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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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Formato: | Online Artículo Texto |
Lenguaje: | English |
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The American Society for Cell Biology
2015
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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. |
format | Online Article Text |
id | pubmed-4279224 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
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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