RapamycinFungusV1, Main, Exploration, bibRecord, 000C57

Nitrogen regulates AMPK to control TORC1 signaling.

Identifieur interne : 000C57 ( Main/Exploration ); précédent : 000C56; suivant : 000C58

Nitrogen regulates AMPK to control TORC1 signaling.

Auteurs : Elizabeth Davie [Royaume-Uni] ; Gabriella M A. Forte [Royaume-Uni] ; Janni Petersen [Australie]

Source :

Current biology : CB [ 1879-0445 ] ; 2015.

RBID : pubmed:25639242

Descripteurs français

KwdFr :
- Azote (métabolisme), Complexe-1 cible mécanistique de la rapamycine (MeSH), Complexes multiprotéiques (génétique), Complexes multiprotéiques (métabolisme), Division cellulaire (MeSH), Phosphorylation (MeSH), Protein-Serine-Threonine Kinases (génétique), Protein-Serine-Threonine Kinases (métabolisme), Protéines de Schizosaccharomyces pombe (génétique), Protéines de Schizosaccharomyces pombe (métabolisme), Schizosaccharomyces (enzymologie), Schizosaccharomyces (génétique), Schizosaccharomyces (physiologie), Sérine-thréonine kinases TOR (génétique), Sérine-thréonine kinases TOR (métabolisme), Transduction du signal (MeSH).
MESH :
- enzymologie : Schizosaccharomyces.
- génétique : Complexes multiprotéiques, Protein-Serine-Threonine Kinases, Protéines de Schizosaccharomyces pombe, Schizosaccharomyces, Sérine-thréonine kinases TOR.
- métabolisme : Azote, Complexes multiprotéiques, Protein-Serine-Threonine Kinases, Protéines de Schizosaccharomyces pombe, Sérine-thréonine kinases TOR.
- physiologie : Schizosaccharomyces.
- Complexe-1 cible mécanistique de la rapamycine, Division cellulaire, Phosphorylation, Transduction du signal.

English descriptors

KwdEn :
- Cell Division (MeSH), Mechanistic Target of Rapamycin Complex 1 (MeSH), Multiprotein Complexes (genetics), Multiprotein Complexes (metabolism), Nitrogen (metabolism), Phosphorylation (MeSH), Protein-Serine-Threonine Kinases (genetics), Protein-Serine-Threonine Kinases (metabolism), Schizosaccharomyces (enzymology), Schizosaccharomyces (genetics), Schizosaccharomyces (physiology), Schizosaccharomyces pombe Proteins (genetics), Schizosaccharomyces pombe Proteins (metabolism), Signal Transduction (MeSH), TOR Serine-Threonine Kinases (genetics), TOR Serine-Threonine Kinases (metabolism).
MESH :
- chemical , genetics : Multiprotein Complexes, Protein-Serine-Threonine Kinases, Schizosaccharomyces pombe Proteins, TOR Serine-Threonine Kinases.
- chemical , metabolism : Multiprotein Complexes, Nitrogen, Protein-Serine-Threonine Kinases, Schizosaccharomyces pombe Proteins, TOR Serine-Threonine Kinases.
- chemical : Mechanistic Target of Rapamycin Complex 1.
- enzymology : Schizosaccharomyces.
- genetics : Schizosaccharomyces.
- physiology : Schizosaccharomyces.
- Cell Division, Phosphorylation, Signal Transduction.

Abstract

BACKGROUND

Cell growth and cell-cycle progression are tightly coordinated to enable cells to adjust their size (timing of division) to the demands of proliferation in varying nutritional environments. In fission yeast, nitrogen stress results in sustained proliferation at a reduced size.

RESULTS

Here, we show that cells can sense nitrogen stress to reduce target of rapamycin complex-1 (TORC1) activity. Nitrogen-stress-induced TORC1 inhibition differs from amino-acid-dependent control of TORC1 and requires the Ssp2 (AMPKα) kinase, the Tsc1/2 complex, and Rhb1 GTPase. Importantly, the β and γ regulatory subunits of AMPK are not required to control cell division in response to nitrogen stress, providing evidence for a nitrogen-sensing mechanism that is independent of changes in intracellular ATP/AMP levels. The CaMKK homolog Ssp1 is constitutively required for phosphorylation of the AMPKα(Ssp2) T loop. However, we find that a second homolog CaMKK(Ppk34) is specifically required to stimulate AMPKα(Ssp2) activation in response to nitrogen stress. Finally, ammonia also controls mTORC1 activity in human cells; mTORC1 is activated upon the addition of ammonium to glutamine-starved Hep3B cancer cells.

CONCLUSIONS

The alternative nitrogen source ammonia can simulate TORC1 activity to support growth and division under challenging nutrient settings, a situation often seen in cancer.

