One of the main biological systems that can be used as a model for studying the molecular mechanisms involved in membrane fusion is the formation of the nuclear envelope (NE). NE assembly to form the male pronucleus at fertilization occurs by binding of NE membrane precursor vesicles to chromatin and their fusion. MV1 is an NE precursor vesicle population of low density, highly enriched in [18:0/20:4]PI. The modification of [18:0/20:4]PI to [18:0/20:4]DAG leads to NE formation, and the depletion of MV1 from the total membrane precursors results in the inhibition of NE assembly. Here we show by 2H NMR studies of various physiologically relevant model membranes made of [18:0/20:4]PI, [18:0/20:4]DAG, and saturated and unsaturated PC that membranes of composition similar to MV1 exhibit dramatically enhanced fluidity and non-lamellar structures, thus providing a possible explanation for the essential role of MV1 and the modification of PI to DAG in membrane precursor vesicles during NE assembly.