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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
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
Self-citation
Cited by
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
The lysosome as a cellular centre for signalling, metabolism and quality control
Lawrence, R. E., & Zoncu, R. (2019) · Nature Cell Biology · doi:10.1038/s41556-018-0244-7 · Cited by 920
Lipid transfer proteins: the lipid commute via shuttles, bridges and tubes
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
Movement of accessible plasma membrane cholesterol by the GRAMD1 lipid transfer protein complex
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
Structure–Function Insights into Direct Lipid Transfer between Membranes by Mmm1–Mdm12 of ERMES
Kawano, S., Tamura, Y., Kojima, R., Bala, S., Asai, E., Michel, A. H., Kornmann, B., Riezman, I., Riezman, H., Sakae, Y., et al. (2018) · Journal of Cell Biology · doi:10.1083/jcb.201704119 · Cited by 148
“…physical contacts between the membranes of two organelles (Kornmann et al., 2009; Elbaz-Alon et al., 2014; Hönscher et al., 2014; Lahiri et al., 2014; Murley et al., 2015) highlights the need for coordinated functions of distinct organelles through direct exchange of metabolites and information.”
BackgroundMolecular basis of accessible plasma membrane cholesterol recognition by the GRAM domain of GRAMD1b
Ercan, B., Naito, T., Koh, D. H. Z., Dharmawan, D., & Saheki, Y. (2021) · The EMBO Journal · doi:10.15252/embj.2020106524 · Cited by 132
GRAM domain proteins specialize functionally distinct ER-PM contact sites in human cells
Besprozvannaya, M., Dickson, E., Li, H., Ginburg, K. S., Bers, D. M., Auwerx, J., & Nunnari, J. (2018) · eLife · doi:10.7554/elife.31019 · Cited by 128
Self-citationCDP-Diacylglycerol Synthases (CDS): Gateway to Phosphatidylinositol and Cardiolipin Synthesis
Blunsom, N. J., & Cockcroft, S. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00063 · Cited by 123
Molecular basis for sterol transport by StART‐like lipid transfer domains
Horenkamp, F. A., Valverde, D. P., Nunnari, J., & Reinisch, K. M. (2018) · The EMBO Journal · doi:10.15252/embj.201798002 · Cited by 113
Self-citationA Phospholipid Transfer Function of ER-Mitochondria Encounter Structure Revealed in Vitro
Kojima, R., Endo, T., & Tamura, Y. (2016) · Scientific Reports · doi:10.1038/srep30777 · Cited by 91
Intracellular Cholesterol Synthesis and Transport
Shi, Q., Chen, J., Zou, X., & Tang, X. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.819281 · Cited by 73
Castro, I. G., Shortill, S. P., Dziurdzik, S. K., Cadou, A., Ganesan, S., Valenti, R., David, Y., Davey, M., Mattes, C., Thomas, F. B., et al. (2022) · eLife · doi:10.7554/elife.74602 · Cited by 60
Structural basis of sterol binding and transport by a yeast StARkin domain
Jentsch, J.-A., Kiburu, I., Pandey, K., Timme, M., Ramlall, T., Levkau, B., Wu, J., Eliezer, D., Boudker, O., & Menon, A. K. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.001881 · Cited by 58
Sterol biosensor reveals LAM-family Ltc1-dependent sterol flow to endosomes upon Arp2/3 inhibition
Marek, M., Vincenzetti, V., & Martin, S. G. (2020) · Journal of Cell Biology · doi:10.1083/jcb.202001147 · Cited by 50
The History and Science of the Major Birch Pollen Allergen Bet v 1
Breiteneder, H., & Kraft, D. (2023) · Biomolecules · doi:10.3390/biom13071151 · Cited by 40
Structural insights into a StART-like domain in Lam4 and its interaction with sterol ligands
Gatta, A. T., Sauerwein, A. C., Zhuravleva, A., Levine, T. P., & Matthews, S. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.12.109 · Cited by 18
An allosteric network governs Tom70 conformational dynamics to coordinate mitochondrial import
Bachochin, M. J., McGuire, K. L., Cook, B. D., Ye, Q., Silletti, S., Corbett, K. D., Komives, E. A., & Herzik, M. A. (2026) · Structure · doi:10.1016/j.str.2025.11.011 · Cited by 7
Membrane contact sites regulate vacuolar fission via sphingolipid metabolism
Hanaoka, K., Nishikawa, K., Ikeda, A., Schlarmann, P., Sasaki, S., Fujii, S., Yamashita, S., Nakaji, A., & Funato, K. (2024) · eLife · doi:10.7554/elife.89938 · Cited by 6
Membrane contact sites regulate vacuolar fission via sphingolipid metabolism
Hanaoka, K., Nishikawa, K., Ikeda, A., Schlarmann, P., Yamashita, S., Nakaji, A., Fujii, S., & Funato, K. (2023) · doi:10.1101/2023.06.21.546015
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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
