A transcriptively active complex of APP with Fe65 and histone acetyltransferase Tip60

被引：1011

作者：

Cao, XW

Südhof, TC

机构：

[1] Univ Texas, SW Med Ctr, Ctr Basic Neurosci, Dept Mol Genet, Dallas, TX 75390 USA

[2] Univ Texas, SW Med Ctr, Howard Hughes Med Inst, Dallas, TX 75390 USA

来源：

SCIENCE | 2001年 / 293卷 / 5527期

关键词：

D O I：

10.1126/science.1058783

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 [理学]; 0710 [生物学]; 09 [农学];

摘要：

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.

引用

页码：115 / 120

页数：6

共 38 条

[1]

It all sticks together - the APP-related family of proteins and Alzheimer's disease [J].