Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.
Johnson & Johnson

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 6 July 2001:
Vol. 293. no. 5527, pp. 115 - 120
DOI: 10.1126/science.1058783
Prev | Table of Contents | Next

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

Read the Full Text

ADVERTISEMENT
Click Me!

ADVERTISEMENT
Click Me!

To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)