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Target of rapamycin complex 1 and Tap42-associated phosphatases are required for sensing changes in nitrogen conditions in the yeast Saccharomyces cerevisiae.

Identifieur interne : 000723 ( Main/Exploration ); précédent : 000722; suivant : 000724

Target of rapamycin complex 1 and Tap42-associated phosphatases are required for sensing changes in nitrogen conditions in the yeast Saccharomyces cerevisiae.

Auteurs : Jinmei Li [République populaire de Chine] ; Gonghong Yan [États-Unis] ; Sichi Liu [République populaire de Chine] ; Tong Jiang [États-Unis] ; Mingming Zhong [États-Unis] ; Wenjie Yuan [République populaire de Chine] ; Shaoxian Chen [République populaire de Chine] ; Yin Zheng [République populaire de Chine] ; Yong Jiang [République populaire de Chine] ; Yu Jiang [États-Unis]

Source :

RBID : pubmed:28976047

Descripteurs français

English descriptors

Abstract

In yeast target of rapamycin complex 1 (TORC1) and Tap42-associated phosphatases regulate expression of genes involved in nitrogen limitation response and the nitrogen discrimination pathway. However, it remains unclear whether TORC1 and the phosphatases are required for sensing nitrogen conditions. Utilizing temperature sensitive mutants of tor2 and tap42, we examined the role of TORC1 and Tap42 in nuclear entry of Gln3, a key transcription factor in yeast nitrogen metabolism, in response to changes in nitrogen conditions. Our data show that TORC1 is essential for Gln3 nuclear entry upon nitrogen limitation and downshift in nitrogen quality. However, Tap42-associated phosphatases are required only under nitrogen limitation condition. In cells grown in poor nitrogen medium, the nitrogen permease reactivator kinase (Npr1) inhibits TORC1 activity and alters its association with Tap42, rendering Tap42-associated phosphatases unresponsive to nitrogen limitation. These findings demonstrate a direct role for TORC1 and Tap42-associated phosphatases in sensing nitrogen conditions and unveil an Npr1-dependent mechanism that controls TORC1 and the phosphatases in response to changes in nitrogen quality.

DOI: 10.1111/mmi.13858
PubMed: 28976047
PubMed Central: PMC5720920


Affiliations:


