RapamycinFungusV1, Main, Exploration, bibRecord, 001144

Plasma membrane proteins Slm1 and Slm2 mediate activation of the AGC kinase Ypk1 by TORC2 and sphingolipids in S. cerevisiae.

Identifieur interne : 001144 ( Main/Exploration ); précédent : 001143; suivant : 001145

Plasma membrane proteins Slm1 and Slm2 mediate activation of the AGC kinase Ypk1 by TORC2 and sphingolipids in S. cerevisiae.

Auteurs : Brad J. Niles [États-Unis] ; Ted Powers

Source :

Cell cycle (Georgetown, Tex.) [ 1551-4005 ] ; 2012.

RBID : pubmed:22895050

Descripteurs français

English descriptors

KwdEn :
- Carrier Proteins (genetics), Carrier Proteins (metabolism), Cell Membrane (chemistry), Cell Membrane (metabolism), Cytoskeletal Proteins (MeSH), Enzyme Activation (MeSH), Feedback, Physiological (MeSH), Gene Expression Regulation, Fungal (MeSH), Glycogen Synthase Kinase 3 (genetics), Glycogen Synthase Kinase 3 (metabolism), Humans (MeSH), Mechanistic Target of Rapamycin Complex 2 (MeSH), Multiprotein Complexes (genetics), Multiprotein Complexes (metabolism), Phosphorylation (MeSH), RNA-Binding Proteins (genetics), RNA-Binding Proteins (metabolism), Saccharomyces cerevisiae (enzymology), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism), Signal Transduction (MeSH), Sphingolipids (biosynthesis), TOR Serine-Threonine Kinases (genetics), TOR Serine-Threonine Kinases (metabolism).
MESH :
- chemical , biosynthesis : Sphingolipids.
- chemical , genetics : Carrier Proteins, Glycogen Synthase Kinase 3, Multiprotein Complexes, RNA-Binding Proteins, Saccharomyces cerevisiae Proteins, TOR Serine-Threonine Kinases.
- chemical , metabolism : Carrier Proteins, Glycogen Synthase Kinase 3, Multiprotein Complexes, RNA-Binding Proteins, Saccharomyces cerevisiae Proteins, TOR Serine-Threonine Kinases.
- chemistry : Cell Membrane.
- enzymology : Saccharomyces cerevisiae.
- genetics : Saccharomyces cerevisiae.
- metabolism : Cell Membrane.
- chemical : Cytoskeletal Proteins, Enzyme Activation, Feedback, Physiological, Gene Expression Regulation, Fungal, Humans, Mechanistic Target of Rapamycin Complex 2, Phosphorylation, Signal Transduction.

Abstract

The PH domain-containing proteins Slm1 and Slm2 were originally identified as substrates of the rapamycin-insensitive TOR complex 2 (TORC2) and as mediators of signaling by the lipid second messenger phosphatidyl-inositol-4,5-bisphosphate (PI4,5P2) in budding yeast S. cerevisiae. More recently, these proteins have been identified as critical effectors that facilitate phosphorylation and activation of the AGC kinases Ypk1 and Ypk2 by TORC2. Here, we review the molecular basis for this regulation as well as place it within the context of recent findings that have revealed Slm1/2 and TORC2-dependent phosphorylation of Ypk1 is coupled to the biosynthesis of complex sphingolipids and to their levels within the plasma membrane (PM) as well as other forms of PM stress. Together, these studies reveal the existence of an intricate homeostatic feedback mechanism, whereby the activity of these signaling components is linked to the biosynthesis of PM lipids according to cellular need.

DOI: 10.4161/cc.21752
PubMed: 22895050
PubMed Central: PMC3495817

Affiliations:

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

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Le document en format XML

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<term>Cell Membrane (metabolism)</term>
<term>Cytoskeletal Proteins (MeSH)</term>
<term>Enzyme Activation (MeSH)</term>
<term>Feedback, Physiological (MeSH)</term>
<term>Gene Expression Regulation, Fungal (MeSH)</term>
<term>Glycogen Synthase Kinase 3 (genetics)</term>
<term>Glycogen Synthase Kinase 3 (metabolism)</term>
<term>Humans (MeSH)</term>
<term>Mechanistic Target of Rapamycin Complex 2 (MeSH)</term>
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<term>RNA-Binding Proteins (metabolism)</term>
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<term>Saccharomyces cerevisiae (genetics)</term>
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<term>Complexe-2 cible mécanistique de la rapamycine (MeSH)</term>
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<term>Membrane cellulaire (métabolisme)</term>
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<term>Protéines de Saccharomyces cerevisiae (métabolisme)</term>
<term>Protéines de liaison à l'ARN (génétique)</term>
<term>Protéines de liaison à l'ARN (métabolisme)</term>
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<term>Protéines de transport (métabolisme)</term>
<term>Protéines du cytosquelette (MeSH)</term>
<term>Régulation de l'expression des gènes fongiques (MeSH)</term>
<term>Rétrocontrôle physiologique (MeSH)</term>
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<term>Saccharomyces cerevisiae (génétique)</term>
<term>Sphingolipides (biosynthèse)</term>
<term>Sérine-thréonine kinases TOR (génétique)</term>
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<term>Humans</term>
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<front><div type="abstract" xml:lang="en">The PH domain-containing proteins Slm1 and Slm2 were originally identified as substrates of the rapamycin-insensitive TOR complex 2 (TORC2) and as mediators of signaling by the lipid second messenger phosphatidyl-inositol-4,5-bisphosphate (PI4,5P2) in budding yeast S. cerevisiae. More recently, these proteins have been identified as critical effectors that facilitate phosphorylation and activation of the AGC kinases Ypk1 and Ypk2 by TORC2. Here, we review the molecular basis for this regulation as well as place it within the context of recent findings that have revealed Slm1/2 and TORC2-dependent phosphorylation of Ypk1 is coupled to the biosynthesis of complex sphingolipids and to their levels within the plasma membrane (PM) as well as other forms of PM stress. Together, these studies reveal the existence of an intricate homeostatic feedback mechanism, whereby the activity of these signaling components is linked to the biosynthesis of PM lipids according to cellular need.</div>
</front>
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<Abstract><AbstractText>The PH domain-containing proteins Slm1 and Slm2 were originally identified as substrates of the rapamycin-insensitive TOR complex 2 (TORC2) and as mediators of signaling by the lipid second messenger phosphatidyl-inositol-4,5-bisphosphate (PI4,5P2) in budding yeast S. cerevisiae. More recently, these proteins have been identified as critical effectors that facilitate phosphorylation and activation of the AGC kinases Ypk1 and Ypk2 by TORC2. Here, we review the molecular basis for this regulation as well as place it within the context of recent findings that have revealed Slm1/2 and TORC2-dependent phosphorylation of Ypk1 is coupled to the biosynthesis of complex sphingolipids and to their levels within the plasma membrane (PM) as well as other forms of PM stress. Together, these studies reveal the existence of an intricate homeostatic feedback mechanism, whereby the activity of these signaling components is linked to the biosynthesis of PM lipids according to cellular need.</AbstractText>
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Plasma membrane proteins Slm1 and Slm2 mediate activation of the AGC kinase Ypk1 by TORC2 and sphingolipids in S. cerevisiae.

Plasma membrane proteins Slm1 and Slm2 mediate activation of the AGC kinase Ypk1 by TORC2 and sphingolipids in S. cerevisiae.

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