Although it is unclear how are these proteins transported to the PV, their partial co-localization in the schizont stage may reflect a common ASP9521 transport pathway that may involved a fraction of ER derived vesicles. It will be interesting to understand whether this transport represents a generic ����overflow���� of highly abundant precursors of nuclear formation or a specific transport mechanism that enables some of the nuclear proteins to fulfill a specific function, distinct from their original role in the nuclei. The PV is created during merozoite invasion. It provides an enclosed environment for parasite development and facilitates nutrient and protein transport between the parasite and host cytoplasm. However, the molecular basis of PV formation, maintenance, and many other aspects of its function are poorly understood. Although, a number of proteins including the Etramp family have been localized to the PV, their molecular functions remain largely uncharacterized. Like these proteins, the functional role of H3 in the PV remains to be investigated, however, this localization indicates its ����moonlighting function����. Moreover, this function is in some way linked with monomethylation of H3 at the lysine residue 9. Alternative functions were previously reported for at least two additional highly abundant Plasmodium proteins. First, P. falciparum aldolase has been implicated in forming a physical bridge between the surface adhesins and the actin Urethane cytoskeleton during the invasion process. This interaction is particularly peculiar since PfAld belongs to the class I aldolases that are highly conserved and in the vast majority of eukaryotic organisms involved strictly in glycolysis. Interestingly, the aldolase involvement in invasion appears to be evolutionarily conserved in most Plasmodium species as well as the related apicomplexan Toxoplasma gondii. Second example is enolase, that similarly to aldolase, is a highly conserved glycolytic enzyme but in P. falciparum it also localizes in the nucleus, food vacuole, and cytoskeleton and plasma membrane.