A transcriptionally [correction of transcriptively] active complex of APP with Fe65 and histone acetyltransferase Tip60
- PMID: 11441186
- DOI: 10.1126/science.1058783
A transcriptionally [correction of transcriptively] active complex of APP with Fe65 and histone acetyltransferase Tip60
Erratum in
- Science 2001 Aug 24;293(5534):1436
Abstract
Amyloid-beta precursor protein (APP), a widely expressed cell-surface protein, is cleaved in the transmembrane region by gamma-secretase. gamma-Cleavage of APP produces the extracellular amyloid beta-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 gamma-cleavage may function in gene expression.
Comment in
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Neuroscience. Elusive protein auditions for several new roles.Science. 2001 Jul 6;293(5527):28-9. doi: 10.1126/science.293.5527.28. Science. 2001. PMID: 11441156 No abstract available.
Comment on
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A neural correlate of working memory in the monkey primary visual cortex.Science. 2001 Jul 6;293(5527):120-4. doi: 10.1126/science.1060496. Science. 2001. PMID: 11441187
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