NUP155 is an essential component of the nuclear pore complex (NPC) that mediates nucleocytoplasmic transport and maintains nuclear envelope integrity 12. The protein is highly conserved across eukaryotes and ubiquitously expressed in human tissues, with two major transcript variants resulting from alternative splicing and polyadenylation 2. Mechanistically, NUP155 serves as a structural scaffold component that stabilizes NPC assembly and forms critical protein-protein interactions, including binding to lamin A/C at the nuclear envelope 34. Recent cryo-EM studies have positioned NUP155 within the cytoplasmic ring structure of the NPC, where it contributes to the overall architectural framework 5. Functionally, NUP155 regulates nucleocytoplasmic transport of proteins and mRNA, and participates in cancer-related pathways including p53 signaling through translational control mechanisms 6. Disease relevance includes mutations causing familial atrial fibrillation through impaired lamin A/C-NUP155 interactions that disrupt nucleocytoplasmic transport 3. Additionally, NUP155 is upregulated across multiple cancer types and correlates with poor prognosis, tumor progression, and immune microenvironment alterations 7. The protein can be targeted for degradation via TRIM21-mediated pathways, leading to nuclear envelope disruption and cell death 8.