Functional rafts in cell membranes

TL;DR: Paclitaxel-loaded LNCs improved permeability of Ptx across intestinal epithelium compared with free Ptx or Taxol by a factor of 3.5 and transmission electronic microscopy showed the presence of nano-objects on the basolateral side of the Caco-2 cell monolayers when LNC's were applied on the apical side.

TL;DR: It is demonstrated that both receptor types undergo constitutive endocytosis via clathrin-coated pits (CCPs) but that only BRII undergoes also caveola-like internalization, which is prerequisite for the localization of BMP receptors in distinct membrane domains.

TL;DR: The experiments reveal an unprecedented specificity of sphingolipid signaling depending on specific synthesizing enzymes, provide a mechanistic link between hepatic lipid deposition and mitochondrial fragmentation in obesity, and define the CerS6-derived sphingoipid/Mff interaction as a therapeutic target for metabolic diseases.

TL;DR: CD48, a glycosylphosphatidylinositol-anchored molecule, is identified to be the complementary FimH-binding moiety in rodent mast cell membrane fractions and is a functionally relevant microbial receptor on mast cells that plays a role in triggering inflammation.

TL;DR: It is shown that a protein with a glycosylphosphatidyl inositol (GPI) anchor can be recovered from lysates of epithelial cells in a low density, detergent-insoluble form, supporting the model proposed by Simons and colleagues for sorting of certain membrane proteins to the apical surface after intracellular association with glycosphingolipids.

TL;DR: Results strongly indicate that the bivalent antibodies produce an aggregation of the surface immunoglobulin molecules in the plane of the membrane, which can occur only if the immunoglOBulin molecules are free to diffuse in the membrane.

TL;DR: Polarized epithelial cells play fundamental roles in the ontogeny and function of a variety of tissues and organs in mammals and are the first overt sign of cellular differentiation in early embryonic development.

TL;DR: It is shown that caveolin interacts with another well characterized signal transducer, Ras, and that recombinant overexpression of caveolin in intact cells is sufficient to functionally recruit a nonfarnesylated mutant of Ras onto membranes, overcoming the normal requirement for lipid modification of Ras.