Both the sequence and length of the C terminus of PEN-2 are critical for intermolecular interactions and function of presenilin complexes - PubMed (original) (raw)

. 2004 Nov 5;279(45):46455-63.

doi: 10.1074/jbc.M406289200. Epub 2004 Aug 17.

Nobuo Sanjo, Fusheng Chen, Yong-Jun Gu, Cortney Shier, Agnes Petit, Toshitaka Kawarai, Taiichi Katayama, Stephen D Schmidt, Paul M Mathews, Gerold Schmitt-Ulms, Paul E Fraser, Peter St George-Hyslop

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Both the sequence and length of the C terminus of PEN-2 are critical for intermolecular interactions and function of presenilin complexes

Hiroshi Hasegawa et al. J Biol Chem. 2004.

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Abstract

Presenilin 1 or presenilin 2, nicastrin, APH-1, and PEN-2 form high molecular weight complexes that play a pivotal role in the cleavage of various Type I transmembrane proteins, including the beta-amyloid precursor protein. The specific function of PEN-2 is unclear. To explore its function and intermolecular interactions, we conducted deletion and mutagenesis studies on a series of conserved residues at the C terminus of PEN-2. These studies suggest that: 1) both the presence and amino acid sequence of the conserved DYLSF domain at the C terminus of PEN-2 (residues 90-94) is critical for binding PEN-2 to other components in the presenilin complex and 2) the overall length of the exposed C terminus is critical for functional gamma-secretase activity.

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