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Phosphatidylserine transport by Ups2–Mdm35 in respiration-active mitochondria
Phosphatidylethanolamine (PE) is an essential phospholipid for mitochondrial functions and is synthesized mainly by phosphatidylserine (PS) decarboxylase at the mitochondrial inner membrane. In Saccharomyces cerevisiae, PS is synthesized in the endoplasmic reticulum (ER), such that mitochondrial PE...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4932372/ https://www.ncbi.nlm.nih.gov/pubmed/27354379 http://dx.doi.org/10.1083/jcb.201601082 |
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author | Miyata, Non Watanabe, Yasunori Tamura, Yasushi Endo, Toshiya Kuge, Osamu |
author_facet | Miyata, Non Watanabe, Yasunori Tamura, Yasushi Endo, Toshiya Kuge, Osamu |
author_sort | Miyata, Non |
collection | PubMed |
description | Phosphatidylethanolamine (PE) is an essential phospholipid for mitochondrial functions and is synthesized mainly by phosphatidylserine (PS) decarboxylase at the mitochondrial inner membrane. In Saccharomyces cerevisiae, PS is synthesized in the endoplasmic reticulum (ER), such that mitochondrial PE synthesis requires PS transport from the ER to the mitochondrial inner membrane. Here, we provide evidence that Ups2–Mdm35, a protein complex localized at the mitochondrial intermembrane space, mediates PS transport for PE synthesis in respiration-active mitochondria. UPS2- and MDM35-null mutations greatly attenuated conversion of PS to PE in yeast cells growing logarithmically under nonfermentable conditions, but not fermentable conditions. A recombinant Ups2–Mdm35 fusion protein exhibited phospholipid-transfer activity between liposomes in vitro. Furthermore, UPS2 expression was elevated under nonfermentable conditions and at the diauxic shift, the metabolic transition from glycolysis to oxidative phosphorylation. These results demonstrate that Ups2–Mdm35 functions as a PS transfer protein and enhances mitochondrial PE synthesis in response to the cellular metabolic state. |
format | Online Article Text |
id | pubmed-4932372 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-49323722017-01-04 Phosphatidylserine transport by Ups2–Mdm35 in respiration-active mitochondria Miyata, Non Watanabe, Yasunori Tamura, Yasushi Endo, Toshiya Kuge, Osamu J Cell Biol Research Articles Phosphatidylethanolamine (PE) is an essential phospholipid for mitochondrial functions and is synthesized mainly by phosphatidylserine (PS) decarboxylase at the mitochondrial inner membrane. In Saccharomyces cerevisiae, PS is synthesized in the endoplasmic reticulum (ER), such that mitochondrial PE synthesis requires PS transport from the ER to the mitochondrial inner membrane. Here, we provide evidence that Ups2–Mdm35, a protein complex localized at the mitochondrial intermembrane space, mediates PS transport for PE synthesis in respiration-active mitochondria. UPS2- and MDM35-null mutations greatly attenuated conversion of PS to PE in yeast cells growing logarithmically under nonfermentable conditions, but not fermentable conditions. A recombinant Ups2–Mdm35 fusion protein exhibited phospholipid-transfer activity between liposomes in vitro. Furthermore, UPS2 expression was elevated under nonfermentable conditions and at the diauxic shift, the metabolic transition from glycolysis to oxidative phosphorylation. These results demonstrate that Ups2–Mdm35 functions as a PS transfer protein and enhances mitochondrial PE synthesis in response to the cellular metabolic state. The Rockefeller University Press 2016-07-04 /pmc/articles/PMC4932372/ /pubmed/27354379 http://dx.doi.org/10.1083/jcb.201601082 Text en © 2016 Miyata et al. 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 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/). |
spellingShingle | Research Articles Miyata, Non Watanabe, Yasunori Tamura, Yasushi Endo, Toshiya Kuge, Osamu Phosphatidylserine transport by Ups2–Mdm35 in respiration-active mitochondria |
title | Phosphatidylserine transport by Ups2–Mdm35 in respiration-active mitochondria |
title_full | Phosphatidylserine transport by Ups2–Mdm35 in respiration-active mitochondria |
title_fullStr | Phosphatidylserine transport by Ups2–Mdm35 in respiration-active mitochondria |
title_full_unstemmed | Phosphatidylserine transport by Ups2–Mdm35 in respiration-active mitochondria |
title_short | Phosphatidylserine transport by Ups2–Mdm35 in respiration-active mitochondria |
title_sort | phosphatidylserine transport by ups2–mdm35 in respiration-active mitochondria |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4932372/ https://www.ncbi.nlm.nih.gov/pubmed/27354379 http://dx.doi.org/10.1083/jcb.201601082 |
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