Authors
Amilina, H., Santos, H. J., Imai, K., Nozaki, T.
Abstract
Nuclear pore complexes (NPCs) are the gateways for macromolecular exchange between the nucleus and cytoplasm. Although NPC architecture is broadly conserved across eukaryotes, substantial lineage-specific diversification has emerged, particularly among divergent protists. Here, we investigated the NPC of Entamoeba histolytica, an evolutionarily divergent amoebozoan and the causative agent of amebiasis. Using the FG-repeat nucleoporin EhNup98-like as bait in affinity purification coupled with mass spectrometry, we identified various associated proteins, including a previously uncharacterized candidate nucleoporin with similarity to Nup53/Nup35. Reciprocal proteomic analysis of EhNup53-like further recovered a broader repertoire of candidate NPC components, including proteins corresponding to conserved nucleoporins as well as several uncharacterized nuclear pore-associated proteins. Structural analyses indicated that this EhNup53-like protein retains a conserved RNA recognition motif (RRM)-like fold despite extensive primary-sequence divergence, while displaying lineage-specific features, including an expanded repeat-rich region and truncation of the C-terminal region typically associated with Nup155 binding. Together, these findings expand the known candidate nucleoporins in E. histolytica and reveal NPC-associated networks that combines recognizable conserved components with extensively remodeled and poorly characterized proteins. Our study highlights the evolutionary plasticity of the NPC and provides a framework for understanding how nuclear pore architecture has diversified across deeply divergent eukaryotic lineages.
Preprint server:
bioRxiv
The authors list and abstract were imported from bioRxiv on 18 Sep 2026.
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