RapamycinFungusV1, Main, Exploration, bibRecord, 001929

Quantitation of changes in protein phosphorylation: a simple method based on stable isotope labeling and mass spectrometry.

Identifieur interne : 001929 ( Main/Exploration ); précédent : 001928; suivant : 001930

Quantitation of changes in protein phosphorylation: a simple method based on stable isotope labeling and mass spectrometry.

Auteurs : Debora Bonenfant [Suisse] ; Tobias Schmelzle ; Estela Jacinto ; Jose L. Crespo ; Thierry Mini ; Michael N. Hall ; Paul Jenoe

Source :

Proceedings of the National Academy of Sciences of the United States of America [ 0027-8424 ] ; 2003.

RBID : pubmed:12540831

Descripteurs français

KwdFr :
- Glutathione transferase (métabolisme), Isotopes (composition chimique), Modèles biologiques (MeSH), Mutation (MeSH), Peptides (composition chimique), Phosphorylation (MeSH), Plasmides (métabolisme), Protéines (composition chimique), Protéines de Saccharomyces cerevisiae (métabolisme), Protéines et peptides de signalisation intracellulaire (MeSH), Saccharomyces cerevisiae (métabolisme), Spectrométrie de masse (méthodes), Spectrométrie de masse MALDI (MeSH), Sérine (métabolisme), Transduction du signal (MeSH), Trypsine (pharmacologie), Électrophorèse sur gel de polyacrylamide (MeSH).
MESH :
- composition chimique : Isotopes, Peptides, Protéines.
- métabolisme : Glutathione transferase, Plasmides, Protéines de Saccharomyces cerevisiae, Saccharomyces cerevisiae, Sérine.
- méthodes : Spectrométrie de masse.
- pharmacologie : Trypsine.
- Modèles biologiques, Mutation, Phosphorylation, Protéines et peptides de signalisation intracellulaire, Spectrométrie de masse MALDI, Transduction du signal, Électrophorèse sur gel de polyacrylamide.

English descriptors

KwdEn :
- Electrophoresis, Polyacrylamide Gel (MeSH), Glutathione Transferase (metabolism), Intracellular Signaling Peptides and Proteins (MeSH), Isotopes (chemistry), Mass Spectrometry (methods), Models, Biological (MeSH), Mutation (MeSH), Peptides (chemistry), Phosphorylation (MeSH), Plasmids (metabolism), Proteins (chemistry), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (metabolism), Serine (metabolism), Signal Transduction (MeSH), Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization (MeSH), Trypsin (pharmacology).
MESH :
- chemical , chemistry : Isotopes, Peptides, Proteins.
- chemical , metabolism : Glutathione Transferase, Saccharomyces cerevisiae Proteins, Serine.
- metabolism : Plasmids, Saccharomyces cerevisiae.
- methods : Mass Spectrometry.
- chemical , pharmacology : Trypsin.
- Electrophoresis, Polyacrylamide Gel, Intracellular Signaling Peptides and Proteins, Models, Biological, Mutation, Phosphorylation, Signal Transduction, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization.

Abstract

Reversible protein phosphorylation plays an important role in many cellular processes. However, a simple and reliable method to measure changes in the extent of phosphorylation is lacking. Here, we present a method to quantitate the changes in phosphorylation occurring in a protein in response to a stimulus. The method consists of three steps: (i) enzymatic digestion in H(2)16O or isotopically enriched H(2)18O to label individual pools of differentially phosphorylated proteins; (ii) affinity selection of phosphopeptides from the combined digests by immobilized metal-affinity chromatography; and (iii) dephosphorylation with alkaline phosphatase to allow for quantitation of changes of phosphorylation by matrix-assisted laser desorption ionization time-of-flight mass spectrometry. We applied this strategy to the analysis of the yeast nitrogen permease reactivator protein kinase involved in the target of rapamycin signaling pathway. Alteration in the extent of phosphorylation at Ser-353 and Ser-357 could be easily assessed and quantitated both in wild-type yeast cells treated with rapamycin and in cells lacking the SIT4 phosphatase responsible for dephosphorylating nitrogen permease reactivator protein. The method described here is simple and allows quantitation of relative changes in the level of phosphorylation in signaling proteins, thus yielding information critical for understanding the regulation of complex protein phosphorylation cascades.

DOI: 10.1073/pnas.232735599
PubMed: 12540831
PubMed Central: PMC298695

Affiliations:

Suisse

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

to stream Main, to step Corpus: 001950
to stream Main, to step Curation: 001950

Le document en format XML

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<front><div type="abstract" xml:lang="en">Reversible protein phosphorylation plays an important role in many cellular processes. However, a simple and reliable method to measure changes in the extent of phosphorylation is lacking. Here, we present a method to quantitate the changes in phosphorylation occurring in a protein in response to a stimulus. The method consists of three steps: (i) enzymatic digestion in H(2)16O or isotopically enriched H(2)18O to label individual pools of differentially phosphorylated proteins; (ii) affinity selection of phosphopeptides from the combined digests by immobilized metal-affinity chromatography; and (iii) dephosphorylation with alkaline phosphatase to allow for quantitation of changes of phosphorylation by matrix-assisted laser desorption ionization time-of-flight mass spectrometry. We applied this strategy to the analysis of the yeast nitrogen permease reactivator protein kinase involved in the target of rapamycin signaling pathway. Alteration in the extent of phosphorylation at Ser-353 and Ser-357 could be easily assessed and quantitated both in wild-type yeast cells treated with rapamycin and in cells lacking the SIT4 phosphatase responsible for dephosphorylating nitrogen permease reactivator protein. The method described here is simple and allows quantitation of relative changes in the level of phosphorylation in signaling proteins, thus yielding information critical for understanding the regulation of complex protein phosphorylation cascades.</div>
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	Serveur d'exploration sur la rapamycine et les champignons
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Quantitation of changes in protein phosphorylation: a simple method based on stable isotope labeling and mass spectrometry.

Quantitation of changes in protein phosphorylation: a simple method based on stable isotope labeling and mass spectrometry.

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