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

Science  06 Jul 2001:
Vol. 293, Issue 5527, pp. 115-120
DOI: 10.1126/science.1058783

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Abstract

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.

  • * To whom correspondence should be addressed. E-mail: Thomas.Sudhof{at}UTSouthwestern.edu

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