Publications by authors named "I Levental"
Chimeric antigen receptor T cells (CART) targeting CD19 through CD28.ζ signaling induce rapid lysis of leukemic blasts, contrasting with persistent tumor control exhibited by 4-1BB.ζ-CART.
View Article and Find Full Text PDFMembranes are molecular interfaces that compartmentalize cells to control the flow of nutrients and information. These functions are facilitated by diverse collections of lipids, nearly all of which are distributed asymmetrically between the two bilayer leaflets. Most models of biomembrane structure and function often include the implicit assumption that these leaflets have similar abundances of phospholipids.
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- Membrane scaffold proteins-based nanodiscs (NDs) enable detailed study of membrane proteins in conditions similar to their natural environment, but traditional methods using detergents can alter protein structure and function.
- A new approach using engineered membrane-solubilizing peptides allows for the extraction of membrane proteins without detergents, creating detergent-free nanodiscs (DeFrNDs) that better preserve native conditions.
- DeFrNDs facilitate high-resolution structural analysis and biochemical studies of membrane proteins directly from native membranes, showcasing their utility in research.
Article Synopsis
- Lipid rafts are specialized areas in cell membranes that help organize proteins and regulate cellular functions, but how desmosomal proteins interact with these rafts is not well understood.
- Researchers focused on desmoglein-1 (DSG1), a key desmosomal protein, and found that specific features of its transmembrane domain (TMD), such as length and size, significantly affect its association with lipid rafts.
- The study concluded that the efficient association of DSG1 with lipid rafts is crucial for the formation and stability of desmosomes, which are important for cell adhesion and mechanical strength.
Caveolin is a monotopic integral membrane protein, widely expressed in metazoa and responsible for constructing enigmatic membrane invaginations known as caveolae. Recently, the high-resolution structure of a purified human caveolin assembly, the CAV1-8S complex, revealed a unique organization of 11 protomers arranged in a tightly packed, radially symmetric spiral disc. One face and the outer rim of this disc are highly hydrophobic, suggesting that the complex incorporates into membranes by displacing hundreds of lipids from one leaflet.
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