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Plasma membrane aminoglycerolipid flippase function is required for signaling competence in the yeast mating pheromone response pathway

The class 4 P-type ATPases (“flippases”) maintain membrane asymmetry by translocating phosphatidylethanolamine and phosphatidylserine from the outer leaflet to the cytosolic leaflet of the plasma membrane. In Saccharomyces cerevisiae, five related gene products (Dnf1, Dnf2, Dnf3, Drs2, and Neo1) are...

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Autores principales: Sartorel, Elodie, Barrey, Evelyne, Lau, Rebecca K., Thorner, Jeremy
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4279224/
https://www.ncbi.nlm.nih.gov/pubmed/25378585
http://dx.doi.org/10.1091/mbc.E14-07-1193
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author Sartorel, Elodie
Barrey, Evelyne
Lau, Rebecca K.
Thorner, Jeremy
author_facet Sartorel, Elodie
Barrey, Evelyne
Lau, Rebecca K.
Thorner, Jeremy
author_sort Sartorel, Elodie
collection PubMed
description The class 4 P-type ATPases (“flippases”) maintain membrane asymmetry by translocating phosphatidylethanolamine and phosphatidylserine from the outer leaflet to the cytosolic leaflet of the plasma membrane. In Saccharomyces cerevisiae, five related gene products (Dnf1, Dnf2, Dnf3, Drs2, and Neo1) are implicated in flipping of phosphatidylethanolamine, phosphatidylserine, and phosphatidylcholine. In MATa cells responding to α-factor, we found that Dnf1, Dnf2, and Dnf3, as well as the flippase-activating protein kinase Fpk1, localize at the projection (“shmoo”) tip where polarized growth is occurring and where Ste5 (the central scaffold protein of the pheromone-initiated MAPK cascade) is recruited. Although viable, a MATa dnf1∆ dnf2∆ dnf3∆ triple mutant exhibited a marked decrease in its ability to respond to α-factor, which we could attribute to pronounced reduction in Ste5 stability resulting from an elevated rate of its Cln2⋅Cdc28-initiated degradation. Similarly, a MATa dnf1∆ dnf3∆ drs2∆ triple mutant also displayed marked reduction in its ability to respond to α-factor, which we could attribute to inefficient recruitment of Ste5 to the plasma membrane due to severe mislocalization of the cellular phosphatidylinositol 4-phosphate and phosphatidylinositol 4,5-bisphosphate pools. Thus proper remodeling of plasma membrane aminoglycerolipids and phosphoinositides is necessary for efficient recruitment, stability, and function of the pheromone signaling apparatus.
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spelling pubmed-42792242015-03-16 Plasma membrane aminoglycerolipid flippase function is required for signaling competence in the yeast mating pheromone response pathway Sartorel, Elodie Barrey, Evelyne Lau, Rebecca K. Thorner, Jeremy Mol Biol Cell Articles The class 4 P-type ATPases (“flippases”) maintain membrane asymmetry by translocating phosphatidylethanolamine and phosphatidylserine from the outer leaflet to the cytosolic leaflet of the plasma membrane. In Saccharomyces cerevisiae, five related gene products (Dnf1, Dnf2, Dnf3, Drs2, and Neo1) are implicated in flipping of phosphatidylethanolamine, phosphatidylserine, and phosphatidylcholine. In MATa cells responding to α-factor, we found that Dnf1, Dnf2, and Dnf3, as well as the flippase-activating protein kinase Fpk1, localize at the projection (“shmoo”) tip where polarized growth is occurring and where Ste5 (the central scaffold protein of the pheromone-initiated MAPK cascade) is recruited. Although viable, a MATa dnf1∆ dnf2∆ dnf3∆ triple mutant exhibited a marked decrease in its ability to respond to α-factor, which we could attribute to pronounced reduction in Ste5 stability resulting from an elevated rate of its Cln2⋅Cdc28-initiated degradation. Similarly, a MATa dnf1∆ dnf3∆ drs2∆ triple mutant also displayed marked reduction in its ability to respond to α-factor, which we could attribute to inefficient recruitment of Ste5 to the plasma membrane due to severe mislocalization of the cellular phosphatidylinositol 4-phosphate and phosphatidylinositol 4,5-bisphosphate pools. Thus proper remodeling of plasma membrane aminoglycerolipids and phosphoinositides is necessary for efficient recruitment, stability, and function of the pheromone signaling apparatus. The American Society for Cell Biology 2015-01-01 /pmc/articles/PMC4279224/ /pubmed/25378585 http://dx.doi.org/10.1091/mbc.E14-07-1193 Text en © 2015 Sartorel et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology.
spellingShingle Articles
Sartorel, Elodie
Barrey, Evelyne
Lau, Rebecca K.
Thorner, Jeremy
Plasma membrane aminoglycerolipid flippase function is required for signaling competence in the yeast mating pheromone response pathway
title Plasma membrane aminoglycerolipid flippase function is required for signaling competence in the yeast mating pheromone response pathway
title_full Plasma membrane aminoglycerolipid flippase function is required for signaling competence in the yeast mating pheromone response pathway
title_fullStr Plasma membrane aminoglycerolipid flippase function is required for signaling competence in the yeast mating pheromone response pathway
title_full_unstemmed Plasma membrane aminoglycerolipid flippase function is required for signaling competence in the yeast mating pheromone response pathway
title_short Plasma membrane aminoglycerolipid flippase function is required for signaling competence in the yeast mating pheromone response pathway
title_sort plasma membrane aminoglycerolipid flippase function is required for signaling competence in the yeast mating pheromone response pathway
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4279224/
https://www.ncbi.nlm.nih.gov/pubmed/25378585
http://dx.doi.org/10.1091/mbc.E14-07-1193
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