Gamma secretase mediates the cleavage of its substrates within the lipid bilayer of cellular membranes. The process begins with the recognition and binding of the substrate to the complex, primarily facilitated by nicastrin. Once bound, the substrate undergoes sequential proteolytic cleavage by presenilin. This cleavage releases the intracellular and extracellular domains of the substrate, which can then participate in various cellular signaling pathways.
