FAIMS-enabled N-terminomics analysis reveals novel legumain substrates in murine spleen

Abstract

Proteases comprise approximately 3% of the human genome and catalyse the cleavage of pepKde bonds1. Proteolysis is essenKal for maintaining protein homeostasis, altering substrate structure, funcKon, and localisaKon2. Proteases contribute to vital cellular funcKons such as cell growth and repair3, immune signalling4, and wound healing5,6; dysregulated protease acKviKes underpin numerous pathological condiKons including cancer, inflammaKon neurodegeneraKon, and gastrointesKnal diseases7. Knowledge of specific cleavage events is crucial in understanding the mechanisKc contribuKons of proteases to normal physiology and disease. The need for sensiKve approaches to catalogue these events has led to the development of pepKde-centric N-terminomics methods, which have rapidly developed over the last decade8–10.