ArticleBiochemistry2015
STARD4 Membrane Interactions and Sterol Binding.
Article in Biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 64 citations in OpenAlex.
- STARD3 regulates lysosome positioning and contacts via a GSK3-controlled phosphorylation switch.The EMBO journal · 2026Article
- An origin for a eukaryotic lipid transfer protein fold in Asgard archaea.bioRxiv : the preprint server for biology · 2025Article
- Nonvesicular cholesterol transport in physiology.The Journal of clinical investigation · 2025Review
- Thirty years of StAR gazing. Expanding the universe of the steroidogenic acute regulatory protein.The Journal of endocrinology · 2025Review
- The conformational plasticity of structurally unrelated lipid transport proteins correlates with their mode of action.PLoS biology · 2024Article
- Ceramide-1-phosphate transfer protein enhances lipid transport by disrupting hydrophobic lipid-membrane contacts.PLoS computational biology · 2023Article
- G protein-coupled receptor 35 attenuates nonalcoholic steatohepatitis by reprogramming cholesterol homeostasis in hepatocytes.Acta pharmaceutica Sinica. B · 2023Article
- Allosterically coupled conformational dynamics in solution prepare the sterol transfer protein StarD4 to release its cargo upon interaction with target membranes.Frontiers in molecular biosciences · 2023Article
- A conserved function of Human DLC3 andeLife · 2022Article
- Membrane hydrophobicity determines the activation free energy of passive lipid transport.Biophysical journal · 2021Article
- STARD4 promotes breast cancer cell malignancy.Oncology reports · 2020Article
- Stable reduction of STARD4 alters cholesterol regulation and lipid homeostasis.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2020Article
- Article
- Visualizing the cellular route of entry of a cystine-knot peptide with Xfect transfection reagent by electron microscopy.Scientific reports · 2019Article
- Structural determinants of lipid specificity within Ups/PRELI lipid transfer proteins.Nature communications · 2019Article
- Lipid transfer proteins: the lipid commute via shuttles, bridges and tubes.Nature reviews. Molecular cell biology · 2019Review
- Structural basis of sterol binding and transport by a yeast StARkin domain.The Journal of biological chemistry · 2018Article
- Molecular basis for sterol transport by StART-like lipid transfer domains.The EMBO journal · 2018Article
- Structural basis of sterol recognition and nonvesicular transport by lipid transfer proteins anchored at membrane contact sites.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Membrane dynamics and organelle biogenesis-lipid pipelines and vesicular carriers.BMC biology · 2017Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The steroidogenic acute regulatory protein-related lipid transfer (START) domain family is defined by a conserved 210-amino acid sequence that folds into an α/β helix-grip structure. Members of this protein family bind a variety of ligands, including cholesterol, phospholipids, sphingolipids, and bile acids, with putative roles in nonvesicular lipid transport, metabolism, and cell signaling. Among the soluble START proteins, STARD4 is expressed in most tissues and has previously been shown to transfer sterol, but the molecular mechanisms of membrane interaction and sterol binding remain unclear. In this work, we use biochemical techniques to characterize regions of STARD4 and determine their role in membrane interaction and sterol binding. Our results show that STARD4 interacts with anionic membranes through a surface-exposed basic patch and that introducing a mutation (L124D) into the Omega-1 (Ω1) loop, which covers the sterol binding pocket, attenuates sterol transfer activity. To gain insight into the attenuating mechanism of the L124D mutation, we conducted structural and biophysical studies of wild-type and L124D STARD4. These studies show that the L124D mutation reduces the conformational flexibility of the protein, resulting in a diminished level of membrane interaction and sterol transfer. These studies also reveal that the C-terminal α-helix, and not the Ω1 loop, partitions into the membrane bilayer. On the basis of these observations, we propose a model of STARD4 membrane interaction and sterol binding and release that requires dynamic movement of both the Ω1 loop and membrane insertion of the C-terminal α-helix.
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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.