RapamycinFungusV1, Main, Exploration, bibRecord, 001682

Stress-responsive Gln3 localization in Saccharomyces cerevisiae is separable from and can overwhelm nitrogen source regulation.

Identifieur interne : 001682 ( Main/Exploration ); précédent : 001681; suivant : 001683

Stress-responsive Gln3 localization in Saccharomyces cerevisiae is separable from and can overwhelm nitrogen source regulation.

Auteurs : Jennifer J. Tate [États-Unis] ; Terrance G. Cooper

Source :

The Journal of biological chemistry [ 0021-9258 ] ; 2007.

RBID : pubmed:17439949

Descripteurs français

English descriptors

KwdEn :
- Carbon (metabolism), Cell Nucleus (metabolism), Cytoplasm (metabolism), Gene Expression Regulation, Fungal (MeSH), Glutamine (metabolism), Methionine Sulfoximine (metabolism), Models, Biological (MeSH), Nitrogen (metabolism), Phosphorylation (MeSH), Proline (metabolism), Repressor Proteins (metabolism), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (metabolism), Signal Transduction (MeSH), Sirolimus (pharmacology), Sodium Chloride (pharmacology), Transcription Factors (metabolism).
MESH :
- chemical , metabolism : Carbon, Glutamine, Methionine Sulfoximine, Nitrogen, Proline, Repressor Proteins, Saccharomyces cerevisiae Proteins, Transcription Factors.
- metabolism : Cell Nucleus, Cytoplasm, Saccharomyces cerevisiae.
- chemical , pharmacology : Sirolimus, Sodium Chloride.
- Gene Expression Regulation, Fungal, Models, Biological, Phosphorylation, Signal Transduction.

Abstract

Intracellular localization of Saccharomyces cerevisiae GATA family transcription activator, Gln3, is used as a downstream readout of rapamycin-inhibited Tor1,2 control of Tap42 and Sit4 activities. Gln3 is cytoplasmic in cells provided with repressive nitrogen sources such as glutamine and is nuclear in cells growing with a derepressive nitrogen source such as proline or those treated with rapamycin or methionine sulfoximine (Msx). Although gross Gln3-Myc13 phosphorylation levels in wild type cells do not correlate with nitrogen source-determined intracellular Gln3-Myc13 localization, the phosphorylation levels are markedly influenced by several environmental perturbations. Msx treatment increases Snf1-independent Gln3-Myc13 phosphorylation, whereas carbon starvation increases both Snf1-dependent and -independent Gln3-Myc13 phosphorylation. Here we demonstrate that a broad spectrum of environmental stresses (temperature, osmotic, and oxidative) increase Gln3-Myc13 phosphorylation. In parallel, these stresses elicit rapid (<5 min for NaCl) Gln3-Myc13 relocalization from the nucleus to the cytoplasm. The response of Gln3-Myc13 localization to stressful conditions can completely overwhelm its response to nitrogen source quality or inhibitor-generated disruption of the Tor1,2 signal transduction pathway. Adding NaCl to cells cultured under conditions in which Gln3-Myc13 is normally nuclear, i.e. proline-grown, nitrogen-starved, Msx-, caffeine-, and rapamycin-treated wild type cells, or ure2Delta cells, results in its prompt relocalization to the cytoplasm. Together these data identify a major new level of regulation to which Gln3 responds, and adds a new dimension to mechanistic studies of the regulation of this transcription factor.

