RapamycinFungusV1, Main, Exploration, bibRecord, 000198

The cytosolic form of aspartate aminotransferase is required for full activation of TOR complex 1 in fission yeast.

Identifieur interne : 000198 ( Main/Exploration ); précédent : 000197; suivant : 000199

The cytosolic form of aspartate aminotransferase is required for full activation of TOR complex 1 in fission yeast.

Auteurs : Sophie Reidman [Israël] ; Adiel Cohen [Israël] ; Martin Kupiec [Israël] ; Ronit Weisman [Israël]

Source :

The Journal of biological chemistry [ 1083-351X ] ; 2019.

RBID : pubmed:31641022

Descripteurs français

KwdFr :
- Acide aspartique (pharmacologie), Arginine (pharmacologie), Asparagine (pharmacologie), Aspartate aminotransferases (génétique), Aspartate aminotransferases (métabolisme), Azote (métabolisme), Complexe-1 cible mécanistique de la rapamycine (génétique), Complexe-1 cible mécanistique de la rapamycine (métabolisme), Cytosol (enzymologie), Isoenzymes (génétique), Isoenzymes (métabolisme), Mutation (MeSH), Méthionine sulfoximine (pharmacologie), Protéines de Schizosaccharomyces pombe (génétique), Protéines de Schizosaccharomyces pombe (métabolisme), Régulation de l'expression des gènes fongiques (effets des médicaments et des substances chimiques), Schizosaccharomyces (enzymologie), Schizosaccharomyces (génétique), Schizosaccharomyces (métabolisme), Sirolimus (pharmacologie).
MESH :
- effets des médicaments et des substances chimiques : Régulation de l'expression des gènes fongiques.
- enzymologie : Cytosol, Schizosaccharomyces.
- génétique : Aspartate aminotransferases, Complexe-1 cible mécanistique de la rapamycine, Isoenzymes, Protéines de Schizosaccharomyces pombe, Schizosaccharomyces.
- métabolisme : Aspartate aminotransferases, Azote, Complexe-1 cible mécanistique de la rapamycine, Isoenzymes, Protéines de Schizosaccharomyces pombe, Schizosaccharomyces.
- pharmacologie : Acide aspartique, Arginine, Asparagine, Méthionine sulfoximine, Sirolimus.
- Mutation.

English descriptors

KwdEn :
- Arginine (pharmacology), Asparagine (pharmacology), Aspartate Aminotransferases (genetics), Aspartate Aminotransferases (metabolism), Aspartic Acid (pharmacology), Cytosol (enzymology), Gene Expression Regulation, Fungal (drug effects), Isoenzymes (genetics), Isoenzymes (metabolism), Mechanistic Target of Rapamycin Complex 1 (genetics), Mechanistic Target of Rapamycin Complex 1 (metabolism), Methionine Sulfoximine (pharmacology), Mutation (MeSH), Nitrogen (metabolism), Schizosaccharomyces (enzymology), Schizosaccharomyces (genetics), Schizosaccharomyces (metabolism), Schizosaccharomyces pombe Proteins (genetics), Schizosaccharomyces pombe Proteins (metabolism), Sirolimus (pharmacology).
MESH :
- chemical , genetics : Aspartate Aminotransferases, Isoenzymes, Mechanistic Target of Rapamycin Complex 1, Schizosaccharomyces pombe Proteins.
- chemical , metabolism : Aspartate Aminotransferases, Isoenzymes, Mechanistic Target of Rapamycin Complex 1, Nitrogen, Schizosaccharomyces pombe Proteins.
- chemical , pharmacology : Arginine, Asparagine, Aspartic Acid, Methionine Sulfoximine, Sirolimus.
- drug effects : Gene Expression Regulation, Fungal.
- enzymology : Cytosol, Schizosaccharomyces.
- genetics : Schizosaccharomyces.
- metabolism : Schizosaccharomyces.
- Mutation.

