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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Toulmay, Alexandre Prinz, William A. Nunnari, Jodi Murley, Andrew Sarsam, Reta D. Yamada, Justin |
| Description | Author Affiliation: Murley A ( Department of Molecular and Cellular Biology, University of California, Davis, Davis, CA 95616.); Sarsam RD ( Department of Molecular and Cellular Biology, University of California, Davis, Davis, CA 95616.); Toulmay A ( National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.); Yamada J ( Department of Molecular and Cellular Biology, University of California, Davis, Davis, CA 95616.); Prinz WA ( National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.); Nunnari J ( Department of Molecular and Cellular Biology, University of California, Davis, Davis, CA 95616 jmnunnari@ucdavis.edu.) |
| Abstract | Organelle contact sites perform fundamental functions in cells, including lipid and ion homeostasis, membrane dynamics, and signaling. Using a forward proteomics approach in yeast, we identified new ER–mitochondria and ER–vacuole contacts specified by an uncharacterized protein, Ylr072w. Ylr072w is a conserved protein with GRAM and VASt domains that selectively transports sterols and is thus termed Ltc1, for Lipid transfer at contact site 1. Ltc1 localized to ER–mitochondria and ER–vacuole contacts via the mitochondrial import receptors Tom70/71 and the vacuolar protein Vac8, respectively. At mitochondria, Ltc1 was required for cell viability in the absence of Mdm34, a subunit of the ER–mitochondria encounter structure. At vacuoles, Ltc1 was required for sterol-enriched membrane domain formation in response to stress. Increasing the proportion of Ltc1 at vacuoles was sufficient to induce sterol-enriched vacuolar domains without stress. Thus, our data support a model in which Ltc1 is a sterol-dependent regulator of organelle and cellular homeostasis via its dual localization to ER–mitochondria and ER–vacuole contact sites. |
| ISSN | 00219525 |
| e-ISSN | 15408140 |
| Journal | The Journal of Cell Biology |
| Issue Number | 4 |
| Volume Number | 209 |
| Language | English |
| Publisher | Rockefeller University Press (United States) |
| Publisher Date | 2015-05-25 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Antiporters Physiology Endoplasmic Reticulum Metabolism Mitochondria Saccharomyces Cerevisiae Proteins Saccharomyces Cerevisiae Vacuoles Ergosterol Intracellular Membranes Protein Transport Signal Transduction Sterol Regulatory Element Binding Protein 2 Stress, Physiological Research Support, N.I.H., Extramural Cell Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Medicine |
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