A Transcriptively Active Complex of APP with Fe65 and Histone Acetyltransferase Tip60

Amyloid-β precursor protein (APP), a widely expressed cell-surface protein, is cleaved in the transmembrane region by γ-secretase. γ-Cleavage of APP produces the extracellular amyloid β-peptide of Alzheimer's disease and releases an intracellular tail fragment of unknown physiological function....

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 2001-07, Vol.293 (5527), p.115-120
Main Authors: Cao, Xinwei, Südhof, Thomas C.
Format: Article
Language:English
Subjects:
Alzheimer's disease
Alzheimers Disease
Amyloid beta-protein
Analysis
Biological and medical sciences
Cell lines
COS cells
DNA
Fe65 protein
Fundamental and applied biological sciences. Psychology
Gene expression
Genes
HEK293 cells
HeLa cells
Histones
Molecular and cellular biology
Molecular genetics
Neurobiology
Neurological research
Peptides
Plasmids
Proteins
Tip60 protein
Transactivation
Transfection
Yeasts
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Summary:Amyloid-β precursor protein (APP), a widely expressed cell-surface protein, is cleaved in the transmembrane region by γ-secretase. γ-Cleavage of APP produces the extracellular amyloid β-peptide of Alzheimer's disease and releases an intracellular tail fragment of unknown physiological function. We now demonstrate that the cytoplasmic tail of APP forms a multimeric complex with the nuclear adaptor protein Fe65 and the histone acetyltransferase Tip60. This complex potently stimulates transcription via heterologous Gal4- or LexA-DNA binding domains, suggesting that release of the cytoplasmic tail of APP by γ-cleavage may function in gene expression.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.1058783