NDLI: Regulation of amyloid beta-protein precursor by phosphorylation and protein interactions.

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Identification of an evolutionarily conserved extracellular threonine residue critical for surface expression and its potential coupling of adjacent voltage-sensing and gating domains in voltage-gated potassium channels.

Thematic minireview series on the molecular basis of Alzheimer disease.

Amyloid precursor protein trafficking, processing, and function.

The role of amyloid precursor protein processing by BACE1, the beta-secretase, in Alzheimer disease pathophysiology.

Intramembrane proteolysis by gamma-secretase.

Regulation of amyloid beta-protein precursor by phosphorylation and protein interactions.

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RNA Editing of Androgen Receptor Gene Transcripts in Prostate Cancer Cells

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Activation-dependent hindrance of photoreceptor G protein diffusion by lipid microdomains.

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Structural classification of toxic amyloid oligomers.

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KLF6 induces apoptosis in prostate cancer cells through up-regulation of ATF3.

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Structural elucidation of the nonclassical secondary cell wall polysaccharide from Bacillus cereus ATCC 10987. Comparison with the polysaccharides from Bacillus anthracis and B. cereus type strain ATCC 14579 reveals both unique and common structural features.

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Regulation of amyloid beta-protein precursor by phosphorylation and protein interactions.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Nakaya, Tadashi Suzuki, Toshiharu
Description	Author Affiliation: Suzuki T ( Laboratory of Neuroscience, Graduate School of Pharmaceutical Sciences, Hokkaido University, Kita-ku, Sapporo 060-0812, Japan. tsuzuki@pharm.hokudai.ac.jp)
Abstract	Amyloid beta-protein precursor (APP), a type I membrane protein, is cleaved by primary alpha-or beta-secretase and secondary gamma-secretase. Cleavage of APP by beta- and gamma-secretases generates amyloid beta-protein, the main constituent of the cerebrovascular amyloid that accompanies Alzheimer disease. The generation and aggregation of amyloid beta-protein in the brain are believed to be a primary cause of Alzheimer disease pathogenesis, and indeed, early onset Alzheimer disease is genetically linked to APP and also to presenilins 1 and 2, which are components of gamma-secretase. Proteolytic cleavage of APP has been investigated as a candidate target for Alzheimer disease therapy, but the mechanisms regulating APP metabolism are still unclear. APP is a type I membrane protein with a short cytoplasmic region consisting of 47 amino acids. Recent research has elucidated the significance of the cytoplasmic region in the metabolism, trafficking, and physiological function of APP. The structure and function of the APP cytoplasmic domain can be modified by phosphorylation and through interaction with cytoplasmic proteins. This minireview summarizes a large body of recent information on the regulation of APP by phosphorylation and protein interaction, along with some of the physiological functions of APP. Recent findings regarding the regulation of APP processing contribute to the development of novel drugs and/or therapies for Alzheimer disease.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	44
Volume Number	283
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2008-10-31
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Alzheimer Disease Metabolism Amyloid Beta-Peptides Gene Expression Regulation Amino Acid Sequence Amino Acids Chemistry Animals Cytoplasm Mice Molecular Conformation Molecular Sequence Data Neurons Phosphorylation Protein Interaction Mapping Protein Structure, Tertiary 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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