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Updated: Jun 10, 2026

Precise Visualization of Insulin Receptors A and B in Murine Brain with an RNA In Situ Hybridization Assay
Published on: July 15, 2025
Insulin regulates Presenilin 1 localization via PI3K/Akt signaling
Masato Maesako1, Kengo Uemura, Masakazu Kubota
1School of Human Health Sciences, Kyoto University Graduate School of Medicine, 53, Shogoinkawahara-cho, Sakyo-ku, Kyoto 606-8507, Japan.
Abstract:
Recently, insulin signaling has been highlighted in the pathology of Alzheimer's disease (AD). Although the association between insulin signaling and Tau pathology has been investigated in several studies, the interaction between insulin signaling and Presenilin 1 (PS1), a key molecule of amyloid beta (Abeta) pathology, has not been elucidated so far. In this study, we demonstrated that insulin inhibited PS1 phosphorylation at serine residues (serine 353, 357) via phosphatidylinositol 3-kinase (PI3K)/Akt signal pathway and strengthened the trimeric complex of PS1/N-cadherin/beta-catenin, consequently relocalizing PS1 to the cell surface. Since our recent report suggests that PS1/N-cadherin/beta-catenin complex regulates Abeta production, it is likely that insulin signaling affects Abeta pathology by regulating PS1 localization.
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