RapamycinFungusV1, Main, Exploration, bibRecord, 001516

Human protein phosphatase PP6 regulatory subunits provide Sit4-dependent and rapamycin-sensitive sap function in Saccharomyces cerevisiae.

Identifieur interne : 001516 ( Main/Exploration ); précédent : 001515; suivant : 001517

Human protein phosphatase PP6 regulatory subunits provide Sit4-dependent and rapamycin-sensitive sap function in Saccharomyces cerevisiae.

Auteurs : Helena Morales-Johansson [États-Unis] ; Rekha Puria ; David L. Brautigan ; Maria E. Cardenas

Source :

PloS one [ 1932-6203 ] ; 2009.

RBID : pubmed:19621075

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence (MeSH), DNA Replication (MeSH), Flow Cytometry (MeSH), G1 Phase (MeSH), Humans (MeSH), Molecular Sequence Data (MeSH), Phosphoprotein Phosphatases (chemistry), Phosphoprotein Phosphatases (genetics), Phosphoprotein Phosphatases (metabolism), Phosphorylation (MeSH), Protein Phosphatase 2 (metabolism), Recombinant Proteins (chemistry), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), Saccharomyces cerevisiae (cytology), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (metabolism), Sequence Homology, Amino Acid (MeSH), Signal Transduction (MeSH), Sirolimus (pharmacology).
MESH :
- chemical , chemistry : Phosphoprotein Phosphatases, Recombinant Proteins.
- chemical , genetics : Phosphoprotein Phosphatases, Recombinant Proteins.
- chemical , metabolism : Phosphoprotein Phosphatases, Protein Phosphatase 2, Recombinant Proteins, Saccharomyces cerevisiae Proteins.
- cytology : Saccharomyces cerevisiae.
- metabolism : Saccharomyces cerevisiae.
- chemical , pharmacology : Sirolimus.
- Amino Acid Sequence, DNA Replication, Flow Cytometry, G1 Phase, Humans, Molecular Sequence Data, Phosphorylation, Sequence Homology, Amino Acid, Signal Transduction.

Abstract

In the budding yeast Saccharomyces cerevisiae the protein phosphatase Sit4 and four associated proteins (Sap4, Sap155, Sap185, and Sap190) mediate G(1) to S cell cycle progression and a number of signaling events controlled by the target of rapamycin TOR signaling cascade. Sit4 and the Sap proteins are ubiquitously conserved and their human orthologs, PP6 and three PP6R proteins, share significant sequence identity with their yeast counterparts. However, relatively little is known about the functions of the PP6 and PP6R proteins in mammalian cells. Here we demonstrate that the human PP6R proteins physically interact with Sit4 when expressed in yeast cells. Remarkably, expression of PP6R2 and PP6R3 but not expression of PP6R1 rescues the growth defect and rapamycin hypersensitivity of yeast cells lacking all four Saps, and these effects require Sit4. Moreover, PP6R2 and PP6R3 enhance cyclin G(1) gene expression and DNA synthesis, and partially abrogate the G(1) cell cycle delay and the budding defect of the yeast quadruple sap mutant strain. In contrast, the human PP6R proteins only modestly support nitrogen catabolite gene expression and are unable to restore normal levels of eIF2alpha phosphorylation in the quadruple sap mutant strain. These results illustrate that the human PP6-associated proteins are capable of providing distinct rapamycin-sensitive and Sit4-dependent Sap functions in the heterologous context of the yeast cell. We hypothesize that the human Saps may play analogous roles in mTORC1-PP6 signaling events in metazoans.

DOI: 10.1371/journal.pone.0006331
PubMed: 19621075
PubMed Central: PMC2708350

Affiliations:

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Le document en format XML

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<front><div type="abstract" xml:lang="en">In the budding yeast Saccharomyces cerevisiae the protein phosphatase Sit4 and four associated proteins (Sap4, Sap155, Sap185, and Sap190) mediate G(1) to S cell cycle progression and a number of signaling events controlled by the target of rapamycin TOR signaling cascade. Sit4 and the Sap proteins are ubiquitously conserved and their human orthologs, PP6 and three PP6R proteins, share significant sequence identity with their yeast counterparts. However, relatively little is known about the functions of the PP6 and PP6R proteins in mammalian cells. Here we demonstrate that the human PP6R proteins physically interact with Sit4 when expressed in yeast cells. Remarkably, expression of PP6R2 and PP6R3 but not expression of PP6R1 rescues the growth defect and rapamycin hypersensitivity of yeast cells lacking all four Saps, and these effects require Sit4. Moreover, PP6R2 and PP6R3 enhance cyclin G(1) gene expression and DNA synthesis, and partially abrogate the G(1) cell cycle delay and the budding defect of the yeast quadruple sap mutant strain. In contrast, the human PP6R proteins only modestly support nitrogen catabolite gene expression and are unable to restore normal levels of eIF2alpha phosphorylation in the quadruple sap mutant strain. These results illustrate that the human PP6-associated proteins are capable of providing distinct rapamycin-sensitive and Sit4-dependent Sap functions in the heterologous context of the yeast cell. We hypothesize that the human Saps may play analogous roles in mTORC1-PP6 signaling events in metazoans.</div>
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	Serveur d'exploration sur la rapamycine et les champignons
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Human protein phosphatase PP6 regulatory subunits provide Sit4-dependent and rapamycin-sensitive sap function in Saccharomyces cerevisiae.

Human protein phosphatase PP6 regulatory subunits provide Sit4-dependent and rapamycin-sensitive sap function in Saccharomyces cerevisiae.

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