Abstract

The evolutionarily conserved TOR complex 1 (TORC1) activates cell growth and proliferation in response to nutritional signals. In the fission yeast Schizosaccharomyces pombe, TORC1 is essential for vegetative growth, and its activity is regulated in response to nitrogen quantity and quality. Yet, how TORC1 senses nitrogen is poorly understood. Rapamycin, a specific TOR inhibitor, inhibits growth in S. pombe only under conditions in which the activity of TORC1 is compromised. In a genetic screen for rapamycin-sensitive mutations, we isolated caa1-1, a loss-of-function mutation of the cytosolic form of aspartate aminotransferase (Caa1). We demonstrate that loss of caa1⁺ partially mimics loss of TORC1 activity and that Caa1 is required for full TORC1 activity. Disruption of caa1⁺ resulted in aspartate auxotrophy, a finding that prompted us to assess the role of aspartate in TORC1 activation. We found that the amino acids glutamine, asparagine, arginine, aspartate, and serine activate TORC1 most efficiently following nitrogen starvation. The glutamine synthetase inhibitor l-methionine sulfoximine abolished the ability of asparagine, arginine, aspartate, or serine, but not that of glutamine, to induce TORC1 activity, consistent with a central role for glutamine in activating TORC1. Neither addition of aspartate nor addition of glutamine restored TORC1 activity in caa1-deleted cells or in cells carrying a Caa1 variant with a catalytic site substitution, suggesting that the catalytic activity of Caa1 is required for TORC1 activation. Taken together, our results reveal the contribution of the key metabolic enzyme Caa1 to TORC1 activity in S. pombe.

DOI: 10.1074/jbc.RA119.010101
PubMed: 31641022
PubMed Central: PMC6885631

Affiliations:

