Functional rafts in cell membranes

TL;DR: It is shown that two distinct phospholipase C‐coupled receptors share the same, homogeneously distributed PIP2 pool at the plasma membrane, even though the neurokinin A receptor is localized to microdomains and is cholesterol dependent in its PIP1 signaling whereas the endothelin receptor is not.

TL;DR: It is found that EGCG but not EC caused dramatic changes in the function of bilayer-incorporated gramicidin channels, and they may play a critical role in the anticancer effects of this and related compounds.

TL;DR: It is demonstrated that the Wiskott-Aldrich syndrome protein (WASP) is recruited to lipid rafts immediately after TCR and CD28 triggering and is required for the movements of lipid rafting.

TL;DR: It is shown that the C-terminal cytoplasmic domain of occludin, the only known transmembrane protein of tight junctions, was sufficient to mediate basolateral expression of a chimeric protein and appears to govern intracellular transport of occLudin.

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.