RapamycinFungusV1, Main, Exploration, bibRecord, 000C07

TORC1 promotes phosphorylation of ribosomal protein S6 via the AGC kinase Ypk3 in Saccharomyces cerevisiae.

Identifieur interne : 000C07 ( Main/Exploration ); précédent : 000C06; suivant : 000C08

TORC1 promotes phosphorylation of ribosomal protein S6 via the AGC kinase Ypk3 in Saccharomyces cerevisiae.

Auteurs : Asier González [Suisse] ; Mitsugu Shimobayashi [Suisse] ; Tobias Eisenberg [Autriche] ; David Adrian Merle [Autriche] ; Tobias Pendl [Autriche] ; Michael N. Hall [Suisse] ; Tarek Moustafa [Autriche]

Source :

PloS one [ 1932-6203 ] ; 2015.

RBID : pubmed:25767889

Descripteurs français

English descriptors

KwdEn :
- Analysis of Variance (MeSH), Cyclic Nucleotide-Regulated Protein Kinases (metabolism), Escherichia coli (MeSH), Immunoblotting (MeSH), Phosphorylation (MeSH), Plasmids (genetics), Polymerase Chain Reaction (MeSH), Protein-Serine-Threonine Kinases (metabolism), Ribosomal Protein S6 Kinases (metabolism), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (metabolism), Transcription Factors (metabolism).
MESH :
- chemical , metabolism : Cyclic Nucleotide-Regulated Protein Kinases, Protein-Serine-Threonine Kinases, Ribosomal Protein S6 Kinases, Saccharomyces cerevisiae Proteins, Transcription Factors.
- genetics : Plasmids.
- metabolism : Saccharomyces cerevisiae.
- Analysis of Variance, Escherichia coli, Immunoblotting, Phosphorylation, Polymerase Chain Reaction.

Abstract

The target of rapamycin complex 1 (TORC1) is an evolutionarily conserved sensor of nutrient availability. Genetic and pharmacological studies in the yeast Saccharomyces cerevisiae have provided mechanistic insights on the regulation of TORC1 signaling in response to nutrients. Using a highly specific antibody that recognizes phosphorylation of the bona fide TORC1 target ribosomal protein S6 (Rps6) in yeast, we found that nutrients rapidly induce Rps6 phosphorylation in a TORC1-dependent manner. Moreover, we demonstrate that Ypk3, an AGC kinase which exhibits high homology to human S6 kinase (S6K), is required for the phosphorylation of Rps6 in vivo. Rps6 phosphorylation is completely abolished in cells lacking Ypk3 (ypk3Δ), whereas Sch9, previously reported to be the yeast ortholog of S6K, is dispensable for Rps6 phosphorylation. Phosphorylation-deficient mutations in regulatory motifs of Ypk3 abrogate Rps6 phosphorylation, and complementation of ypk3Δ cells with human S6 kinase restores Rps6 phosphorylation in a rapamycin-sensitive manner. Our findings demonstrate that Ypk3 is a critical component of the TORC1 pathway and that the use of a phospho-S6 specific antibody offers a valuable tool to identify new nutrient-dependent and rapamycin-sensitive targets in vivo.

DOI: 10.1371/journal.pone.0120250
PubMed: 25767889
PubMed Central: PMC4359079

Affiliations:

Autriche, Suisse

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

to stream Main, to step Corpus: 000C93
to stream Main, to step Curation: 000C93

Le document en format XML

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<front><div type="abstract" xml:lang="en">The target of rapamycin complex 1 (TORC1) is an evolutionarily conserved sensor of nutrient availability. Genetic and pharmacological studies in the yeast Saccharomyces cerevisiae have provided mechanistic insights on the regulation of TORC1 signaling in response to nutrients. Using a highly specific antibody that recognizes phosphorylation of the bona fide TORC1 target ribosomal protein S6 (Rps6) in yeast, we found that nutrients rapidly induce Rps6 phosphorylation in a TORC1-dependent manner. Moreover, we demonstrate that Ypk3, an AGC kinase which exhibits high homology to human S6 kinase (S6K), is required for the phosphorylation of Rps6 in vivo. Rps6 phosphorylation is completely abolished in cells lacking Ypk3 (ypk3Δ), whereas Sch9, previously reported to be the yeast ortholog of S6K, is dispensable for Rps6 phosphorylation. Phosphorylation-deficient mutations in regulatory motifs of Ypk3 abrogate Rps6 phosphorylation, and complementation of ypk3Δ cells with human S6 kinase restores Rps6 phosphorylation in a rapamycin-sensitive manner. Our findings demonstrate that Ypk3 is a critical component of the TORC1 pathway and that the use of a phospho-S6 specific antibody offers a valuable tool to identify new nutrient-dependent and rapamycin-sensitive targets in vivo. </div>
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	Serveur d'exploration sur la rapamycine et les champignons
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TORC1 promotes phosphorylation of ribosomal protein S6 via the AGC kinase Ypk3 in Saccharomyces cerevisiae.

TORC1 promotes phosphorylation of ribosomal protein S6 via the AGC kinase Ypk3 in Saccharomyces cerevisiae.

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