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A phosphatidylinositol transfer protein controls the phosphatidylcholine content of yeast Golgi membranes
SEC14p is required for protein transport from the yeast Golgi complex. We describe a quantitative analysis of yeast bulk membrane and Golgi membrane phospholipid composition under conditions where Golgi secretory function has been uncoupled from its usual SEC14p requirement. The data demonstrate tha...
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1994
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2119930/ https://www.ncbi.nlm.nih.gov/pubmed/8294512 |
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collection | PubMed |
description | SEC14p is required for protein transport from the yeast Golgi complex. We describe a quantitative analysis of yeast bulk membrane and Golgi membrane phospholipid composition under conditions where Golgi secretory function has been uncoupled from its usual SEC14p requirement. The data demonstrate that SEC14p specifically functions to maintain a reduced phosphatidylcholine content in Golgi membranes and indicate that overproduction of SEC14p markedly reduces the apparent rate of phosphatidylcholine biosynthesis via the CDP-choline pathway in vivo. We suggest that SEC14p serves as a sensor of Golgi membrane phospholipid composition through which the activity of the CDP-choline pathway in Golgi membranes is regulated such that a phosphatidylcholine content that is compatible with the essential secretory function of these membranes is maintained. |
format | Text |
id | pubmed-2119930 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1994 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21199302008-05-01 A phosphatidylinositol transfer protein controls the phosphatidylcholine content of yeast Golgi membranes J Cell Biol Articles SEC14p is required for protein transport from the yeast Golgi complex. We describe a quantitative analysis of yeast bulk membrane and Golgi membrane phospholipid composition under conditions where Golgi secretory function has been uncoupled from its usual SEC14p requirement. The data demonstrate that SEC14p specifically functions to maintain a reduced phosphatidylcholine content in Golgi membranes and indicate that overproduction of SEC14p markedly reduces the apparent rate of phosphatidylcholine biosynthesis via the CDP-choline pathway in vivo. We suggest that SEC14p serves as a sensor of Golgi membrane phospholipid composition through which the activity of the CDP-choline pathway in Golgi membranes is regulated such that a phosphatidylcholine content that is compatible with the essential secretory function of these membranes is maintained. The Rockefeller University Press 1994-02-01 /pmc/articles/PMC2119930/ /pubmed/8294512 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Articles A phosphatidylinositol transfer protein controls the phosphatidylcholine content of yeast Golgi membranes |
title | A phosphatidylinositol transfer protein controls the phosphatidylcholine content of yeast Golgi membranes |
title_full | A phosphatidylinositol transfer protein controls the phosphatidylcholine content of yeast Golgi membranes |
title_fullStr | A phosphatidylinositol transfer protein controls the phosphatidylcholine content of yeast Golgi membranes |
title_full_unstemmed | A phosphatidylinositol transfer protein controls the phosphatidylcholine content of yeast Golgi membranes |
title_short | A phosphatidylinositol transfer protein controls the phosphatidylcholine content of yeast Golgi membranes |
title_sort | phosphatidylinositol transfer protein controls the phosphatidylcholine content of yeast golgi membranes |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2119930/ https://www.ncbi.nlm.nih.gov/pubmed/8294512 |