[HTML][HTML] The intracellular domain of the β-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a notch-like manner
WT Kimberly, JB Zheng, SY Guénette… - Journal of Biological …, 2001 - ASBMB
The β-amyloid precursor protein (APP) is a ubiquitous receptor-like molecule without a
known function. However, the recent recognition that APP and Notch undergo highly similar
proteolytic processing has suggested a potential signaling function for APP. After ligand
binding, Notch is cleaved by the ADAM-17 metalloprotease followed by an intramembrane
cleavage mediated by γ-secretase. The γ-secretase cut releases the Notch intracellular
domain (NICD), which enters the nucleus and modulates transcription. Because APP is …
known function. However, the recent recognition that APP and Notch undergo highly similar
proteolytic processing has suggested a potential signaling function for APP. After ligand
binding, Notch is cleaved by the ADAM-17 metalloprotease followed by an intramembrane
cleavage mediated by γ-secretase. The γ-secretase cut releases the Notch intracellular
domain (NICD), which enters the nucleus and modulates transcription. Because APP is …