DOI: 10.1016/j.cub.2014.12.034
PubMed: 25639242
PubMed Central: PMC4331286

Affiliations:

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

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Le document en format XML

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<term>Mechanistic Target of Rapamycin Complex 1 (MeSH)</term>
<term>Multiprotein Complexes (genetics)</term>
<term>Multiprotein Complexes (metabolism)</term>
<term>Nitrogen (metabolism)</term>
<term>Phosphorylation (MeSH)</term>
<term>Protein-Serine-Threonine Kinases (genetics)</term>
<term>Protein-Serine-Threonine Kinases (metabolism)</term>
<term>Schizosaccharomyces (enzymology)</term>
<term>Schizosaccharomyces (genetics)</term>
<term>Schizosaccharomyces (physiology)</term>
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<term>TOR Serine-Threonine Kinases (genetics)</term>
<term>TOR Serine-Threonine Kinases (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Azote (métabolisme)</term>
<term>Complexe-1 cible mécanistique de la rapamycine (MeSH)</term>
<term>Complexes multiprotéiques (génétique)</term>
<term>Complexes multiprotéiques (métabolisme)</term>
<term>Division cellulaire (MeSH)</term>
<term>Phosphorylation (MeSH)</term>
<term>Protein-Serine-Threonine Kinases (génétique)</term>
<term>Protein-Serine-Threonine Kinases (métabolisme)</term>
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<term>Protéines de Schizosaccharomyces pombe (métabolisme)</term>
<term>Schizosaccharomyces (enzymologie)</term>
<term>Schizosaccharomyces (génétique)</term>
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<term>Sérine-thréonine kinases TOR (génétique)</term>
<term>Sérine-thréonine kinases TOR (métabolisme)</term>
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<term>Protein-Serine-Threonine Kinases</term>
<term>Schizosaccharomyces pombe Proteins</term>
<term>TOR Serine-Threonine Kinases</term>
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<term>Nitrogen</term>
<term>Protein-Serine-Threonine Kinases</term>
<term>Schizosaccharomyces pombe Proteins</term>
<term>TOR Serine-Threonine Kinases</term>
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<term>Protein-Serine-Threonine Kinases</term>
<term>Protéines de Schizosaccharomyces pombe</term>
<term>Schizosaccharomyces</term>
<term>Sérine-thréonine kinases TOR</term>
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<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Azote</term>
<term>Complexes multiprotéiques</term>
<term>Protein-Serine-Threonine Kinases</term>
<term>Protéines de Schizosaccharomyces pombe</term>
<term>Sérine-thréonine kinases TOR</term>
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<term>Phosphorylation</term>
<term>Signal Transduction</term>
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<front><div type="abstract" xml:lang="en"><p><b>BACKGROUND</b>
</p>
<p>Cell growth and cell-cycle progression are tightly coordinated to enable cells to adjust their size (timing of division) to the demands of proliferation in varying nutritional environments. In fission yeast, nitrogen stress results in sustained proliferation at a reduced size.</p>
</div>
<div type="abstract" xml:lang="en"><p><b>RESULTS</b>
</p>
<p>Here, we show that cells can sense nitrogen stress to reduce target of rapamycin complex-1 (TORC1) activity. Nitrogen-stress-induced TORC1 inhibition differs from amino-acid-dependent control of TORC1 and requires the Ssp2 (AMPKα) kinase, the Tsc1/2 complex, and Rhb1 GTPase. Importantly, the β and γ regulatory subunits of AMPK are not required to control cell division in response to nitrogen stress, providing evidence for a nitrogen-sensing mechanism that is independent of changes in intracellular ATP/AMP levels. The CaMKK homolog Ssp1 is constitutively required for phosphorylation of the AMPKα(Ssp2) T loop. However, we find that a second homolog CaMKK(Ppk34) is specifically required to stimulate AMPKα(Ssp2) activation in response to nitrogen stress. Finally, ammonia also controls mTORC1 activity in human cells; mTORC1 is activated upon the addition of ammonium to glutamine-starved Hep3B cancer cells.</p>
</div>
<div type="abstract" xml:lang="en"><p><b>CONCLUSIONS</b>
</p>
<p>The alternative nitrogen source ammonia can simulate TORC1 activity to support growth and division under challenging nutrient settings, a situation often seen in cancer.</p>
</div>
</front>
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<AbstractText Label="RESULTS" NlmCategory="RESULTS">Here, we show that cells can sense nitrogen stress to reduce target of rapamycin complex-1 (TORC1) activity. Nitrogen-stress-induced TORC1 inhibition differs from amino-acid-dependent control of TORC1 and requires the Ssp2 (AMPKα) kinase, the Tsc1/2 complex, and Rhb1 GTPase. Importantly, the β and γ regulatory subunits of AMPK are not required to control cell division in response to nitrogen stress, providing evidence for a nitrogen-sensing mechanism that is independent of changes in intracellular ATP/AMP levels. The CaMKK homolog Ssp1 is constitutively required for phosphorylation of the AMPKα(Ssp2) T loop. However, we find that a second homolog CaMKK(Ppk34) is specifically required to stimulate AMPKα(Ssp2) activation in response to nitrogen stress. Finally, ammonia also controls mTORC1 activity in human cells; mTORC1 is activated upon the addition of ammonium to glutamine-starved Hep3B cancer cells.</AbstractText>
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Nitrogen regulates AMPK to control TORC1 signaling.

Nitrogen regulates AMPK to control TORC1 signaling.

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