RapamycinFungusV1, Main, Exploration, bibRecord, 000E07

Stress conditions promote yeast Gap1 permease ubiquitylation and down-regulation via the arrestin-like Bul and Aly proteins.

Identifieur interne : 000E07 ( Main/Exploration ); précédent : 000E06; suivant : 000E08

Stress conditions promote yeast Gap1 permease ubiquitylation and down-regulation via the arrestin-like Bul and Aly proteins.

Auteurs : Myriam Crapeau [Belgique] ; Ahmad Merhi [Belgique] ; Bruno André [Belgique]

Source :

The Journal of biological chemistry [ 1083-351X ] ; 2014.

RBID : pubmed:24942738

Descripteurs français

English descriptors

KwdEn :
- 14-3-3 Proteins (metabolism), Adaptor Proteins, Signal Transducing (metabolism), Amino Acid Transport Systems (chemistry), Amino Acid Transport Systems (genetics), Amino Acid Transport Systems (metabolism), Amino Acids (metabolism), Arrestins (metabolism), Binding Sites (MeSH), Down-Regulation (drug effects), Lysine (chemistry), Models, Biological (MeSH), Models, Molecular (MeSH), Saccharomyces cerevisiae (drug effects), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (antagonists & inhibitors), Saccharomyces cerevisiae Proteins (chemistry), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism), Sirolimus (pharmacology), Stress, Physiological (MeSH), Transcription Factors (antagonists & inhibitors), Ubiquitin-Protein Ligases (metabolism), Ubiquitination (drug effects).
MESH :
- chemical , antagonists & inhibitors : Saccharomyces cerevisiae Proteins, Transcription Factors.
- chemical , chemistry : Amino Acid Transport Systems, Lysine, Saccharomyces cerevisiae Proteins.
- chemical , genetics : Amino Acid Transport Systems, Saccharomyces cerevisiae Proteins.
- chemical , metabolism : 14-3-3 Proteins, Adaptor Proteins, Signal Transducing, Amino Acid Transport Systems, Amino Acids, Arrestins, Saccharomyces cerevisiae Proteins, Ubiquitin-Protein Ligases.
- drug effects : Down-Regulation, Saccharomyces cerevisiae, Ubiquitination.
- genetics : Saccharomyces cerevisiae.
- metabolism : Saccharomyces cerevisiae.
- chemical , pharmacology : Sirolimus.
- Binding Sites, Models, Biological, Models, Molecular, Stress, Physiological.

Abstract

Gap1, the yeast general amino acid permease, is a convenient model for studying how the intracellular traffic of membrane transporters is regulated. Present at the plasma membrane under poor nitrogen supply conditions, it undergoes ubiquitylation, endocytosis, and degradation upon activation of the TORC1 kinase complex in response to an increase in internal amino acids. This down-regulation is stimulated by TORC1-dependent phosphoinhibition of the Npr1 kinase, resulting in activation by dephosphorylation of the arrestin-like Bul1 and Bul2 adaptors recruiting the Rsp5 ubiquitin ligase to Gap1. We report here that Gap1 is also down-regulated when cells are treated with the TORC1 inhibitor rapamycin or subjected to various stresses and that a lack of the Tco89 subunit of TORC1 causes constitutive Gap1 down-regulation. Both the Bul1 and Bul2 and the Aly1 and Aly2 arrestin-like adaptors of Rsp5 promote this down-regulation without undergoing dephosphorylation. Furthermore, they act via the C-terminal regions of Gap1 not involved in ubiquitylation in response to internal amino acids, whereas a Gap1 mutant altered in the N-terminal tail and resistant to ubiquitylation by internal amino acids is efficiently down-regulated under stress via the Bul and Aly adaptors. Although the Bul proteins mediate Gap1 ubiquitylation of two possible lysines, Lys-9 and Lys-16, the Aly proteins promote ubiquitylation of the Lys-16 residue only. This stress-induced pathway of Gap1 down-regulation targets other permeases as well, and it likely allows cells facing adverse conditions to retrieve amino acids from permease degradation.

DOI: 10.1074/jbc.M114.582320
PubMed: 24942738
PubMed Central: PMC4139224

Affiliations:

