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Science 6 July 2001:
Vol. 293. no. 5527, pp. 115 - 120
DOI: 10.1126/science.1058783
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Reports

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

Xinwei Cao, Thomas C. Südhof*

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.

The Center for Basic Neuroscience, Department of Molecular Genetics, and Howard Hughes Medical Institute, The University of Texas Southwestern Medical Center, Dallas, TX 75390-9111 USA.
*   To whom correspondence should be addressed. E-mail: Thomas.Sudhof{at}UTSouthwestern.edu

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