Israël

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

to stream Main, to step Corpus: 000173
to stream Main, to step Curation: 000173

Le document en format XML

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<term>Asparagine (pharmacology)</term>
<term>Aspartate Aminotransferases (genetics)</term>
<term>Aspartate Aminotransferases (metabolism)</term>
<term>Aspartic Acid (pharmacology)</term>
<term>Cytosol (enzymology)</term>
<term>Gene Expression Regulation, Fungal (drug effects)</term>
<term>Isoenzymes (genetics)</term>
<term>Isoenzymes (metabolism)</term>
<term>Mechanistic Target of Rapamycin Complex 1 (genetics)</term>
<term>Mechanistic Target of Rapamycin Complex 1 (metabolism)</term>
<term>Methionine Sulfoximine (pharmacology)</term>
<term>Mutation (MeSH)</term>
<term>Nitrogen (metabolism)</term>
<term>Schizosaccharomyces (enzymology)</term>
<term>Schizosaccharomyces (genetics)</term>
<term>Schizosaccharomyces (metabolism)</term>
<term>Schizosaccharomyces pombe Proteins (genetics)</term>
<term>Schizosaccharomyces pombe Proteins (metabolism)</term>
<term>Sirolimus (pharmacology)</term>
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<term>Arginine (pharmacologie)</term>
<term>Asparagine (pharmacologie)</term>
<term>Aspartate aminotransferases (génétique)</term>
<term>Aspartate aminotransferases (métabolisme)</term>
<term>Azote (métabolisme)</term>
<term>Complexe-1 cible mécanistique de la rapamycine (génétique)</term>
<term>Complexe-1 cible mécanistique de la rapamycine (métabolisme)</term>
<term>Cytosol (enzymologie)</term>
<term>Isoenzymes (génétique)</term>
<term>Isoenzymes (métabolisme)</term>
<term>Mutation (MeSH)</term>
<term>Méthionine sulfoximine (pharmacologie)</term>
<term>Protéines de Schizosaccharomyces pombe (génétique)</term>
<term>Protéines de Schizosaccharomyces pombe (métabolisme)</term>
<term>Régulation de l'expression des gènes fongiques (effets des médicaments et des substances chimiques)</term>
<term>Schizosaccharomyces (enzymologie)</term>
<term>Schizosaccharomyces (génétique)</term>
<term>Schizosaccharomyces (métabolisme)</term>
<term>Sirolimus (pharmacologie)</term>
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<term>Isoenzymes</term>
<term>Mechanistic Target of Rapamycin Complex 1</term>
<term>Schizosaccharomyces pombe Proteins</term>
</keywords>
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<term>Mechanistic Target of Rapamycin Complex 1</term>
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<term>Methionine Sulfoximine</term>
<term>Sirolimus</term>
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<term>Schizosaccharomyces</term>
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<term>Schizosaccharomyces</term>
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</keywords>
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<term>Complexe-1 cible mécanistique de la rapamycine</term>
<term>Isoenzymes</term>
<term>Protéines de Schizosaccharomyces pombe</term>
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<term>Complexe-1 cible mécanistique de la rapamycine</term>
<term>Isoenzymes</term>
<term>Protéines de Schizosaccharomyces pombe</term>
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<term>Asparagine</term>
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<front><div type="abstract" xml:lang="en">The evolutionarily conserved TOR complex 1 (TORC1) activates cell growth and proliferation in response to nutritional signals. In the fission yeast <i>Schizosaccharomyces pombe</i>
, TORC1 is essential for vegetative growth, and its activity is regulated in response to nitrogen quantity and quality. Yet, how TORC1 senses nitrogen is poorly understood. Rapamycin, a specific TOR inhibitor, inhibits growth in <i>S. pombe</i>
 only under conditions in which the activity of TORC1 is compromised. In a genetic screen for rapamycin-sensitive mutations, we isolated <i>caa1-1</i>
, a loss-of-function mutation of the cytosolic form of aspartate aminotransferase (Caa1). We demonstrate that loss of <i>caa1</i>
<sup>+</sup>
 partially mimics loss of TORC1 activity and that Caa1 is required for full TORC1 activity. Disruption of <i>caa1</i>
<sup>+</sup>
 resulted in aspartate auxotrophy, a finding that prompted us to assess the role of aspartate in TORC1 activation. We found that the amino acids glutamine, asparagine, arginine, aspartate, and serine activate TORC1 most efficiently following nitrogen starvation. The glutamine synthetase inhibitor l-methionine sulfoximine abolished the ability of asparagine, arginine, aspartate, or serine, but not that of glutamine, to induce TORC1 activity, consistent with a central role for glutamine in activating TORC1. Neither addition of aspartate nor addition of glutamine restored TORC1 activity in <i>caa1</i>
-deleted cells or in cells carrying a Caa1 variant with a catalytic site substitution, suggesting that the catalytic activity of Caa1 is required for TORC1 activation. Taken together, our results reveal the contribution of the key metabolic enzyme Caa1 to TORC1 activity in <i>S. pombe</i>
.</div>
</front>
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<Abstract><AbstractText>The evolutionarily conserved TOR complex 1 (TORC1) activates cell growth and proliferation in response to nutritional signals. In the fission yeast <i>Schizosaccharomyces pombe</i>
, TORC1 is essential for vegetative growth, and its activity is regulated in response to nitrogen quantity and quality. Yet, how TORC1 senses nitrogen is poorly understood. Rapamycin, a specific TOR inhibitor, inhibits growth in <i>S. pombe</i>
 only under conditions in which the activity of TORC1 is compromised. In a genetic screen for rapamycin-sensitive mutations, we isolated <i>caa1-1</i>
, a loss-of-function mutation of the cytosolic form of aspartate aminotransferase (Caa1). We demonstrate that loss of <i>caa1</i>
<sup>+</sup>
 partially mimics loss of TORC1 activity and that Caa1 is required for full TORC1 activity. Disruption of <i>caa1</i>
<sup>+</sup>
 resulted in aspartate auxotrophy, a finding that prompted us to assess the role of aspartate in TORC1 activation. We found that the amino acids glutamine, asparagine, arginine, aspartate, and serine activate TORC1 most efficiently following nitrogen starvation. The glutamine synthetase inhibitor l-methionine sulfoximine abolished the ability of asparagine, arginine, aspartate, or serine, but not that of glutamine, to induce TORC1 activity, consistent with a central role for glutamine in activating TORC1. Neither addition of aspartate nor addition of glutamine restored TORC1 activity in <i>caa1</i>
-deleted cells or in cells carrying a Caa1 variant with a catalytic site substitution, suggesting that the catalytic activity of Caa1 is required for TORC1 activation. Taken together, our results reveal the contribution of the key metabolic enzyme Caa1 to TORC1 activity in <i>S. pombe</i>
.</AbstractText>
<CopyrightInformation>© 2019 Reidman et al.</CopyrightInformation>
</Abstract>
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<ForeName>Sophie</ForeName>
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The cytosolic form of aspartate aminotransferase is required for full activation of TOR complex 1 in fission yeast.

The cytosolic form of aspartate aminotransferase is required for full activation of TOR complex 1 in fission yeast.

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