Identification of divergent

Background: A hallmark of the eukaryotic cell is the regulated transport between the nucleus and cytoplasm, which is mediated by a multi-subunit protein assembly called the nuclear pore complex (NPC). While its overall architecture has been preserved across eukaryotes, variations in NPC structure appear to have tuned its function in different organisms. Outside of a handful of model systems, the NPC has not been comprehensively studied. This is particularly true of species that are not closely related to well-studied models, such as apicomplexan parasites. Indeed, the evolutionary divergence of Apicomplexa has complicated facile prediction of these proteins in these organisms. Because of this, the NPC components remain largely unidentified, and therefore NPC cellular function in Apicomplexa is poorly understood. Principal Findings: Here we identified, experimentally validated, and functionally characterized protein components of the NPC in the apicomplexan parasite Conclusion: Our work highlights the distinct composition of multiple subcomplexes of the