ArticleBiochemistry2007
A new N-terminal recognition domain in caveolin-1 interacts with sterol carrier protein-2 (SCP-2).
Article in Biochemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 23 citations in OpenAlex.
- SCP2 mediates the transport of lipid hydroperoxides to mitochondria in chondrocyte ferroptosis.Cell death discovery · 2023Article
- Template-free prediction of a new monotopic membrane protein fold and assembly by AlphaFold2.Biophysical journal · 2023Article
- The building blocks of caveolae revealed: caveolins finally take center stage.Biochemical Society transactions · 2023Article
- Impact ofJournal of lipid research · 2017Article
- Mandarin fish caveolin 1 interaction with major capsid protein of infectious spleen and kidney necrosis virus and its role in early stages of infection.Journal of virology · 2013Article
- Loss of liver FA binding protein significantly alters hepatocyte plasma membrane microdomains.Journal of lipid research · 2012Article
- A novel model of cholesterol efflux from lipid-loaded cells.Acta pharmacologica Sinica · 2010Review
- Effect of sterol carrier protein-2 gene ablation on HDL-mediated cholesterol efflux from cultured primary mouse hepatocytes.American journal of physiology. Gastrointestinal and liver physiology · 2010Article
- Use of dansyl-cholestanol as a probe of cholesterol behavior in membranes of living cells.Journal of lipid research · 2010Article
- Hepatic phenotype of liver fatty acid binding protein gene-ablated mice.American journal of physiology. Gastrointestinal and liver physiology · 2009Article
- Overexpression of sterol carrier protein-2 differentially alters hepatic cholesterol accumulation in cholesterol-fed mice.Journal of lipid research · 2009Article
- Review
- Article
- Effect of sterol carrier protein-2 expression on sphingolipid distribution in plasma membrane lipid rafts/caveolae.Lipids · 2007Article
- Sterol carrier protein-2: new roles in regulating lipid rafts and signaling.Biochimica et biophysica acta · 2007Review
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Although plasma membrane domains, such as caveolae, provide an organizing principle for signaling pathways and cholesterol homeostasis in the cell, relatively little is known regarding specific mechanisms, whereby intracellular lipid-binding proteins are targeted to caveolae. Therefore, the interaction between caveolin-1 and sterol carrier protein-2 (SCP-2), a protein that binds and transfers both cholesterol and signaling lipids (e.g., phosphatidylinositides and sphingolipids), was examined by yeast two-hybrid, in vitro binding and fluorescence resonance energy transfer (FRET) analyses. Results of the in vivo and in vitro assays identified for the first time the N-terminal amino acids (aa) 1-32 amphipathic alpha helix of SCP-2 functionally interacted with caveolin-1. This interaction was independent of the classic caveolin-1 scaffolding domain, in which many signaling proteins interact. Instead, SCP-2 bound caveolin-1 through a new domain identified in the N-terminal domain of caveolin-1 between aa 34-40. Modeling studies suggested that electrostatic interactions between the SCP-2 N-terminal aa 1-32 amphipathic alpha-helical domain (cationic, positively charged face) and the caveolin-1 N-terminal aa 33-59 alpha helix (anionic, negatively charged face) may significantly contribute to this interaction. These findings provide new insights on how SCP-2 enhances cholesterol retention within the cell as well as regulates the distribution of signaling lipids, such as phosphoinositides and sphingolipids, at plasma membrane caveolae.
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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.