DOI: 10.1074/jbc.M609550200
PubMed: 17439949
PubMed Central: PMC2269007

Affiliations:

États-Unis

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Le document en format XML

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<term>Methionine Sulfoximine (metabolism)</term>
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<term>Transcription Factors (metabolism)</term>
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<term>Glutamine (métabolisme)</term>
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<term>Protéines de Saccharomyces cerevisiae (métabolisme)</term>
<term>Protéines de répression (métabolisme)</term>
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<term>Sirolimus (pharmacologie)</term>
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<front><div type="abstract" xml:lang="en">Intracellular localization of Saccharomyces cerevisiae GATA family transcription activator, Gln3, is used as a downstream readout of rapamycin-inhibited Tor1,2 control of Tap42 and Sit4 activities. Gln3 is cytoplasmic in cells provided with repressive nitrogen sources such as glutamine and is nuclear in cells growing with a derepressive nitrogen source such as proline or those treated with rapamycin or methionine sulfoximine (Msx). Although gross Gln3-Myc13 phosphorylation levels in wild type cells do not correlate with nitrogen source-determined intracellular Gln3-Myc13 localization, the phosphorylation levels are markedly influenced by several environmental perturbations. Msx treatment increases Snf1-independent Gln3-Myc13 phosphorylation, whereas carbon starvation increases both Snf1-dependent and -independent Gln3-Myc13 phosphorylation. Here we demonstrate that a broad spectrum of environmental stresses (temperature, osmotic, and oxidative) increase Gln3-Myc13 phosphorylation. In parallel, these stresses elicit rapid (<5 min for NaCl) Gln3-Myc13 relocalization from the nucleus to the cytoplasm. The response of Gln3-Myc13 localization to stressful conditions can completely overwhelm its response to nitrogen source quality or inhibitor-generated disruption of the Tor1,2 signal transduction pathway. Adding NaCl to cells cultured under conditions in which Gln3-Myc13 is normally nuclear, i.e. proline-grown, nitrogen-starved, Msx-, caffeine-, and rapamycin-treated wild type cells, or ure2Delta cells, results in its prompt relocalization to the cytoplasm. Together these data identify a major new level of regulation to which Gln3 responds, and adds a new dimension to mechanistic studies of the regulation of this transcription factor.</div>
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<Abstract><AbstractText>Intracellular localization of Saccharomyces cerevisiae GATA family transcription activator, Gln3, is used as a downstream readout of rapamycin-inhibited Tor1,2 control of Tap42 and Sit4 activities. Gln3 is cytoplasmic in cells provided with repressive nitrogen sources such as glutamine and is nuclear in cells growing with a derepressive nitrogen source such as proline or those treated with rapamycin or methionine sulfoximine (Msx). Although gross Gln3-Myc13 phosphorylation levels in wild type cells do not correlate with nitrogen source-determined intracellular Gln3-Myc13 localization, the phosphorylation levels are markedly influenced by several environmental perturbations. Msx treatment increases Snf1-independent Gln3-Myc13 phosphorylation, whereas carbon starvation increases both Snf1-dependent and -independent Gln3-Myc13 phosphorylation. Here we demonstrate that a broad spectrum of environmental stresses (temperature, osmotic, and oxidative) increase Gln3-Myc13 phosphorylation. In parallel, these stresses elicit rapid (<5 min for NaCl) Gln3-Myc13 relocalization from the nucleus to the cytoplasm. The response of Gln3-Myc13 localization to stressful conditions can completely overwhelm its response to nitrogen source quality or inhibitor-generated disruption of the Tor1,2 signal transduction pathway. Adding NaCl to cells cultured under conditions in which Gln3-Myc13 is normally nuclear, i.e. proline-grown, nitrogen-starved, Msx-, caffeine-, and rapamycin-treated wild type cells, or ure2Delta cells, results in its prompt relocalization to the cytoplasm. Together these data identify a major new level of regulation to which Gln3 responds, and adds a new dimension to mechanistic studies of the regulation of this transcription factor.</AbstractText>
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	Serveur d'exploration sur la rapamycine et les champignons
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Stress-responsive Gln3 localization in Saccharomyces cerevisiae is separable from and can overwhelm nitrogen source regulation.

Stress-responsive Gln3 localization in Saccharomyces cerevisiae is separable from and can overwhelm nitrogen source regulation.

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