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Here, molecular level changes in lipid organization induced by multivalent toxin binding were investigated using grazing incidence X-ray diffraction. Structural changes to lipid monolayers at the air-water interface and bilayers at the solid-water interface were studied before and after specific binding of cholera toxin to membrane embedded receptors. At biologically relevant surface pressures, protein binding perturbed lipid packing within monolayers and bilayers resulting in topological defects and the emergence of a new orientationally textured lipid phase. In bilayers this altered lipid order was transmitted from the receptor laden exterior membrane leaflet to the inner leaflet, representing a potential mechanism for lipid mediated outside-in signaling by multivalent protein binding. It is further hypothesized that cell-surface micro-domains exhibiting this type of lipid order may serve as nucleation sites for vesicle formation in clathrin independent endocytosis of cholera toxin.<\/jats:p>","DOI":"10.1073\/pnas.1014579108","type":"journal-article","created":{"date-parts":[[2011,4,8]],"date-time":"2011-04-08T00:05:30Z","timestamp":1302221130000},"page":"6975-6980","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":76,"title":["Membrane texture induced by specific protein binding and receptor clustering: active roles for lipids in cellular function"],"prefix":"10.1073","volume":"108","author":[{"given":"E. B.","family":"Watkins","sequence":"first","affiliation":[{"name":"Biophysics Graduate Group, University of California, Davis, CA 95616;"},{"name":"Manuel Lujan Jr. Neutron Scattering Center, Los Alamos National Laboratory, Los Alamos, NM 87545;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"C. 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