NDLI: Cytoplasmic fragment of Alcadein generated by regulated intramembrane proteolysis enhances amyloid ß-protein precursor (APP) transport into the late secretory pathway and facilitates APP cleavage.

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Cytoplasmic fragment of Alcadein generated by regulated intramembrane proteolysis enhances amyloid ß-protein precursor (APP) transport into the late secretory pathway and facilitates APP cleavage.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Araki, Yoichi Kimura, Ayano Urano, Satomi Piao, Yi Hata, Saori Nakaya, Tadashi Taru, Hidenori Suzuki, Toshiharu Yamamoto, Tohru Sobu, Yuriko Takei, Norio
Description	Author Affiliation: Takei N ( From the Laboratory of Neuroscience, Graduate School of Pharmaceutical Sciences, Hokkaido University, Kita-12 Nishi-6, Kita-ku, Sapporo 060-0812, Japan and.); Sobu Y ( From the Laboratory of Neuroscience, Graduate School of Pharmaceutical Sciences, Hokkaido University, Kita-12 Nishi-6, Kita-ku, Sapporo 060-0812, Japan and.); Kimura A ( From the Laboratory of Neuroscience, Graduate School of Pharmaceutical Sciences, Hokkaido University, Kita-12 Nishi-6, Kita-ku, Sapporo 060-0812, Japan and.); Urano S ( From the Laboratory of Neuroscience, Graduate School of Pharmaceutical Sciences, Hokkaido University, Kita-12 Nishi-6, Kita-ku, Sapporo 060-0812, Japan and.); Piao Y ( From the Laboratory of Neuroscience, Graduate School of Pharmaceutical Sciences, Hokkaido University, Kita-12 Nishi-6, Kita-ku, Sapporo 060-0812, Japan and.); Araki Y ( From the Laboratory of Neuroscience, Graduate School of Pharmaceutical Sciences, Hokkaido University, Kita-12 Nishi-6, Kita-ku, Sapporo 060-0812, Japan and.); Taru H ( From the Laboratory of Neuroscience, Graduate School of Pharmaceutical Sciences, Hokkaido University, Kita-12 Nishi-6, Kita-ku, Sapporo 060-0812, Japan and.); Yamamoto T ( Department of Molecular Neurobiology, Faculty of Medicine, Kagawa University, Miki-cho 761-0793, Japan.); Hata S ( From the Laboratory of Neuroscience, Graduate School of Pharmaceutical Sciences, Hokkaido University, Kita-12 Nishi-6, Kita-ku, Sapporo 060-0812, Japan and.); Nakaya T ( From the Laboratory of Neuroscience, Graduate School of Pharmaceutical Sciences, Hokkaido University, Kita-12 Nishi-6, Kita-ku, Sapporo 060-0812, Japan and.); Suzuki T ( From the Laboratory of Neuroscience, Graduate School of Pharmaceutical Sciences, Hokkaido University, Kita-12 Nishi-6, Kita-ku, Sapporo 060-0812, Japan and tsuzuki@pharm.hokudai.ac.jp.)
Abstract	The neural type I membrane protein Alcadein (Alc ), is primarily cleaved by amyloid ß-protein precursor (APP) -secretase to generate a membrane-associated carboxyl-terminal fragment (Alc CTF), which is further cleaved by Î³-secretase to secrete p3-Alc peptides and generate an intracellular cytoplasmic domain fragment (Alc ICD) in the late secretory pathway. By association with the neural adaptor protein X11L (X11-like), Alc and APP form a ternary complex that suppresses the cleavage of both Alc and APP by regulating the transport of these membrane proteins into the late secretory pathway where secretases are active. However, it has not been revealed how Alc and APP are directed from the ternary complex formed largely in the Golgi into the late secretory pathway to reach a nerve terminus. Using a novel transgenic mouse line expressing excess amounts of human Alc CTF (hAlc CTF) in neurons, we found that expression of hAlc CTF induced excess production of hAlc ICD, which facilitated APP transport into the nerve terminus and enhanced APP metabolism, including Aß generation. In vitro cell studies also demonstrated that excess expression of Alc ICD released both APP and Alc from the ternary complex. These results indicate that regulated intramembrane proteolysis of Alc by Î³-secretase regulates APP trafficking and the production of Aß in vivo.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	2
Volume Number	290
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2015-01-09
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Amyloid Precursor Protein Secretases Genetics Metabolism Amyloid Beta-Protein Precursor Calcium-Binding Proteins Chemistry Animals Cadherins Carrier Proteins Cytoplasm Golgi Apparatus Membrane Proteins Mice Mice, Transgenic Nerve Tissue Proteins Protein Structure, Tertiary Proteolysis Secretory Pathway Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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