The N-terminal domain of yeast Bap2 permease is phosphorylated dependently on the Npr1 kinase in response to starvation.
Identifieur interne : 001899 ( Main/Corpus ); précédent : 001898; suivant : 001900The N-terminal domain of yeast Bap2 permease is phosphorylated dependently on the Npr1 kinase in response to starvation.
Auteurs : Fumihiko Omura ; Yukiko KodamaSource :
- FEMS microbiology letters [ 0378-1097 ] ; 2004.
English descriptors
- KwdEn :
- Amino Acid Transport Systems (chemistry), Amino Acid Transport Systems (genetics), Amino Acid Transport Systems (metabolism), Antifungal Agents (pharmacology), Culture Media (MeSH), Gene Expression Regulation, Fungal (MeSH), Phosphorylation (MeSH), Protein Kinases (genetics), Protein Kinases (metabolism), Protein-Serine-Threonine Kinases (MeSH), Saccharomyces cerevisiae (drug effects), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (physiology), Saccharomyces cerevisiae Proteins (chemistry), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism), Sirolimus (pharmacology).
- MESH :
- chemical , chemistry : Amino Acid Transport Systems, Saccharomyces cerevisiae Proteins.
- chemical , genetics : Amino Acid Transport Systems, Protein Kinases, Saccharomyces cerevisiae Proteins.
- chemical , metabolism : Amino Acid Transport Systems, Protein Kinases, Saccharomyces cerevisiae Proteins.
- chemical , pharmacology : Antifungal Agents, Sirolimus.
- chemical : Culture Media, Protein-Serine-Threonine Kinases.
- drug effects : Saccharomyces cerevisiae.
- genetics : Saccharomyces cerevisiae.
- physiology : Saccharomyces cerevisiae.
- Gene Expression Regulation, Fungal, Phosphorylation.
Abstract
The Saccharomyces cerevisiae branched-chain amino acid permease Bap2p plays a major role in leucine, isoleucine, and valine transport, and its synthesis is regulated transcriptionally. Bap2p undergoes a starvation-induced degradation depending upon ubiquitination and the functions of N- and C-terminal domains of Bap2p. Here we show that the N-terminal domain of Bap2p is phosphorylated in response to rapamycin treatment when both the N- and C-termini of Bap2p are fused to glutathione S-transferase. The phosphorylation is dependent on Ser/Thr kinase Npr1p. In npr1 cells, Bap2p becomes slightly more susceptible to the rapamycin-induced degradation, suggesting that Npr1p counteracts the degradation system for Bap2p.
DOI: 10.1016/S0378-1097(03)00918-2
PubMed: 14757244
Links to Exploration step
pubmed:14757244Le document en format XML
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Bap2p undergoes a starvation-induced degradation depending upon ubiquitination and the functions of N- and C-terminal domains of Bap2p. Here we show that the N-terminal domain of Bap2p is phosphorylated in response to rapamycin treatment when both the N- and C-termini of Bap2p are fused to glutathione S-transferase. The phosphorylation is dependent on Ser/Thr kinase Npr1p. In npr1 cells, Bap2p becomes slightly more susceptible to the rapamycin-induced degradation, suggesting that Npr1p counteracts the degradation system for Bap2p.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">14757244</PMID><DateCompleted><Year>2004</Year><Month>04</Month><Day>16</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>30</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0378-1097</ISSN><JournalIssue CitedMedium="Print"><Volume>230</Volume><Issue>2</Issue><PubDate><Year>2004</Year><Month>Jan</Month><Day>30</Day></PubDate></JournalIssue><Title>FEMS microbiology letters</Title><ISOAbbreviation>FEMS Microbiol Lett</ISOAbbreviation></Journal><ArticleTitle>The N-terminal domain of yeast Bap2 permease is phosphorylated dependently on the Npr1 kinase in response to starvation.</ArticleTitle><Pagination><MedlinePgn>227-34</MedlinePgn></Pagination><Abstract><AbstractText>The Saccharomyces cerevisiae branched-chain amino acid permease Bap2p plays a major role in leucine, isoleucine, and valine transport, and its synthesis is regulated transcriptionally. Bap2p undergoes a starvation-induced degradation depending upon ubiquitination and the functions of N- and C-terminal domains of Bap2p. Here we show that the N-terminal domain of Bap2p is phosphorylated in response to rapamycin treatment when both the N- and C-termini of Bap2p are fused to glutathione S-transferase. The phosphorylation is dependent on Ser/Thr kinase Npr1p. 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