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

to stream Main, to step Corpus: 000E28
to stream Main, to step Curation: 000E28

Le document en format XML

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<term>Amino Acid Transport Systems (chemistry)</term>
<term>Amino Acid Transport Systems (genetics)</term>
<term>Amino Acid Transport Systems (metabolism)</term>
<term>Amino Acids (metabolism)</term>
<term>Arrestins (metabolism)</term>
<term>Binding Sites (MeSH)</term>
<term>Down-Regulation (drug effects)</term>
<term>Lysine (chemistry)</term>
<term>Models, Biological (MeSH)</term>
<term>Models, Molecular (MeSH)</term>
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<term>Saccharomyces cerevisiae (genetics)</term>
<term>Saccharomyces cerevisiae (metabolism)</term>
<term>Saccharomyces cerevisiae Proteins (antagonists & inhibitors)</term>
<term>Saccharomyces cerevisiae Proteins (chemistry)</term>
<term>Saccharomyces cerevisiae Proteins (genetics)</term>
<term>Saccharomyces cerevisiae Proteins (metabolism)</term>
<term>Sirolimus (pharmacology)</term>
<term>Stress, Physiological (MeSH)</term>
<term>Transcription Factors (antagonists & inhibitors)</term>
<term>Ubiquitin-Protein Ligases (metabolism)</term>
<term>Ubiquitination (drug effects)</term>
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<term>Facteurs de transcription (antagonistes et inhibiteurs)</term>
<term>Lysine (composition chimique)</term>
<term>Modèles biologiques (MeSH)</term>
<term>Modèles moléculaires (MeSH)</term>
<term>Protéines 14-3-3 (métabolisme)</term>
<term>Protéines adaptatrices de la transduction du signal (métabolisme)</term>
<term>Protéines de Saccharomyces cerevisiae (antagonistes et inhibiteurs)</term>
<term>Protéines de Saccharomyces cerevisiae (composition chimique)</term>
<term>Protéines de Saccharomyces cerevisiae (génétique)</term>
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<term>Saccharomyces cerevisiae (métabolisme)</term>
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<term>Systèmes de transport d'acides aminés (métabolisme)</term>
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<term>Protéines 14-3-3</term>
<term>Protéines adaptatrices de la transduction du signal</term>
<term>Protéines de Saccharomyces cerevisiae</term>
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<front><div type="abstract" xml:lang="en">Gap1, the yeast general amino acid permease, is a convenient model for studying how the intracellular traffic of membrane transporters is regulated. Present at the plasma membrane under poor nitrogen supply conditions, it undergoes ubiquitylation, endocytosis, and degradation upon activation of the TORC1 kinase complex in response to an increase in internal amino acids. This down-regulation is stimulated by TORC1-dependent phosphoinhibition of the Npr1 kinase, resulting in activation by dephosphorylation of the arrestin-like Bul1 and Bul2 adaptors recruiting the Rsp5 ubiquitin ligase to Gap1. We report here that Gap1 is also down-regulated when cells are treated with the TORC1 inhibitor rapamycin or subjected to various stresses and that a lack of the Tco89 subunit of TORC1 causes constitutive Gap1 down-regulation. Both the Bul1 and Bul2 and the Aly1 and Aly2 arrestin-like adaptors of Rsp5 promote this down-regulation without undergoing dephosphorylation. Furthermore, they act via the C-terminal regions of Gap1 not involved in ubiquitylation in response to internal amino acids, whereas a Gap1 mutant altered in the N-terminal tail and resistant to ubiquitylation by internal amino acids is efficiently down-regulated under stress via the Bul and Aly adaptors. Although the Bul proteins mediate Gap1 ubiquitylation of two possible lysines, Lys-9 and Lys-16, the Aly proteins promote ubiquitylation of the Lys-16 residue only. This stress-induced pathway of Gap1 down-regulation targets other permeases as well, and it likely allows cells facing adverse conditions to retrieve amino acids from permease degradation. </div>
</front>
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<Abstract><AbstractText>Gap1, the yeast general amino acid permease, is a convenient model for studying how the intracellular traffic of membrane transporters is regulated. Present at the plasma membrane under poor nitrogen supply conditions, it undergoes ubiquitylation, endocytosis, and degradation upon activation of the TORC1 kinase complex in response to an increase in internal amino acids. This down-regulation is stimulated by TORC1-dependent phosphoinhibition of the Npr1 kinase, resulting in activation by dephosphorylation of the arrestin-like Bul1 and Bul2 adaptors recruiting the Rsp5 ubiquitin ligase to Gap1. We report here that Gap1 is also down-regulated when cells are treated with the TORC1 inhibitor rapamycin or subjected to various stresses and that a lack of the Tco89 subunit of TORC1 causes constitutive Gap1 down-regulation. Both the Bul1 and Bul2 and the Aly1 and Aly2 arrestin-like adaptors of Rsp5 promote this down-regulation without undergoing dephosphorylation. Furthermore, they act via the C-terminal regions of Gap1 not involved in ubiquitylation in response to internal amino acids, whereas a Gap1 mutant altered in the N-terminal tail and resistant to ubiquitylation by internal amino acids is efficiently down-regulated under stress via the Bul and Aly adaptors. Although the Bul proteins mediate Gap1 ubiquitylation of two possible lysines, Lys-9 and Lys-16, the Aly proteins promote ubiquitylation of the Lys-16 residue only. This stress-induced pathway of Gap1 down-regulation targets other permeases as well, and it likely allows cells facing adverse conditions to retrieve amino acids from permease degradation. </AbstractText>
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<ForeName>Bruno</ForeName>
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<AffiliationInfo><Affiliation>From Molecular Physiology of the Cell, Institut de Biologie et de Médecine Moléculaires, Université Libre de Bruxelles, 6041 Gosselies, Belgium bran@ulb.ac.be.</Affiliation>
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	Serveur d'exploration sur la rapamycine et les champignons
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Stress conditions promote yeast Gap1 permease ubiquitylation and down-regulation via the arrestin-like Bul and Aly proteins.

Stress conditions promote yeast Gap1 permease ubiquitylation and down-regulation via the arrestin-like Bul and Aly proteins.

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