Conclusions

The major interest of such a subproteomics approach dealing with PM is that it presents clues on both the membrane compartment where proteins are working and their putative cellular functions. The PM is a site of very specific functions, and consequently the PM proteome is expected to gather many different types of proteins with regard to their physicochemical properties. Therefore, as illustrated by the analysis of the compilation of almost all PM proteomes reported so far, it is necessary to combine complementary protein extraction procedures to retrieve the most exhaustive protein inventory. This analysis confirmed the wide diversity of the proteins as expected; indeed, they display physicochemical characteristics over a large range of values for pI, MW, GRAVY index, and so on; 40% have from 1 to 16 predicted TMDs and 17% display lipid modifications. The functional analysis corroborated functions classically associated with PM, such as transport, endocellular trafficking, and secretion, but it also spotlighted the unique role of PM in cell signaling.

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