<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Azote</term>
<term>Complexes multiprotéiques</term>
<term>Phosphatidylinositol 3-kinases</term>
<term>Protein kinases</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Saccharomyces cerevisiae</term>
<term>Sérine-thréonine kinases TOR</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Autophagy</term>
<term>Electrophoresis, Polyacrylamide Gel</term>
<term>Mass Spectrometry</term>
<term>Mitosis</term>
<term>Mutation</term>
<term>Phosphorylation</term>
<term>Solubility</term>
<term>Time Factors</term>
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<term>Complexe-1 cible mécanistique de la rapamycine</term>
<term>Facteurs temps</term>
<term>Mitose</term>
<term>Mutation</term>
<term>Phosphorylation</term>
<term>Protéine-7 associée à l'autophagie</term>
<term>Protéines associées à l'autophagie</term>
<term>Solubilité</term>
<term>Spectrométrie de masse</term>
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<front><div type="abstract" xml:lang="en">Accumulation of insoluble protein in cells is associated with aging and aging-related diseases; however, the roles of insoluble protein in these processes are uncertain. The nature and impact of changes to protein solubility during normal aging are less well understood. Using quantitative mass spectrometry, we identify 480 proteins that become insoluble during postmitotic aging in Saccharomyces cerevisiae and show that this ensemble of insoluble proteins is similar to those that accumulate in aging nematodes. SDS-insoluble protein is present exclusively in a nonquiescent subpopulation of postmitotic cells, indicating an asymmetrical distribution of this protein. In addition, we show that nitrogen starvation of young cells is sufficient to cause accumulation of a similar group of insoluble proteins. Although many of the insoluble proteins identified are known to be autophagic substrates, induction of macroautophagy is not required for insoluble protein formation. However, genetic or chemical inhibition of the Tor1 kinase is sufficient to promote accumulation of insoluble protein. We conclude that target of rapamycin complex 1 regulates accumulation of insoluble proteins via mechanisms acting upstream of macroautophagy. Our data indicate that the accumulation of proteins in an SDS-insoluble state in postmitotic cells represents a novel autophagic cargo preparation process that is regulated by the Tor1 kinase.</div>
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<Abstract><AbstractText>Accumulation of insoluble protein in cells is associated with aging and aging-related diseases; however, the roles of insoluble protein in these processes are uncertain. The nature and impact of changes to protein solubility during normal aging are less well understood. Using quantitative mass spectrometry, we identify 480 proteins that become insoluble during postmitotic aging in Saccharomyces cerevisiae and show that this ensemble of insoluble proteins is similar to those that accumulate in aging nematodes. SDS-insoluble protein is present exclusively in a nonquiescent subpopulation of postmitotic cells, indicating an asymmetrical distribution of this protein. In addition, we show that nitrogen starvation of young cells is sufficient to cause accumulation of a similar group of insoluble proteins. Although many of the insoluble proteins identified are known to be autophagic substrates, induction of macroautophagy is not required for insoluble protein formation. However, genetic or chemical inhibition of the Tor1 kinase is sufficient to promote accumulation of insoluble protein. We conclude that target of rapamycin complex 1 regulates accumulation of insoluble proteins via mechanisms acting upstream of macroautophagy. Our data indicate that the accumulation of proteins in an SDS-insoluble state in postmitotic cells represents a novel autophagic cargo preparation process that is regulated by the Tor1 kinase.</AbstractText>
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	Serveur d'exploration sur la rapamycine et les champignons
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Tor1 regulates protein solubility in Saccharomyces cerevisiae.

Tor1 regulates protein solubility in Saccharomyces cerevisiae.

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