Interaction mapping between nucleoporins in the fission yeast Schizosaccharomyces pombe using mass-spectrometry.

This article focuses on the unique structural organization and protein–protein interactions within the nuclear pore complex (NPC) of the fission yeast Schizosaccharomyces pombe. Using affinity capture mass spectrometry on 32 nucleoporins (Nups), the study reveals that the cytoplasmic and nucleoplasmic outer rings of the S. pombe NPC are composed of distinct sets of Nups forming separate complexes, unlike the symmetrical outer rings seen in other eukaryotes. Among inner ring Nups, spNup155 interacts broadly with both outer ring complexes and other NPC subcomplexes, suggesting it functions as a central hub supporting the NPC's asymmetric architecture. These findings provide biochemical evidence for the modular and asymmetric organization of the S. pombe NPC, highlighting spNup155's key role in maintaining its unique structure.