Advances in ribosome profiling have revealed that our understanding of the proteome is far from complete. Beyond the well-annotated set of canonical proteins lies the dark proteome, a growing collection of previously overlooked translation products, often encoded by small open reading frames (sORFs) hidden in regions once dismissed as non-coding.

These newly discovered peptides are frequently short, dynamic, and tightly regulated. Many respond to environmental cues or cellular stress, suggesting they play key roles in modulating metabolism, signaling pathways, or cell identity. Yet, their functions remain largely unexplored.

Our lab is particularly interested in how the mitochondrial genome contributes to this emerging layer of regulation. Despite being compact, mitochondria retain their own genetic code and translation machinery.

By charting this uncharacterized space, we hope to uncover new regulatory molecules that link mitochondrial activity to cell fate decisions, offering fresh insight into how cells adapt to stress and mediate plasticity.