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<term>Adaptor Proteins, Signal Transducing (metabolism)</term>
<term>Cell Cycle Proteins (genetics)</term>
<term>Cell Cycle Proteins (metabolism)</term>
<term>Gene Expression Regulation, Fungal (MeSH)</term>
<term>Mechanistic Target of Rapamycin Complex 1 (antagonists & inhibitors)</term>
<term>Mechanistic Target of Rapamycin Complex 1 (metabolism)</term>
<term>Mutation (MeSH)</term>
<term>Nitrogen (deficiency)</term>
<term>Nitrogen (metabolism)</term>
<term>Phosphatidylinositol 3-Kinases (genetics)</term>
<term>Phosphatidylinositol 3-Kinases (metabolism)</term>
<term>Phosphoric Monoester Hydrolases (metabolism)</term>
<term>Protein Kinases (pharmacology)</term>
<term>Saccharomyces cerevisiae (genetics)</term>
<term>Saccharomyces cerevisiae (metabolism)</term>
<term>Saccharomyces cerevisiae Proteins (genetics)</term>
<term>Saccharomyces cerevisiae Proteins (metabolism)</term>
<term>Saccharomyces cerevisiae Proteins (pharmacology)</term>
<term>Thermosensing (genetics)</term>
<term>Transcription Factors (genetics)</term>
<term>Transcription Factors (metabolism)</term>
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<term>Azote (déficit)</term>
<term>Azote (métabolisme)</term>
<term>Complexe-1 cible mécanistique de la rapamycine (antagonistes et inhibiteurs)</term>
<term>Complexe-1 cible mécanistique de la rapamycine (métabolisme)</term>
<term>Facteurs de transcription (génétique)</term>
<term>Facteurs de transcription (métabolisme)</term>
<term>Mutation (MeSH)</term>
<term>Phosphatidylinositol 3-kinases (génétique)</term>
<term>Phosphatidylinositol 3-kinases (métabolisme)</term>
<term>Phosphoric monoester hydrolases (métabolisme)</term>
<term>Protein kinases (pharmacologie)</term>
<term>Protéines adaptatrices de la transduction du signal (génétique)</term>
<term>Protéines adaptatrices de la transduction du signal (métabolisme)</term>
<term>Protéines de Saccharomyces cerevisiae (génétique)</term>
<term>Protéines de Saccharomyces cerevisiae (métabolisme)</term>
<term>Protéines de Saccharomyces cerevisiae (pharmacologie)</term>
<term>Protéines du cycle cellulaire (génétique)</term>
<term>Protéines du cycle cellulaire (métabolisme)</term>
<term>Régulation de l'expression des gènes fongiques (MeSH)</term>
<term>Saccharomyces cerevisiae (génétique)</term>
<term>Saccharomyces cerevisiae (métabolisme)</term>
<term>Thermoception (génétique)</term>
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<term>Cell Cycle Proteins</term>
<term>Phosphatidylinositol 3-Kinases</term>
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<term>Transcription Factors</term>
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<term>Adaptor Proteins, Signal Transducing</term>
<term>Cell Cycle Proteins</term>
<term>Mechanistic Target of Rapamycin Complex 1</term>
<term>Nitrogen</term>
<term>Phosphatidylinositol 3-Kinases</term>
<term>Phosphoric Monoester Hydrolases</term>
<term>Saccharomyces cerevisiae Proteins</term>
<term>Transcription Factors</term>
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<term>Saccharomyces cerevisiae Proteins</term>
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<term>Complexe-1 cible mécanistique de la rapamycine</term>
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<term>Azote</term>
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<term>Saccharomyces cerevisiae</term>
<term>Thermosensing</term>
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<keywords scheme="MESH" qualifier="génétique" xml:lang="fr">
<term>Facteurs de transcription</term>
<term>Phosphatidylinositol 3-kinases</term>
<term>Protéines adaptatrices de la transduction du signal</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Protéines du cycle cellulaire</term>
<term>Saccharomyces cerevisiae</term>
<term>Thermoception</term>
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<term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr">
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<term>Complexe-1 cible mécanistique de la rapamycine</term>
<term>Facteurs de transcription</term>
<term>Phosphatidylinositol 3-kinases</term>
<term>Phosphoric monoester hydrolases</term>
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<term>Protéines de Saccharomyces cerevisiae</term>
<term>Protéines du cycle cellulaire</term>
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<term>Protéines de Saccharomyces cerevisiae</term>
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<term>Mutation</term>
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<div type="abstract" xml:lang="en">In yeast target of rapamycin complex 1 (TORC1) and Tap42-associated phosphatases regulate expression of genes involved in nitrogen limitation response and the nitrogen discrimination pathway. However, it remains unclear whether TORC1 and the phosphatases are required for sensing nitrogen conditions. Utilizing temperature sensitive mutants of tor2 and tap42, we examined the role of TORC1 and Tap42 in nuclear entry of Gln3, a key transcription factor in yeast nitrogen metabolism, in response to changes in nitrogen conditions. Our data show that TORC1 is essential for Gln3 nuclear entry upon nitrogen limitation and downshift in nitrogen quality. However, Tap42-associated phosphatases are required only under nitrogen limitation condition. In cells grown in poor nitrogen medium, the nitrogen permease reactivator kinase (Npr1) inhibits TORC1 activity and alters its association with Tap42, rendering Tap42-associated phosphatases unresponsive to nitrogen limitation. These findings demonstrate a direct role for TORC1 and Tap42-associated phosphatases in sensing nitrogen conditions and unveil an Npr1-dependent mechanism that controls TORC1 and the phosphatases in response to changes in nitrogen quality.</div>
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<AbstractText>In yeast target of rapamycin complex 1 (TORC1) and Tap42-associated phosphatases regulate expression of genes involved in nitrogen limitation response and the nitrogen discrimination pathway. However, it remains unclear whether TORC1 and the phosphatases are required for sensing nitrogen conditions. Utilizing temperature sensitive mutants of tor2 and tap42, we examined the role of TORC1 and Tap42 in nuclear entry of Gln3, a key transcription factor in yeast nitrogen metabolism, in response to changes in nitrogen conditions. Our data show that TORC1 is essential for Gln3 nuclear entry upon nitrogen limitation and downshift in nitrogen quality. However, Tap42-associated phosphatases are required only under nitrogen limitation condition. In cells grown in poor nitrogen medium, the nitrogen permease reactivator kinase (Npr1) inhibits TORC1 activity and alters its association with Tap42, rendering Tap42-associated phosphatases unresponsive to nitrogen limitation. These findings demonstrate a direct role for TORC1 and Tap42-associated phosphatases in sensing nitrogen conditions and unveil an Npr1-dependent mechanism that controls TORC1 and the phosphatases in response to changes in nitrogen quality.</AbstractText>
<CopyrightInformation>© 2017 John Wiley & Sons Ltd.</CopyrightInformation>
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<LastName>Yan</LastName>
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