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Beta-amyloid precursor protein is modified with O-linked N-acetylglucosamine
L S Griffith1, M Mathes, B Schmitz
1Department of Biochemistry, Rheinische Friedrich-Wilhelms University, Bonn, Germany.
Journal of Neuroscience Research
|June 1, 1995
Summary
Beta-amyloid precursor protein (APP) is modified with O-GlcNAc, a sugar linkage on cytoplasmic residues. This novel finding in a plasma membrane protein may impact Alzheimer's disease research and protein stability.
Area of Science:
- Molecular Biology
- Biochemistry
- Neuroscience
Background:
- The beta-amyloid precursor protein (APP) is linked to Alzheimer's disease etiology.
- Beta-amyloid is known to be involved in amyloid plaque formation.
- Protein glycosylation, specifically O-GlcNAc modification, is widespread across organisms.
Purpose of the Study:
- To investigate post-translational modifications of the beta-amyloid precursor protein (APP).
- To report the novel O-GlcNAc modification on APP, a plasma membrane protein.
Main Methods:
- Analysis of protein modifications.
- Identification of N-acetylglucosamine linkage to cytoplasmic serine or threonine residues on APP.
Main Results:
- Evidence presented for O-GlcNAc modification of APP at cytoplasmic serine or threonine residues.
- This is the first report of O-GlcNAc modification on a plasma membrane protein.
- O-GlcNAc modification occurs at PEST sequences, potentially increasing proteolytic stability.
Conclusions:
- APP undergoes O-GlcNAc modification, a significant finding for understanding APP function.
- This modification may play a role in protein multimerization and stability, potentially influencing Alzheimer's disease.
- O-GlcNAc modification may serve as an alternative to phosphorylation in cellular signaling pathways.