RapamycinFungusV1, Main, Exploration, bibRecord, 001761

Pmr1, a Golgi Ca2+/Mn2+-ATPase, is a regulator of the target of rapamycin (TOR) signaling pathway in yeast.

Identifieur interne : 001761 ( Main/Exploration ); précédent : 001760; suivant : 001762

Pmr1, a Golgi Ca2+/Mn2+-ATPase, is a regulator of the target of rapamycin (TOR) signaling pathway in yeast.

Auteurs : Gina Devasahayam [États-Unis] ; Danilo Ritz ; Stephen B. Helliwell ; Daniel J. Burke ; Thomas W. Sturgill

Source :

Proceedings of the National Academy of Sciences of the United States of America [ 0027-8424 ] ; 2006.

RBID : pubmed:17095607

Descripteurs français

English descriptors

Abstract

The rapamycin.FKBP12 complex inhibits target of rapamycin (TOR) kinase in TORC1. We screened the yeast nonessential gene deletion collection to identify mutants that conferred rapamycin resistance, and we identified PMR1, encoding the Golgi Ca2+/Mn2+ -ATPase. Deleting PMR1 in two genetic backgrounds confers rapamycin resistance. Epistasis analyses show that Pmr1 functions upstream from Npr1 and Gln-3 in opposition to Lst8, a regulator of TOR. Npr1 kinase is largely cytoplasmic, and a portion localizes to the Golgi where amino acid permeases are modified and sorted. Nuclear translocation of Gln-3 and Gln-3 reporter activity in pmr1 cells are impaired, but expression of functional Gap1 in the plasma membrane of a pmr1 strain in response to nitrogen limitation is enhanced. These two phenotypes suggest up-regulation of Npr1 function in the absence of Pmr1. Together, our results establish that Pmr1-dependent Ca2+ and/or Mn2+ ion homeostasis is necessary for TOR signaling.

DOI: 10.1073/pnas.0604303103
PubMed: 17095607
PubMed Central: PMC1693834

Affiliations:

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

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Le document en format XML

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<term>Calcium-Transporting ATPases (genetics)</term>
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<term>Gene Expression Regulation, Fungal (MeSH)</term>
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<term>Molecular Chaperones (genetics)</term>
<term>Molecular Chaperones (metabolism)</term>
<term>Protein Kinases (genetics)</term>
<term>Protein Kinases (metabolism)</term>
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<term>Recombinant Fusion Proteins (genetics)</term>
<term>Recombinant Fusion Proteins (metabolism)</term>
<term>Saccharomyces cerevisiae (cytology)</term>
<term>Saccharomyces cerevisiae (enzymology)</term>
<term>Saccharomyces cerevisiae Proteins (genetics)</term>
<term>Saccharomyces cerevisiae Proteins (metabolism)</term>
<term>Signal Transduction (physiology)</term>
<term>Sirolimus (metabolism)</term>
<term>Transcription Factors (metabolism)</term>
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<term>Calcium-Transporting ATPases (métabolisme)</term>
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<term>Protein kinases (métabolisme)</term>
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<term>Protéines de Saccharomyces cerevisiae (métabolisme)</term>
<term>Protéines de fusion recombinantes (génétique)</term>
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<term>Saccharomyces cerevisiae (cytologie)</term>
<term>Saccharomyces cerevisiae (enzymologie)</term>
<term>Sirolimus (métabolisme)</term>
<term>Systèmes de transport d'acides aminés (génétique)</term>
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<front><div type="abstract" xml:lang="en">The rapamycin.FKBP12 complex inhibits target of rapamycin (TOR) kinase in TORC1. We screened the yeast nonessential gene deletion collection to identify mutants that conferred rapamycin resistance, and we identified PMR1, encoding the Golgi Ca2+/Mn2+ -ATPase. Deleting PMR1 in two genetic backgrounds confers rapamycin resistance. Epistasis analyses show that Pmr1 functions upstream from Npr1 and Gln-3 in opposition to Lst8, a regulator of TOR. Npr1 kinase is largely cytoplasmic, and a portion localizes to the Golgi where amino acid permeases are modified and sorted. Nuclear translocation of Gln-3 and Gln-3 reporter activity in pmr1 cells are impaired, but expression of functional Gap1 in the plasma membrane of a pmr1 strain in response to nitrogen limitation is enhanced. These two phenotypes suggest up-regulation of Npr1 function in the absence of Pmr1. Together, our results establish that Pmr1-dependent Ca2+ and/or Mn2+ ion homeostasis is necessary for TOR signaling.</div>
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	Serveur d'exploration sur la rapamycine et les champignons
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Pmr1, a Golgi Ca2+/Mn2+-ATPase, is a regulator of the target of rapamycin (TOR) signaling pathway in yeast.

Pmr1, a Golgi Ca2+/Mn2+-ATPase, is a regulator of the target of rapamycin (TOR) signaling pathway in yeast.

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