ArticleeLife2015
A new family of StART domain proteins at membrane contact sites has a role in ER-PM sterol transport.
Article in eLife, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 144 papers, 1 of them a synthesis that pooled it.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
144 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Stay in touch with the endoplasmic reticulum.Science China. Life sciences · 2024Pooled it
- Sterol binding mechanism of a plant START-like domain: A new sterol transport paradigm via an amphiphilic cavity.The FEBS journal · 2026Article
- Lipid traffic: an enigmatic alliance between ORPs and a TMEM16-like protein at membrane contact sites.Biochemical Society transactions · 2026Review
- Hoi1 targets BLTP2 to ER-PM contact sites to regulate lipid homeostasis.The Journal of cell biology · 2026Article
- A dynamic feedback loop between retrograde sterol transport and TORC2 controls adaptation of the plasma membrane to stress.The EMBO journal · 2025Article
- Role of Pex31 in metabolic adaptation of the nucleus-vacuole junction.Journal of cell science · 2025Article
- Ist2 promotes lipid transfer by Osh6 via its membrane tethering and lipid scramblase activities.Science advances · 2025Article
- Key challenges and recommendations for defining organelle membrane contact sites.Nature reviews. Molecular cell biology · 2025Review
- Unbiased MD simulations identify lipid binding sites in lipid transfer proteins.The Journal of cell biology · 2024Article
- Mammalian START-like phosphatidylinositol transfer proteins - Physiological perspectives and roles in cancer biology.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2024Review
- Otilonium Bromide Exhibits Potent Antifungal Effects by Blocking Ergosterol Plasma Membrane Localization and Triggering Cytotoxic Autophagy in Candida Albicans.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Article
- Endoplasmic Reticulum Membrane Homeostasis and the Unfolded Protein Response.Cold Spring Harbor perspectives in biology · 2024Review
- The molecular mechanism of on-demand sterol biosynthesis at organelle contact sites.bioRxiv : the preprint server for biology · 2024Article
- Novel sterol binding domains in bacteria.eLife · 2024Article
- Insights into the role of sterol metabolism in antifungal drug resistance: a mini-review.Frontiers in microbiology · 2024Review
- MiR-4646-5p Acts as a Tumor-Suppressive Factor in Triple Negative Breast Cancer and Targets the Cholesterol Transport Protein GRAMD1B.Non-coding RNA · 2023Article
- Organelles are miscommunicating: Membrane contact sites getting hijacked by pathogens.Virulence · 2023Review
- Regulation of cellular cholesterol distribution via non-vesicular lipid transport at ER-Golgi contact sites.Nature communications · 2023Article
- A dynamic actin cytoskeleton is required to prevent constitutive VDAC-dependent MAPK signalling and aberrant lipid homeostasis.iScience · 2023Article
84 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Sterol traffic between the endoplasmic reticulum (ER) and plasma membrane (PM) is a fundamental cellular process that occurs by a poorly understood non-vesicular mechanism. We identified a novel, evolutionarily diverse family of ER membrane proteins with StART-like lipid transfer domains and studied them in yeast. StART-like domains from Ysp2p and its paralog Lam4p specifically bind sterols, and Ysp2p, Lam4p and their homologs Ysp1p and Sip3p target punctate ER-PM contact sites distinct from those occupied by known ER-PM tethers. The activity of Ysp2p, reflected in amphotericin-sensitivity assays, requires its second StART-like domain to be positioned so that it can reach across ER-PM contacts. Absence of Ysp2p, Ysp1p or Sip3p reduces the rate at which exogenously supplied sterols traffic from the PM to the ER. Our data suggest that these StART-like proteins act in trans to mediate a step in sterol exchange between the PM and ER.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.