NUP42 (nucleoporin 42) is a nuclear pore complex (NPC) component that plays a critical role in mRNA export and nucleocytoplasmic transport. Its primary function is to facilitate the activation of the DEAD-box helicase DDX19 (Dbp5 in yeast) through interaction with Gle1, enabling removal of mRNA export factors from exported mRNAs 1. The Nup42 carboxy-terminal domain binds Gle1 at a distinct interface from the Gle1-DDX19 interaction site, and this high-affinity interaction is integral to efficient mRNA export 2. NUP42 also participates in Crm1-mediated nuclear protein export, selectively interacting with export complexes 3, and associates with the Smt3-specific protease Ulp1 at the nuclear pore 4. Clinically, NUP42 dysfunction has implications for neurological disease. Mutations affecting the Nup42-Gle1 interaction cause decreased Gle1 thermostability and have been linked to motor neuron diseases 1. Additionally, genome-wide association studies using dopaminergic neuron-specific expression quantitative trait loci nominated NUP42 as a potential causal gene for Parkinson's disease 5. During coronavirus infection, NUP42 undergoes cytoplasmic dispersion and structural alterations that disrupt nucleocytoplasmic trafficking and suppress antiviral immune responses 6.