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The enzyme gamma-secretase catalyzes the proteolytic cleavage of the membrane to generate amyloid β-peptide from β-amyloid precursor protein. The presenilin (PS) protein is one of four integral membrane protein components of the mature γ-secretase complex. The PS protein itself undergoes endoproteolytic processing to generate stable heterodimers of N-terminal and C-terminal fragments (NTF and CTF, respectively). Here we demonstrate that coexpression of PS1 NTFs and CTFs functionally mimics the expression of full-length PS1 protein and restores γ-secretase activity in PS-deficient mammalian cells. The coexpressed fragments reassociate with each other inside the cell, where they also interact with nicastrin, another γ-secretase complex component.