Protein-lipid interactions modulate lipid composition, membrane dynamics and structure

The interactions of proteins with membrane surfaces are important to many biological processes, including signaling, recognition, and membrane trafficking, cell division and cell structure. When the Fluid Mosaic Model (FMM) of membrane structure was introduced by Singer and Nicolson (1972), it was envisaged as a basic model for cell membranes that could clarify existing observations on membrane proteins and lipid structures and their dynamics. Accordingly, the membrane was topologically defined as a biological fluid of proteins and lipids oriented in two dimensions. In the FMM, amphipathic phospholipids are oriented in a lamellar mesophase organization with hydrophobic fatty acyl chains embedded within the interior of the membrane and the hydrophilic polar groups facing the aqueous environment. However, several biological processes cannot be explained on the basis of this typical phospholipid orientation but exhibit other conformations. The Lipid Whisker Model (LWM) is an extension of the FMM, introduced upon observations into the conformation of oxidized phospholipid (oxPL) species recognized by CD36 (Li et al., 2007). Thus, in the LWM, when cell membranes undergo oxidation, if not adapted by the action of phospholipases, they may “produce whiskers” including a variety of oxidized sn-2 fatty acids of diverse structures. In the (LWM), the assembly of many oxPL within cell membranes is different compared with one observed in non-oxPL described in the FMM. Indeed, biophysical evidence indicates that addition of an oxygen atom to the acyl chain produces significant changes that prevent its immersion in the interior of the membrane, because the presence of peroxyl radicals project toward the aqueous interface. However, controversies exist on the validity of the validity of this “floating peroxyl radical” hypothesis. This has been discussed in an opinion article (Catala, 2015). Fil: Catala, Angel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas; Argentina