Compartment-specific synthesis of phosphatidylethanolamine is required for normal heavy metal resistance
| العنوان: | Compartment-specific synthesis of phosphatidylethanolamine is required for normal heavy metal resistance |
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| المؤلفون: | Puja Shahi, W. Scott Moye-Rowley, Kailash Gulshan |
| المصدر: | Molecular Biology of the Cell |
| سنة النشر: | 2009 |
| مصطلحات موضوعية: | Saccharomyces cerevisiae Proteins, Carboxy-Lyases, Membrane lipids, Recombinant Fusion Proteins, Phospholipid, Vacuole, Endosomes, Saccharomyces cerevisiae, Biology, Cell membrane, R-SNARE Proteins, 03 medical and health sciences, chemistry.chemical_compound, Membrane Lipids, Phospholipid transfer protein, medicine, Phospholipid Transfer Proteins, Molecular Biology, Phosphatidylinositol transfer protein, 030304 developmental biology, Phosphatidylethanolamine, 0303 health sciences, Phosphatidylethanolamines, 030302 biochemistry & molecular biology, Cell Membrane, Cell Biology, Articles, Cell biology, Mitochondria, Isoenzymes, medicine.anatomical_structure, chemistry, Membrane Trafficking, Vacuoles, ATP-Binding Cassette Transporters, Phosphatidylserine decarboxylase, Cadmium |
| الوصف: | The enzyme Psd2 catalyzes endosomal synthesis of the phospholipid PE. While this pool of PE represents a minority of total cellular PE, function of Psd2 is required for normal activity of the vacuolar ABC transporter Ycf1. Psd2 controls vacuolar PE levels by acting at the level of the endosome. 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. |
| تدمد: | 1939-4586 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c611564f1aaa7fb6cecb540eb5eec363Test https://pubmed.ncbi.nlm.nih.gov/20016005Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....c611564f1aaa7fb6cecb540eb5eec363 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 19394586 |
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