A transcriptionally [correction of transcriptively] active complex of APP with Fe65 and histone acetyltransferase Tip60
- Science. 2001 Jul 6;293(5527):115-20. doi: 10.1126/science.1058783.
Affiliations
- 1. 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.
PMID: 11441186
DOI: 10.1126/science.1058783
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.