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EN
Lipid rafts (LRs) are highly enriched in glycosphingolipids, sphingomyelins, and cholesterol membrane microdomains, existing in a liquid-ordered phase of the plasma membrane. In the literature, LRs are also known as detergent-insoluble membranes, detergent- resistant membranes, glycosphingolipids-enriched membranes, detergent-insoluble glycolipid-rich membranes, and Triton-insoluble floating fractions. These properties enabled their separation from the rest of the phospholipid bilayer, providing new insight into the structure of the plasma membrane, which until then was believed to represent a two-dimensional liquid structure with proteins uniformly solubilized in the lipid solvent. Although there have been many articles concerning LRs, there is still controversy about their existence in the natural state, their size, definition, and function. Different techniques have been developed to visualize LRs in living cells, but the results are contradictory. In this minireview, some recent papers concerning LRs, their existence in vivo, their dynamics, size, methods of isolation, and their association with different proteins are discussed.
EN
The plasma membrane of T cells is made up of a combination of phospholipids and proteins organized as glycolipoprotein microdomains termed lipid rafts. The structural assembly of lipid rafts was investigated by various physical and biochemical assays. Depending on the differentiation status of T cells, the lipid rafts seclude various protein receptors instrumental for the early T cell signaling, cytoskeleton reorganization, protein and membrane trafficking, and the entry of infectious organisms into the cells. This review article summarizes recent information on the assembly of lipid rafts in plasma membrane of T cells and their signaling output in mature and thymic precursors towards cell growth and differentiation, and possible modalities by which the function of lipid rafts can be altered by drugs and T cell ligands. The concept of using lipid rafts as a target for pharmaceutical compounds and biological T cell ligands to ultimately alter the T cell function is discussed.
EN
The Ly-6 locus on mouse chromosome 15 encodes a family of 10?12 kDa proteins that are linked to the cell surface by a glycosylphosphatidyl-inositol anchor and have cell signaling and cell adhesion properties. Expression of Ly-6 proteins is tightly regulated during development; these proteins continue to serve as excellent differentiation surface markers on normal and abnormal cells, but their role in driving cellular differentiation is still emerging. Recent studies suggest that Ly-6 gene products participate in regulating signaling through other cell type-specific receptors, perhaps by virtue of these proteins being localized in lipid rafts that play a key role in relaying signals from the membrane to the nucleus. Ligands for some Ly-6 proteins have been reported; the consequence of their interactions with the Ly-6 receptor remains to be fully uncovered. Mouse Ly-6-like proteins have also been reported from a variety of life forms ranging from Caenorhabditis elegans to humans that show a limited amino acid identity and share structural features with members of mouse Ly-6. Despite these similarities, the non-murine Ly-6 proteins bind distinct ligands and appear to have different cellular functions. All members of the Ly-6 super gene family perhaps evolved from an ancestral gene by a gene duplication mechanism.
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