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Presenilin 1 is involved in maturation and trafficking of N-cadherin to the plasma membrane

✍ Scribed by Kengo Uemura; Naoyuki Kitagawa; Ryuichi Kohno; Akira Kuzuya; Takashi Kageyama; Kazuhisa Chonabayashi; Hiroshi Shibasaki; Shun Shimohama

Publisher: John Wiley and Sons
Year: 2003
Tongue: English
Weight: 812 KB
Volume: 74
Category: Article
ISSN: 0360-4012
DOI: 10.1002/jnr.10753

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✦ Synopsis

Abstract

One pathological characteristic of Alzheimer's disease (AD) is extensive synapse loss. Presenilin 1 (PS1) is linked to the pathogenesis of early onset familial Alzheimer's disease (FAD) and is localized at the synapse, where it binds N‐cadherin and modulates its adhesive activity. To elucidate the role of the PS1/N‐cadherin interaction in synaptic contact, we established SH‐SY5Y cells stably expressing wild‐type (wt) PS1 and dominant‐negative (D385A) PS1. We show that the formation of cadherin‐based cell–cell contact among SH‐SY5Y cells stably expressing D385A PS1 was suppressed. Conversely, wt PS1 cells exhibited enhanced cell–cell contact and colony formation. Suppression of cell–cell contact in D385A cells was accompanied by an alteration in N‐cadherin subcellular localization; N‐cadherin was retained mainly in the endoplasmic reticulum (ER) and cell surface expression was reduced. We conclude that PS1 is essential for efficient trafficking of N‐cadherin from the ER to the plasma membrane. PS1‐mediated delivery of N‐cadherin to the plasma membrane is important for N‐cadherin to exert its physiological function, and it may control the state of cell–cell contact. © 2003 Wiley‐Liss, Inc.

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