Mitochondria directly interact with the nuclear pore complex

Mitochondria were found to directly interact with the nuclear pore complex on June 10, 2026, a discovery detailed in a Nature publication. This interaction occurs through a binding mechanism involving VDAC1 and RANBP2 proteins. The primary function of this direct contact is to sustain nuclear adenosine triphosphate (ATP) levels. Researchers observed that VDAC1, a voltage-dependent anion channel located in the outer mitochondrial membrane, physically associates with RANBP2, a protein component of the nuclear pore complex. This physical link facilitates the transfer of ATP from mitochondria to the nucleus. The study utilized advanced microscopy techniques and biochemical assays to confirm this novel cellular communication pathway. The findings suggest a more integrated role for mitochondria in nuclear function than previously understood, impacting gene expression and overall cellular energy homeostasis. This direct ATP supply mechanism bypasses the typical diffusion of ATP through the cytoplasm, ensuring a more immediate and localized energy source for nuclear processes. The research team highlighted that disruptions in this VDAC1–RANBP2 interaction could have significant implications for cellular health and disease, particularly in conditions characterized by mitochondrial dysfunction or altered nuclear activity. Further investigation is planned to explore the specific nuclear processes regulated by this direct mitochondrial-nuclear pore complex interaction and its potential therapeutic targets.