The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Ltc1 is an ER-localized sterol transporter and a component of ER–mitochondria and ER–vacuole contacts
Open accessAbstract
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.
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Cites
The I-TASSER Suite: protein structure and function prediction
Yang, J., Yan, R., Roy, A., Xu, D., Poisson, J., & Zhang, Y. (2015) · Nature Methods · doi:10.1038/nmeth.3213 · Cited by 5,596
An ER-Mitochondria Tethering Complex Revealed by a Synthetic Biology Screen
Kornmann, B., Currie, E., Collins, S. R., Schuldiner, M., Nunnari, J., Weissman, J. S., & Walter, P. (2009) · Science · doi:10.1126/science.1175088 · Cited by 1,275
Self-citationMitochondrial protein import: from proteomics to functional mechanisms
Schmidt, O., Pfanner, N., & Meisinger, C. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2959 · Cited by 717
An early age increase in vacuolar pH limits mitochondrial function and lifespan in yeast
Hughes, A. L., & Gottschling, D. E. (2012) · Nature · doi:10.1038/nature11654 · Cited by 559
Murley, A., Lackner, L. L., Osman, C., West, M., Voeltz, G. K., Walter, P., & Nunnari, J. (2013) · eLife · doi:10.7554/elife.00422 · Cited by 326
Self-citationLahiri, S., Chao, J. T., Tavassoli, S., Wong, A. K. O., Choudhary, V., Young, B. P., Loewen, C. J. R., & Prinz, W. A. (2014) · PLoS Biology · doi:10.1371/journal.pbio.1001969 · Cited by 306
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Mitochondrial proteins: from biogenesis to functional networks
Pfanner, N., Warscheid, B., & Wiedemann, N. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0092-0 · Cited by 1,028
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Lawrence, R. E., & Zoncu, R. (2019) · Nature Cell Biology · doi:10.1038/s41556-018-0244-7 · Cited by 920
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Wong, L. H., Gatta, A. T., & Levine, T. P. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0071-5 · Cited by 505
Sandhu, J., Li, S., Fairall, L., Pfisterer, S. G., Gurnett, J. E., Xiao, X., Weston, T. A., Vashi, D., Ferrari, A., Orozco, J. L., et al. (2018) · Cell · doi:10.1016/j.cell.2018.08.033 · Cited by 287
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Naito, T., Ercan, B., Krshnan, L., Triebl, A., Koh, D. H. Z., Wei, F.-Y., Tomizawa, K., Torta, F. T., Wenk, M. R., & Saheki, Y. (2019) · eLife · doi:10.7554/elife.51401 · Cited by 171
Metadata
- Authors
- Murley, A., Sarsam, R. D., Toulmay, A., Yamada, J., Prinz, W. A., & Nunnari, J.
- Venue
- Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2015-05-18
- Volume
- 209
- Issue
- 4
- Pages
- 539-548
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- OpenAlex
- W1898232548
- Cited by
- 292
- References
- 6
- FWCI
- 14.18
- Type
- journal article
- Language
- en
- Open access
- hybrid
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