Sphingomyelin is a major sphingolipid in mammalian cells. Recent results indicate that sphingomyelin is a reservoir of lipid second messengers, ceramide and sphingosine-1-phosphate. Sphingomyelin is also a major component of sphingolipid and cholesterol-rich membrane domains (lipid rafts). Lysenin is a pore-forming toxin that specifically binds sphingomyelin. The binding of lysenin to sphingomyelin is dependent on the membrane distribution of the lipid, i.e. the toxin selectively binds sphingomyelin clusters. Development of a non-toxic lysenin mutant revealed the spatial and functional heterogeneity of sphingolipid-rich membrane domains.
Download full-text PDF |
Source |
---|---|
http://dx.doi.org/10.1016/j.bbagen.2007.09.001 | DOI Listing |
Analyst
July 2024
Department of Chemistry, Graduate School of Science, Kyushu University, 744 Motooka, Nishi-ku, Fukuoka 819-0395, Japan.
In biological membranes, lipids often interact with membrane proteins (MPs), regulating the localization and activity of MPs in cells. Although elucidating lipid-MP interactions is critical to comprehend the physiological roles of lipids, a systematic and comprehensive identification of lipid-binding proteins has not been adequately established. Therefore, we report the development of lipid-immobilized beads where lipid molecules were covalently immobilized.
View Article and Find Full Text PDFJ Am Chem Soc
July 2021
Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, California 92093, United States.
Despite the central importance of lipid membranes in cellular organization, it is challenging to reconstitute their formation from minimal chemical and biological elements. Here, we describe a chemoenzymatic route to membrane-forming noncanonical phospholipids in which cysteine-modified lysolipids undergo spontaneous coupling with fatty acyl-CoA thioesters generated enzymatically by a fatty acyl-CoA ligase. Due to the high efficiency of the reaction, we were able to optimize phospholipid formation in a cell-free transcription-translation (TX-TL) system.
View Article and Find Full Text PDFMethods Enzymol
June 2021
UMR 7021 CNRS, Université de Strasbourg, Illkirch, France. Electronic address:
Sensors (Basel)
October 2020
Department of Physics, Boise State University, Boise, ID 83725, USA.
Lysenin is a pore-forming protein extracted from the earthworm , which inserts large conductance pores in artificial and natural lipid membranes containing sphingomyelin. Its cytolytic and hemolytic activity is rather indicative of a pore-forming toxin; however, lysenin channels present intricate regulatory features manifested as a reduction in conductance upon exposure to multivalent ions. Lysenin pores also present a large unobstructed channel, which enables the translocation of analytes, such as short DNA and peptide molecules, driven by electrochemical gradients.
View Article and Find Full Text PDFInt J Mol Sci
August 2020
Laboratory of Biomembrane, Tokyo Metropolitan Institute of Medical Science, Tokyo 156-8506, Japan.
Lipid rafts are dynamic assemblies of glycosphingolipids, sphingomyelin, cholesterol, and specific proteins which are stabilized into platforms involved in the regulation of vital cellular processes. The rafts at the cell surface play important functions in signal transduction. Recent reports have demonstrated that lipid rafts are spatially and compositionally heterogeneous in the single-cell membrane.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!