Mitochondria directly tether to nuclear pores to supply energy for cell division and differentiation
Researchers have discovered that mitochondria directly interact with the nuclear pore complex (NPC) via the protein RANBP2, forming a previously unrecognized contact site between these two organelles. The study, published in Nature, used multiple genomic, proteomic, and imaging approaches—including CRISPR-edited cell lines and mouse models—to characterize this interaction and its functional consequences for nuclear gene regulation and energy supply. The finding expands the known landscape of mitochondrial contact sites and suggests a direct physical mechanism by which mitochondria influence nuclear activity.
A new study published in Nature reports that mitochondria form direct contact sites with the nuclear pore complex (NPC), mediated by the nucleoporin RANBP2 (also known as Nup358). Using a combination of RNA-seq, ChIP-seq, ATAC-seq, proteomics, biophysical modeling of ATP diffusion, and phylogenetic analysis of vertebrate RANBP2, the researchers characterized the molecular basis and functional significance of this interaction. The work builds on a growing body of literature documenting mitochondrial contact sites with organelles such as the endoplasmic reticulum, lysosomes, peroxisomes, and lipid droplets, but represents the first detailed description of a direct mitochondria-NPC interface. The authors propose that this proximity facilitates local ATP delivery to the nucleus and may influence chromatin remodeling and transcriptional regulation. CRISPR-edited cell lines and a mouse model were generated to probe the biological consequences of disrupting this contact. All large datasets have been deposited in public repositories, and the biophysical modeling code is publicly available. The study raises new questions about how mitochondrial positioning near the nucleus contributes to mitonuclear communication in health and disease.
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Mitochondria directly interact with the nuclear pore complex
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