Access

Brief Communication

Nature Cell Biology 3, 751–754 (1 August 2001) | doi:10.1038/35087069

Nicastrin binds to membrane-tethered Notch

Fusheng Chen , Gang Yu , Shigeki Arawaka , Masaki Nishimura , Toshitaka Kawarai , Haung Yu , Anurag Tandon , Agnes Supala , You Qiang Song , Ekaterina Rogaeva , Paul Milman , Christine Sato , Cong Yu , Christopher Janus , Julie Lee , Lixin Song , Lili Zhang , Paul E. Fraser & P. H. St George-Hyslop

The presenilins and nicastrin, a type 1 transmembrane glycoprotein, form high molecular weight complexes that are involved in cleaving the β-amyloid precursor protein (βAPP) and Notch in their transmembrane domains. The former process (termed γ-secretase cleavage) generates amyloid β-peptide (Aβ), which is involved in the pathogenesis of Alzheimer's disease.