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Compartment-specific Synthesis of Phosphatidylethanolamine Is Required for Normal Heavy Metal Resistance
Control of lipid composition of membranes is crucial to ensure normal cellular functions. Saccharomyces cerevisiae has two different phosphatidylserine decarboxylase enzymes (Psd1 and Psd2) that catalyze formation of phosphatidylethanolamine. The mitochondrial Psd1 provides roughly 70% of the phosph...
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Formato: | Texto |
Lenguaje: | English |
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The American Society for Cell Biology
2010
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2814789/ https://www.ncbi.nlm.nih.gov/pubmed/20016005 http://dx.doi.org/10.1091/mbc.E09-06-0519 |
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author | Gulshan, Kailash Shahi, Puja Moye-Rowley, W. Scott |
author_facet | Gulshan, Kailash Shahi, Puja Moye-Rowley, W. Scott |
author_sort | Gulshan, Kailash |
collection | PubMed |
description | Control of lipid composition of membranes is crucial to ensure normal cellular functions. Saccharomyces cerevisiae has two different phosphatidylserine decarboxylase enzymes (Psd1 and Psd2) that catalyze formation of phosphatidylethanolamine. The mitochondrial Psd1 provides roughly 70% of the phosphatidylethanolamine (PE) biosynthesis in the cell with Psd2 carrying out the remainder. Here, we demonstrate that loss of Psd2 causes cells to acquire sensitivity to cadmium even though Psd1 remains intact. This cadmium sensitivity results from loss of normal activity of a vacuolar ATP-binding cassette transporter protein called Ycf1. Measurement of phospholipid levels indicates that loss of Psd2 causes a specific reduction in vacuolar membrane PE levels, whereas total PE levels are not significantly affected. The presence of a phosphatidylinositol transfer protein called Pdr17 is required for Psd2 function and normal cadmium tolerance. We demonstrate that Pdr17 and Psd2 form a complex in vivo that seems essential for maintenance of vacuolar PE levels. Finally, we refine the localization of Psd2 to the endosome arguing that this enzyme controls vacuolar membrane phospholipid content by regulating phospholipids in compartments that will eventually give rise to the vacuole. Disturbance of this regulation of intracellular phospholipid balance leads to selective loss of membrane protein function in the vacuole. |
format | Text |
id | pubmed-2814789 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-28147892010-04-16 Compartment-specific Synthesis of Phosphatidylethanolamine Is Required for Normal Heavy Metal Resistance Gulshan, Kailash Shahi, Puja Moye-Rowley, W. Scott Mol Biol Cell Articles Control of lipid composition of membranes is crucial to ensure normal cellular functions. Saccharomyces cerevisiae has two different phosphatidylserine decarboxylase enzymes (Psd1 and Psd2) that catalyze formation of phosphatidylethanolamine. The mitochondrial Psd1 provides roughly 70% of the phosphatidylethanolamine (PE) biosynthesis in the cell with Psd2 carrying out the remainder. Here, we demonstrate that loss of Psd2 causes cells to acquire sensitivity to cadmium even though Psd1 remains intact. This cadmium sensitivity results from loss of normal activity of a vacuolar ATP-binding cassette transporter protein called Ycf1. Measurement of phospholipid levels indicates that loss of Psd2 causes a specific reduction in vacuolar membrane PE levels, whereas total PE levels are not significantly affected. The presence of a phosphatidylinositol transfer protein called Pdr17 is required for Psd2 function and normal cadmium tolerance. We demonstrate that Pdr17 and Psd2 form a complex in vivo that seems essential for maintenance of vacuolar PE levels. Finally, we refine the localization of Psd2 to the endosome arguing that this enzyme controls vacuolar membrane phospholipid content by regulating phospholipids in compartments that will eventually give rise to the vacuole. Disturbance of this regulation of intracellular phospholipid balance leads to selective loss of membrane protein function in the vacuole. The American Society for Cell Biology 2010-02-01 /pmc/articles/PMC2814789/ /pubmed/20016005 http://dx.doi.org/10.1091/mbc.E09-06-0519 Text en © 2010 by The American Society for Cell Biology |
spellingShingle | Articles Gulshan, Kailash Shahi, Puja Moye-Rowley, W. Scott Compartment-specific Synthesis of Phosphatidylethanolamine Is Required for Normal Heavy Metal Resistance |
title | Compartment-specific Synthesis of Phosphatidylethanolamine Is Required for Normal Heavy Metal Resistance |
title_full | Compartment-specific Synthesis of Phosphatidylethanolamine Is Required for Normal Heavy Metal Resistance |
title_fullStr | Compartment-specific Synthesis of Phosphatidylethanolamine Is Required for Normal Heavy Metal Resistance |
title_full_unstemmed | Compartment-specific Synthesis of Phosphatidylethanolamine Is Required for Normal Heavy Metal Resistance |
title_short | Compartment-specific Synthesis of Phosphatidylethanolamine Is Required for Normal Heavy Metal Resistance |
title_sort | compartment-specific synthesis of phosphatidylethanolamine is required for normal heavy metal resistance |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2814789/ https://www.ncbi.nlm.nih.gov/pubmed/20016005 http://dx.doi.org/10.1091/mbc.E09-06-0519 |
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