Article
Aph-1 contributes to the stabilization and trafficking of the gamma-secretase complex through mechanisms involving intermolecular and intramolecular interactions.
The Journal of biological chemistry - 1 Apr 2005
Niimura Manabu, Isoo Noriko, Takasugi Nobumasa, Tsuruoka Makiko, Ui-Tei Kumiko, Saigo Kaoru, Morohashi Yuichi, Tomita Taisuke, Iwatsubo Takeshi
Abstract excerpt
Gamma-secretase cleaves type I transmembrane proteins, including beta-amyloid precursor protein and Notch, and requires the formation of a protein complex comprised of presenilin, nicastrin, Aph-1, and Pen-2 for its activity. Aph-1 is implicated in the stabilization of this complex, although its precise mechanistic role remains unknown. Substitution of the first glycine within the transmembrane GXXXG motif of...
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