An ER Protein Functionally Couples Neutral Lipid Metabolism on Lipid Droplets to Membrane Lipid Synthesis in the ER
Eukaryotic cells store neutral lipids such as triacylglycerol (TAG) in lipid droplets (LDs). Here, we have addressed how LDs are functionally linked to the endoplasmic reticulum (ER). We show that, in S. cerevisiae, LD growth is sustained by LD-localized enzymes. When LDs grow in early stationary ph...
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| Format: | Article |
| Language: | English |
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Elsevier
2014-01-01
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| Series: | Cell Reports |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2211124713007304 |
| _version_ | 1818042749906059264 |
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| author | Daniel F. Markgraf Robin W. Klemm Mirco Junker Hans K. Hannibal-Bach Christer S. Ejsing Tom A. Rapoport |
| author_facet | Daniel F. Markgraf Robin W. Klemm Mirco Junker Hans K. Hannibal-Bach Christer S. Ejsing Tom A. Rapoport |
| author_sort | Daniel F. Markgraf |
| collection | DOAJ |
| description | Eukaryotic cells store neutral lipids such as triacylglycerol (TAG) in lipid droplets (LDs). Here, we have addressed how LDs are functionally linked to the endoplasmic reticulum (ER). We show that, in S. cerevisiae, LD growth is sustained by LD-localized enzymes. When LDs grow in early stationary phase, the diacylglycerol acyl-transferase Dga1p moves from the ER to LDs and is responsible for all TAG synthesis from diacylglycerol (DAG). During LD breakdown in early exponential phase, an ER membrane protein (Ice2p) facilitates TAG utilization for membrane-lipid synthesis. Ice2p has a cytosolic domain with affinity for LDs and is required for the efficient utilization of LD-derived DAG in the ER. Ice2p breaks a futile cycle on LDs between TAG degradation and synthesis, promoting the rapid relocalization of Dga1p to the ER. Our results show that Ice2p functionally links LDs with the ER and explain how cells switch neutral lipid metabolism from storage to consumption. |
| first_indexed | 2024-12-10T08:51:16Z |
| format | Article |
| id | doaj.art-10d8043dabf64ab28dc370e9064e250d |
| institution | Directory Open Access Journal |
| issn | 2211-1247 |
| language | English |
| last_indexed | 2024-12-10T08:51:16Z |
| publishDate | 2014-01-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Cell Reports |
| spelling | doaj.art-10d8043dabf64ab28dc370e9064e250d2022-12-22T01:55:34ZengElsevierCell Reports2211-12472014-01-0161445510.1016/j.celrep.2013.11.046An ER Protein Functionally Couples Neutral Lipid Metabolism on Lipid Droplets to Membrane Lipid Synthesis in the ERDaniel F. Markgraf0Robin W. Klemm1Mirco Junker2Hans K. Hannibal-Bach3Christer S. Ejsing4Tom A. Rapoport5Department of Cell Biology, Howard Hughes Medical Institute, Harvard Medical School, Boston, MA 02115, USADepartment of Cell Biology, Howard Hughes Medical Institute, Harvard Medical School, Boston, MA 02115, USADepartment of Cell Biology, Howard Hughes Medical Institute, Harvard Medical School, Boston, MA 02115, USADepartment of Biochemistry and Molecular Biology, University of Southern Denmark, 5230 Odense, DenmarkDepartment of Biochemistry and Molecular Biology, University of Southern Denmark, 5230 Odense, DenmarkDepartment of Cell Biology, Howard Hughes Medical Institute, Harvard Medical School, Boston, MA 02115, USAEukaryotic cells store neutral lipids such as triacylglycerol (TAG) in lipid droplets (LDs). Here, we have addressed how LDs are functionally linked to the endoplasmic reticulum (ER). We show that, in S. cerevisiae, LD growth is sustained by LD-localized enzymes. When LDs grow in early stationary phase, the diacylglycerol acyl-transferase Dga1p moves from the ER to LDs and is responsible for all TAG synthesis from diacylglycerol (DAG). During LD breakdown in early exponential phase, an ER membrane protein (Ice2p) facilitates TAG utilization for membrane-lipid synthesis. Ice2p has a cytosolic domain with affinity for LDs and is required for the efficient utilization of LD-derived DAG in the ER. Ice2p breaks a futile cycle on LDs between TAG degradation and synthesis, promoting the rapid relocalization of Dga1p to the ER. Our results show that Ice2p functionally links LDs with the ER and explain how cells switch neutral lipid metabolism from storage to consumption.http://www.sciencedirect.com/science/article/pii/S2211124713007304 |
| spellingShingle | Daniel F. Markgraf Robin W. Klemm Mirco Junker Hans K. Hannibal-Bach Christer S. Ejsing Tom A. Rapoport An ER Protein Functionally Couples Neutral Lipid Metabolism on Lipid Droplets to Membrane Lipid Synthesis in the ER Cell Reports |
| title | An ER Protein Functionally Couples Neutral Lipid Metabolism on Lipid Droplets to Membrane Lipid Synthesis in the ER |
| title_full | An ER Protein Functionally Couples Neutral Lipid Metabolism on Lipid Droplets to Membrane Lipid Synthesis in the ER |
| title_fullStr | An ER Protein Functionally Couples Neutral Lipid Metabolism on Lipid Droplets to Membrane Lipid Synthesis in the ER |
| title_full_unstemmed | An ER Protein Functionally Couples Neutral Lipid Metabolism on Lipid Droplets to Membrane Lipid Synthesis in the ER |
| title_short | An ER Protein Functionally Couples Neutral Lipid Metabolism on Lipid Droplets to Membrane Lipid Synthesis in the ER |
| title_sort | er protein functionally couples neutral lipid metabolism on lipid droplets to membrane lipid synthesis in the er |
| url | http://www.sciencedirect.com/science/article/pii/S2211124713007304 |
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