ArticleBiophysical journal2009
Fatty acid transfer from Yarrowia lipolytica sterol carrier protein 2 to phospholipid membranes.
Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 25 citations in OpenAlex.
- Advances inFoods (Basel, Switzerland) · 2025Review
- Fifty years of biophysics in Argentina.Biophysical reviews · 2023Article
- Sterol carrier protein 2: A promising target in the pathogenesis of atherosclerosis.Genes & diseases · 2023Review
- Quantitative Proteomic Analysis of Tibetan Pig Livers at Different Altitudes.Molecules (Basel, Switzerland) · 2023Article
- HSDL2 Acts as a Promoter in Pancreatic Cancer by Regulating Cell Proliferation and Lipid Metabolism.OncoTargets and therapy · 2021Article
- Lipid-free antigen B subunits from echinococcus granulosus: oligomerization, ligand binding, and membrane interaction properties.PLoS neglected tropical diseases · 2015Article
- The crystal structure of sterol carrier protein 2 from Yarrowia lipolytica and the evolutionary conservation of a large, non-specific lipid-binding cavity.Journal of structural and functional genomics · 2013Article
- Effects of mutations in Aedes aegypti sterol carrier protein-2 on the biological function of the protein.Biochemistry · 2010Article
- Kinetics of stearic acid transfer between human serum albumin and sterically stabilized liposomes.European biophysics journal : EBJ · 2010Article
- Sterol carrier protein-x gene and effects of sterol carrier protein-2 inhibitors on lipid uptake in Manduca sexta.BMC physiology · 2010Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sterol carrier protein 2 (SCP2) is an intracellular protein domain found in all forms of life. It was originally identified as a sterol transfer protein, but was recently shown to also bind phospholipids, fatty acids, and fatty-acyl-CoA with high affinity. Based on studies carried out in higher eukaryotes, it is believed that SCP2 targets its ligands to compartmentalized intracellular pools and participates in lipid traffic, signaling, and metabolism. However, the biological functions of SCP2 are incompletely characterized and may be different in microorganisms. Herein, we demonstrate the preferential localization of SCP2 of Yarrowia lipolytica (YLSCP2) in peroxisome-enriched fractions and examine the rate and mechanism of transfer of anthroyloxy fatty acid from YLSCP2 to a variety of phospholipid membranes using a fluorescence resonance energy transfer assay. The results show that fatty acids are transferred by a collision-mediated mechanism, and that negative charges on the membrane surface are important for establishing a "collisional complex". Phospholipids, which are major constituents of peroxisome and mitochondria, induce special effects on the rates of transfer. In conclusion, YLSCP2 may function as a fatty acid transporter with some degree of specificity, and probably diverts fatty acids to the peroxisomal metabolism.
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