Characterization of a phosphoinositide-binding protein containing a PHOX homology domain in the malaria parasite Plasmodium falciparum.

ABSTRACT: Phosphoinositides (PIPs), are key regulators of membrane identity and vesicular trafficking. By dynamically shaping the lipid composition of intracellular membranes, PIPs help ensure the specificity of cargo delivery. In apicomplexan parasites such as Plasmodium falciparum, the biogenesis of the specialized secretory organelles involved in erythrocyte invasion (named rhoptries, micronemes, and dense granules), remains poorly understood, particularly regarding how proteins are sorted and specifically targeted to their respective destinations. Our hypothesis is that PIPs might play a role in this process. We here present our characterization of the P. falciparum protein Pf3D7_0704400, a putative PIP-binding protein containing a PX domain. We named this protein PfPX2, following the previously

SUBMITTER: Roucheray S 

PROVIDER: S-EPMC12546714 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature