RapamycinFungusV1, Main, Exploration, bibRecord, 000480

TOR complex 2-regulated protein kinase Ypk1 controls sterol distribution by inhibiting StARkin domain-containing proteins located at plasma membrane-endoplasmic reticulum contact sites.

Identifieur interne : 000480 ( Main/Exploration ); précédent : 000479; suivant : 000481

TOR complex 2-regulated protein kinase Ypk1 controls sterol distribution by inhibiting StARkin domain-containing proteins located at plasma membrane-endoplasmic reticulum contact sites.

Auteurs : Françoise M. Roelants [États-Unis] ; Neha Chauhan [États-Unis] ; Alexander Muir [États-Unis] ; Jameson C. Davis [États-Unis] ; Anant K. Menon [États-Unis] ; Timothy P. Levine [Royaume-Uni] ; Jeremy Thorner [États-Unis]

Source :

Molecular biology of the cell [ 1939-4586 ] ; 2018.

RBID : pubmed:29927351

Descripteurs français

English descriptors

KwdEn :
- Cell Membrane (metabolism), Endoplasmic Reticulum (metabolism), Homeostasis (MeSH), Mechanistic Target of Rapamycin Complex 2 (metabolism), Phosphorylation (MeSH), Protein Domains (MeSH), Protein-Serine-Threonine Kinases (chemistry), Protein-Serine-Threonine Kinases (metabolism), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (chemistry), Saccharomyces cerevisiae Proteins (metabolism), Sphingolipids (metabolism), Sterols (metabolism), Stress, Physiological (MeSH).
MESH :
- chemical , chemistry : Protein-Serine-Threonine Kinases, Saccharomyces cerevisiae Proteins.
- chemical , metabolism : Mechanistic Target of Rapamycin Complex 2, Protein-Serine-Threonine Kinases, Saccharomyces cerevisiae Proteins, Sphingolipids, Sterols.
- metabolism : Cell Membrane, Endoplasmic Reticulum, Saccharomyces cerevisiae.
- Homeostasis, Phosphorylation, Protein Domains, Stress, Physiological.

Abstract

In our proteome-wide screen, Ysp2 (also known as Lam2/Ltc4) was identified as a likely physiologically relevant target of the TOR complex 2 (TORC2)-dependent protein kinase Ypk1 in the yeast Saccharomyces cerevisiae. Ysp2 was subsequently shown to be one of a new family of sterol-binding proteins located at plasma membrane (PM)-endoplasmic reticulum (ER) contact sites. Here we document that Ysp2 and its paralogue Lam4/Ltc3 are authentic Ypk1 substrates in vivo and show using genetic and biochemical criteria that Ypk1-mediated phosphorylation inhibits the ability of these proteins to promote retrograde transport of sterols from the PM to the ER. Furthermore, we provide evidence that a change in PM sterol homeostasis promotes cell survival under membrane-perturbing conditions known to activate TORC2-Ypk1 signaling. These observations define the underlying molecular basis of a new regulatory mechanism for cellular response to plasma membrane stress.

DOI: 10.1091/mbc.E18-04-0229
PubMed: 29927351
PubMed Central: PMC6232965

Affiliations:

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

to stream Main, to step Corpus: 000523
to stream Main, to step Curation: 000523

Le document en format XML

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<front><div type="abstract" xml:lang="en">In our proteome-wide screen, Ysp2 (also known as Lam2/Ltc4) was identified as a likely physiologically relevant target of the TOR complex 2 (TORC2)-dependent protein kinase Ypk1 in the yeast Saccharomyces cerevisiae. Ysp2 was subsequently shown to be one of a new family of sterol-binding proteins located at plasma membrane (PM)-endoplasmic reticulum (ER) contact sites. Here we document that Ysp2 and its paralogue Lam4/Ltc3 are authentic Ypk1 substrates in vivo and show using genetic and biochemical criteria that Ypk1-mediated phosphorylation inhibits the ability of these proteins to promote retrograde transport of sterols from the PM to the ER. Furthermore, we provide evidence that a change in PM sterol homeostasis promotes cell survival under membrane-perturbing conditions known to activate TORC2-Ypk1 signaling. These observations define the underlying molecular basis of a new regulatory mechanism for cellular response to plasma membrane stress.</div>
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<Abstract><AbstractText>In our proteome-wide screen, Ysp2 (also known as Lam2/Ltc4) was identified as a likely physiologically relevant target of the TOR complex 2 (TORC2)-dependent protein kinase Ypk1 in the yeast Saccharomyces cerevisiae. Ysp2 was subsequently shown to be one of a new family of sterol-binding proteins located at plasma membrane (PM)-endoplasmic reticulum (ER) contact sites. Here we document that Ysp2 and its paralogue Lam4/Ltc3 are authentic Ypk1 substrates in vivo and show using genetic and biochemical criteria that Ypk1-mediated phosphorylation inhibits the ability of these proteins to promote retrograde transport of sterols from the PM to the ER. Furthermore, we provide evidence that a change in PM sterol homeostasis promotes cell survival under membrane-perturbing conditions known to activate TORC2-Ypk1 signaling. These observations define the underlying molecular basis of a new regulatory mechanism for cellular response to plasma membrane stress.</AbstractText>
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	Serveur d'exploration sur la rapamycine et les champignons
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TOR complex 2-regulated protein kinase Ypk1 controls sterol distribution by inhibiting StARkin domain-containing proteins located at plasma membrane-endoplasmic reticulum contact sites.

TOR complex 2-regulated protein kinase Ypk1 controls sterol distribution by inhibiting StARkin domain-containing proteins located at plasma membrane-endoplasmic reticulum contact sites.

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